CS12A_ACISB
ID CS12A_ACISB Reviewed; 1307 AA.
AC U2UMQ6;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=CRISPR-associated endonuclease Cas12a {ECO:0000303|PubMed:28111461};
DE EC=3.1.21.1 {ECO:0000250|UniProtKB:A0Q7Q2};
DE EC=4.6.1.22 {ECO:0000250|UniProtKB:A0Q7Q2};
DE AltName: Full=AsCpf1 {ECO:0000303|PubMed:26422227};
DE AltName: Full=CRISPR-associated endonuclease Cpf1 {ECO:0000303|PubMed:26422227};
GN Name=cas12a {ECO:0000303|PubMed:28111461};
GN Synonyms=cpf1 {ECO:0000303|PubMed:26422227}; ORFNames=HMPREF1246_0236;
OS Acidaminococcus sp. (strain BV3L6).
OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus; unclassified Acidaminococcus.
OX NCBI_TaxID=1111120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3L6;
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, AND BIOTECHNOLOGY.
RC STRAIN=BV3L6;
RX PubMed=26422227; DOI=10.1016/j.cell.2015.09.038;
RA Zetsche B., Gootenberg J.S., Abudayyeh O.O., Slaymaker I.M., Makarova K.S.,
RA Essletzbichler P., Volz S.E., Joung J., van der Oost J., Regev A.,
RA Koonin E.V., Zhang F.;
RT "Cpf1 is a single RNA-guided endonuclease of a class 2 CRISPR-Cas system.";
RL Cell 163:759-771(2015).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=26593719; DOI=10.1016/j.molcel.2015.10.008;
RA Shmakov S., Abudayyeh O.O., Makarova K.S., Wolf Y.I., Gootenberg J.S.,
RA Semenova E., Minakhin L., Joung J., Konermann S., Severinov K., Zhang F.,
RA Koonin E.V.;
RT "Discovery and functional characterization of diverse class 2 CRISPR-Cas
RT systems.";
RL Mol. Cell 60:385-397(2015).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=27347757; DOI=10.1038/nbt.3620;
RA Kleinstiver B.P., Tsai S.Q., Prew M.S., Nguyen N.T., Welch M.M.,
RA Lopez J.M., McCaw Z.R., Aryee M.J., Joung J.K.;
RT "Genome-wide specificities of CRISPR-Cas Cpf1 nucleases in human cells.";
RL Nat. Biotechnol. 34:869-874(2016).
RN [5]
RP NOMENCLATURE.
RX PubMed=28111461; DOI=10.1038/nrmicro.2016.184;
RA Shmakov S., Smargon A., Scott D., Cox D., Pyzocha N., Yan W.,
RA Abudayyeh O.O., Gootenberg J.S., Makarova K.S., Wolf Y.I., Severinov K.,
RA Zhang F., Koonin E.V.;
RT "Diversity and evolution of class 2 CRISPR-Cas systems.";
RL Nat. Rev. Microbiol. 15:169-182(2017).
RN [6] {ECO:0007744|PDB:5B43}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GUIDE RNA AND TARGET
RP DNA, FUNCTION, ACTIVE SITE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF THR-167;
RP ARG-176; ARG-192; TRP-382; LYS-548; MET-604; LYS-607; LYS-780; GLY-783;
RP ASP-908; ARG-951; ARG-955; TRP-958; GLU-993; ARG-1226; SER-1228; ASP-1235
RP AND ASP-1263.
RX PubMed=27114038; DOI=10.1016/j.cell.2016.04.003;
RA Yamano T., Nishimasu H., Zetsche B., Hirano H., Slaymaker I.M., Li Y.,
RA Fedorova I., Nakane T., Makarova K.S., Koonin E.V., Ishitani R., Zhang F.,
RA Nureki O.;
RT "Crystal structure of Cpf1 in complex with guide RNA and target DNA.";
RL Cell 165:949-962(2016).
RN [7] {ECO:0007744|PDB:5KK5}
RP X-RAY CRYSTALLOGRAPHY (3.29 ANGSTROMS) IN COMPLEX WITH CRRNA AND TARGET
RP DNA, SUBUNIT, DOMAIN, DNA-BINDING, AND RNA-BINDING.
RX PubMed=27444870; DOI=10.1038/cr.2016.88;
RA Gao P., Yang H., Rajashankar K.R., Huang Z., Patel D.J.;
RT "Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-
RT mediated target DNA recognition.";
RL Cell Res. 26:901-913(2016).
RN [8] {ECO:0007744|PDB:5XH6, ECO:0007744|PDB:5XH7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT PROTEIN ABLE TO RECOGNIZE
RP ALTERED PAM, AND BIOTECHNOLOGY.
RX PubMed=28595896; DOI=10.1016/j.molcel.2017.04.019;
RA Nishimasu H., Yamano T., Gao L., Zhang F., Ishitani R., Nureki O.;
RT "Structural basis for the altered PAM recognition by engineered CRISPR-
RT Cpf1.";
RL Mol. Cell 67:139-147(2017).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA).
CC Recognizes a short motif in the CRISPR repeat sequences (the 5' PAM or
CC protospacer adjacent motif, TTTN in this organism) to help distinguish
CC self versus nonself, as targets within the bacterial CRISPR locus do
CC not have PAMs (PubMed:26422227). Has dsDNA endonuclease activity,
CC results in staggered 4-base 5' overhangs 19 and 22 bases downstream of
CC the PAM on the non-targeted and targeted strand respectively
CC (PubMed:26422227). Non-target strand cleavage by the RuvC domain is
CC probably a prerequisite of target strand cleavage by the Nuc domain
CC (PubMed:27114038). In this CRISPR system correct processing of pre-
CC crRNA requires only this protein and the CRISPR locus (By similarity).
CC {ECO:0000250|UniProtKB:A0Q7Q2, ECO:0000269|PubMed:26422227,
CC ECO:0000269|PubMed:27114038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-
CC phosphooligonucleotide end-products.; EC=3.1.21.1;
CC Evidence={ECO:0000250|UniProtKB:A0Q7Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA = a 5'-hydroxy-ribonucleotide + n nucleoside-2',3'-
CC cyclophosphates.; EC=4.6.1.22;
CC Evidence={ECO:0000250|UniProtKB:A0Q7Q2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0Q7Q2};
CC -!- SUBUNIT: Monomer (PubMed:27114038). {ECO:0000269|PubMed:27114038,
CC ECO:0000269|PubMed:27444870}.
CC -!- DOMAIN: Has a bilobed structure, with the REC lobe (residues 35-526)
CC connected to the NUC lobe (residues 1-35 and 526-1307) by a
CC discontinuous wedge domain (PubMed:27114038, PubMed:27444870). The
CC crRNA-target DNA heteroduplex is bound in the channel between the 2
CC lobes (PubMed:27114038, PubMed:27444870). One nuclease site is found in
CC the discontinuous RuvC domain which probably cuts target DNA strand in
CC the crRNA-DNA heteroduplex (residues 884-940, 957-1066 and 1262-1307),
CC the other in the NUC domain and probably cuts the non-target DNA strand
CC outside the heteroduplex (residues 1067-1261) (PubMed:27114038). Target
CC DNA binding induces domain movement (PubMed:27444870).
CC {ECO:0000269|PubMed:27114038, ECO:0000269|PubMed:27444870}.
CC -!- BIOTECHNOLOGY: This class of CRISPR enzymes recognize a 5' T-rich
CC protospacer adjacent motif (PAM, TTTN for this specific enzyme), unlike
CC Cas9 enzymes which recognize 3' G-rich PAMs, thus this enzyme increases
CC the possibilites for genome editing (PubMed:26422227). When
CC appropriately expressed in a human cell line mediates human genome
CC editing via indel formation; its T-rich PAM sequence may make it useful
CC for engineering of AT-rich genomes or of regions such as scaffold-
CC matrix attachment areas (PubMed:26422227, PubMed:27347757). It has also
CC been engineered to recognize altered PAM sequences, which will enlarge
CC its target scope (PubMed:28595896). {ECO:0000269|PubMed:26422227,
CC ECO:0000269|PubMed:27347757, ECO:0000269|PubMed:28595896}.
CC -!- MISCELLANEOUS: Part of a type V-A CRISPR-Cas system.
CC {ECO:0000305|PubMed:26593719, ECO:0000305|PubMed:28111461}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas12a
CC family. {ECO:0000305|PubMed:28111461}.
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DR EMBL; AWUR01000016; ERL19323.1; -; Genomic_DNA.
DR RefSeq; WP_021736722.1; NZ_AWUR01000016.1.
DR PDB; 5B43; X-ray; 2.80 A; A=1-1307.
DR PDB; 5KK5; X-ray; 3.29 A; A=1-1307.
DR PDB; 5XH6; X-ray; 2.00 A; A=1-1307.
DR PDB; 5XH7; X-ray; 2.00 A; A=1-1307.
DR PDBsum; 5B43; -.
DR PDBsum; 5KK5; -.
DR PDBsum; 5XH6; -.
DR PDBsum; 5XH7; -.
DR AlphaFoldDB; U2UMQ6; -.
DR SMR; U2UMQ6; -.
DR PATRIC; fig|1111120.3.peg.776; -.
DR GO; GO:0033898; F:Bacillus subtilis ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR InterPro; IPR027620; Cas12a.
DR InterPro; IPR040882; Cas12a_NUC.
DR InterPro; IPR040787; Cas12a_REC1.
DR InterPro; IPR040852; RuvC_1.
DR Pfam; PF18510; NUC; 1.
DR Pfam; PF18501; REC1; 1.
DR Pfam; PF18516; RuvC_1; 1.
DR TIGRFAMs; TIGR04330; cas_Cpf1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Coiled coil; DNA-binding; Endonuclease;
KW Hydrolase; Lyase; Magnesium; Nuclease; RNA-binding.
FT CHAIN 1..1307
FT /note="CRISPR-associated endonuclease Cas12a"
FT /id="PRO_0000434903"
FT DNA_BIND 599..607
FT /note="PAM-binding on target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT DNA_BIND 780..783
FT /note="Target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT DNA_BIND 951..968
FT /note="Target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT DNA_BIND 1051..1053
FT /note="Target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT REGION 1..35
FT /note="WED-I (OBD-I)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 36..320
FT /note="REC1 (helical-I)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 321..526
FT /note="WED-II (helical-II)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 527..598
FT /note="WED-II (OBD-I)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 599..718
FT /note="PI (LHD)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 719..884
FT /note="WED-III (OBD-III)"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 885..940
FT /note="RuvC-I"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 941..957
FT /note="Bridge helix"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 958..1066
FT /note="RuvC-II"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 1067..1262
FT /note="Nuclease domain"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT REGION 1263..1307
FT /note="RuvC-III"
FT /evidence="ECO:0000303|PubMed:27114038,
FT ECO:0000303|PubMed:27444870"
FT COILED 74..106
FT /evidence="ECO:0000255"
FT ACT_SITE 800
FT /note="For pre-crRNA processing"
FT /evidence="ECO:0000250|UniProtKB:A0Q7Q2"
FT ACT_SITE 809
FT /note="For pre-crRNA processing"
FT /evidence="ECO:0000250|UniProtKB:A0Q7Q2"
FT ACT_SITE 860
FT /note="For pre-crRNA processing"
FT /evidence="ECO:0000250|UniProtKB:A0Q7Q2"
FT ACT_SITE 908
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000269|PubMed:27114038"
FT ACT_SITE 993
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000269|PubMed:27114038"
FT ACT_SITE 1226
FT /note="For DNase activity of nuclease domain"
FT /evidence="ECO:0000269|PubMed:27114038"
FT ACT_SITE 1263
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000269|PubMed:27114038"
FT BINDING 47..51
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT BINDING 175..176
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT BINDING 307..310
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT BINDING 752..761
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT BINDING 806..808
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:27114038"
FT SITE 18
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 167
FT /note="Binds PAM on target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 192
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 382
FT /note="Binds crRNA-target DNA heteroduplex"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 548
FT /note="Binds PAM on target DNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 607
FT /note="Binds sequence-specific recognition of both target
FT and non-target strand bases in PAM"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 872
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:27114038,
FT ECO:0000269|PubMed:27444870"
FT SITE 1014
FT /note="Binds target DNA"
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 167
FT /note="T->A: Wild-type to slightly improved guided indel
FT formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 176
FT /note="R->A: Decreased guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 192
FT /note="R->A: Decreased guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 382
FT /note="W->A: Nearly complete loss of guided indel
FT formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 548
FT /note="K->A: Decreased guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 604
FT /note="M->A: Decreased guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 607
FT /note="K->A: Nearly complete loss of guided indel
FT formation, probable loss of PAM recognition."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 780
FT /note="K->A: Nearly complete loss of guided indel
FT formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 783
FT /note="G->P: Complete loss of guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 908
FT /note="D->P: Complete loss of guided indel formation;
FT neither DNA strand is cleaved in vitro."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 951
FT /note="R->A: Nearly complete loss of guided indel
FT formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 955
FT /note="R->A: Partial loss of guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 958
FT /note="W->A: Partial loss of guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 993
FT /note="E->P: Complete loss of guided indel formation;
FT neither DNA strand is cleaved in vitro."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 1226
FT /note="R->A: Nearly complete loss of guided indel
FT formation; nickase cleaves only the non-target DNA strand
FT in vitro."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 1228
FT /note="S->A: Wild-type to slightly improved guided indel
FT formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 1235
FT /note="D->A: About half loss of guided indel formation."
FT /evidence="ECO:0000269|PubMed:27114038"
FT MUTAGEN 1263
FT /note="D->A: Nearly complete loss of guided indel
FT formation; neither DNA strand is cleaved in vitro."
FT /evidence="ECO:0000269|PubMed:27114038"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 13..23
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 36..68
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 89..111
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5KK5"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 197..214
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 326..342
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 429..451
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 461..481
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 494..507
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:5XH7"
FT TURN 538..541
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 587..597
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:5KK5"
FT HELIX 657..663
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 666..686
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 688..692
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 707..714
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 719..727
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 728..736
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:5B43"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:5KK5"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 771..775
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 778..781
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 786..790
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 812..817
FT /evidence="ECO:0007829|PDB:5B43"
FT HELIX 820..830
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 840..845
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 862..864
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 868..878
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 879..884
FT /evidence="ECO:0007829|PDB:5KK5"
FT HELIX 888..898
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 904..908
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 911..914
FT /evidence="ECO:0007829|PDB:5KK5"
FT STRAND 916..920
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 926..931
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 933..935
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 940..956
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 965..986
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 989..993
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1011..1024
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:5KK5"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1062..1065
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1070..1073
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1085..1087
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1091..1099
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1101..1106
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 1108..1110
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1113..1118
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1123..1125
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1134..1140
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1145..1147
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1159..1161
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1174..1176
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1178..1188
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1200..1206
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1209..1223
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1226..1229
FT /evidence="ECO:0007829|PDB:5XH6"
FT TURN 1230..1233
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1234..1242
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1248..1250
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1251..1253
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1262..1283
FT /evidence="ECO:0007829|PDB:5XH6"
FT STRAND 1284..1287
FT /evidence="ECO:0007829|PDB:5XH6"
FT HELIX 1295..1306
FT /evidence="ECO:0007829|PDB:5XH6"
SQ SEQUENCE 1307 AA; 151207 MW; CD5A76A624FEC1A8 CRC64;
MTQFEGFTNL YQVSKTLRFE LIPQGKTLKH IQEQGFIEED KARNDHYKEL KPIIDRIYKT
YADQCLQLVQ LDWENLSAAI DSYRKEKTEE TRNALIEEQA TYRNAIHDYF IGRTDNLTDA
INKRHAEIYK GLFKAELFNG KVLKQLGTVT TTEHENALLR SFDKFTTYFS GFYENRKNVF
SAEDISTAIP HRIVQDNFPK FKENCHIFTR LITAVPSLRE HFENVKKAIG IFVSTSIEEV
FSFPFYNQLL TQTQIDLYNQ LLGGISREAG TEKIKGLNEV LNLAIQKNDE TAHIIASLPH
RFIPLFKQIL SDRNTLSFIL EEFKSDEEVI QSFCKYKTLL RNENVLETAE ALFNELNSID
LTHIFISHKK LETISSALCD HWDTLRNALY ERRISELTGK ITKSAKEKVQ RSLKHEDINL
QEIISAAGKE LSEAFKQKTS EILSHAHAAL DQPLPTTLKK QEEKEILKSQ LDSLLGLYHL
LDWFAVDESN EVDPEFSARL TGIKLEMEPS LSFYNKARNY ATKKPYSVEK FKLNFQMPTL
ASGWDVNKEK NNGAILFVKN GLYYLGIMPK QKGRYKALSF EPTEKTSEGF DKMYYDYFPD
AAKMIPKCST QLKAVTAHFQ THTTPILLSN NFIEPLEITK EIYDLNNPEK EPKKFQTAYA
KKTGDQKGYR EALCKWIDFT RDFLSKYTKT TSIDLSSLRP SSQYKDLGEY YAELNPLLYH
ISFQRIAEKE IMDAVETGKL YLFQIYNKDF AKGHHGKPNL HTLYWTGLFS PENLAKTSIK
LNGQAELFYR PKSRMKRMAH RLGEKMLNKK LKDQKTPIPD TLYQELYDYV NHRLSHDLSD
EARALLPNVI TKEVSHEIIK DRRFTSDKFF FHVPITLNYQ AANSPSKFNQ RVNAYLKEHP
ETPIIGIDRG ERNLIYITVI DSTGKILEQR SLNTIQQFDY QKKLDNREKE RVAARQAWSV
VGTIKDLKQG YLSQVIHEIV DLMIHYQAVV VLENLNFGFK SKRTGIAEKA VYQQFEKMLI
DKLNCLVLKD YPAEKVGGVL NPYQLTDQFT SFAKMGTQSG FLFYVPAPYT SKIDPLTGFV
DPFVWKTIKN HESRKHFLEG FDFLHYDVKT GDFILHFKMN RNLSFQRGLP GFMPAWDIVF
EKNETQFDAK GTPFIAGKRI VPVIENHRFT GRYRDLYPAN ELIALLEEKG IVFRDGSNIL
PKLLENDDSH AIDTMVALIR SVLQMRNSNA ATGEDYINSP VRDLNGVCFD SRFQNPEWPM
DADANGAYHI ALKGQLLLNH LKESKDLKLQ NGISNQDWLA YIQELRN
