CS13A_LISSS
ID CS13A_LISSS Reviewed; 1120 AA.
AC P0DPB8;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28111461};
DE EC=3.1.-.- {ECO:0000269|PubMed:27669025};
DE AltName: Full=CRISPR-associated endoribonuclease C2c2 {ECO:0000303|PubMed:26593719};
DE Short=EndoRNase;
DE AltName: Full=LseC2c2 {ECO:0000303|PubMed:27669025};
GN Name=cas13 {ECO:0000303|PubMed:28111461};
GN Synonyms=c2c2 {ECO:0000303|PubMed:26593719}; OrderedLocusNames=lse_1149;
OS Listeria seeligeri serovar 1/2b (strain ATCC 35967 / DSM 20751 / CCM 3970 /
OS CIP 100100 / NCTC 11856 / SLCC 3954 / 1120).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=683837;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35967 / DSM 20751 / CCM 3970 / CIP 100100 / NCTC 11856 / SLCC
RC 3954 / 1120;
RX PubMed=20061480; DOI=10.1128/jb.01415-09;
RA Steinweg C., Kuenne C.T., Billion A., Mraheil M.A., Domann E., Ghai R.,
RA Barbuddhe S.B., Karst U., Goesmann A., Puhler A., Weisshaar B., Wehland J.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T., Hain T.;
RT "Complete genome sequence of Listeria seeligeri, a nonpathogenic member of
RT the genus Listeria.";
RL J. Bacteriol. 192:1473-1474(2010).
RN [2]
RP IDENTIFICATION, AND DOMAIN.
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 [3]
RP FUNCTION IN CRRNA PROCESSING, AND FUNCTION AS AN ENDORIBONUCLEASE.
RC STRAIN=ATCC 35967 / DSM 20751 / CCM 3970 / CIP 100100 / NCTC 11856 / SLCC
RC 3954 / 1120;
RX PubMed=27669025; DOI=10.1038/nature19802;
RA East-Seletsky A., O'Connell M.R., Knight S.C., Burstein D., Cate J.H.,
RA Tjian R., Doudna J.A.;
RT "Two distinct RNase activities of CRISPR-C2c2 enable guide-RNA processing
RT and RNA detection.";
RL Nature 538:270-273(2016).
RN [4]
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 [5]
RP DISCUSSION OF SEQUENCE.
RX PubMed=28475872; DOI=10.1016/j.molcel.2017.04.008;
RA East-Seletsky A., O'Connell M.R., Burstein D., Knott G.J., Doudna J.A.;
RT "RNA targeting by functionally orthogonal type VI-A CRISPR-Cas enzymes.";
RL Mol. Cell 66:373-383(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. Unlike
CC many single-component effectors, this CRISPR-Cas system targets RNA (By
CC similarity). CRISPR clusters are transcribed from pre-CRISPR RNA
CC (crRNA) and processed into crRNA by this protein (PubMed:27669025).
CC {ECO:0000250|UniProtKB:P0DOC6, ECO:0000269|PubMed:27669025}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:C7NBY4};
CC Note=Pre-crRNA processing is metal independent, while crRNA-guided
CC target RNA cleavage is dependent on divalent metal.
CC {ECO:0000250|UniProtKB:C7NBY4};
CC -!- DOMAIN: The target ssRNase active sites are probably within the 2 HEPN-
CC like folds, and the 2 folds interact in vivo (PubMed:26593719).
CC {ECO:0000250|UniProtKB:C7NBY4, ECO:0000305|PubMed:26593719}.
CC -!- MISCELLANEOUS: Part of a type VI uridine-prefering CRISPR-Cas system.
CC {ECO:0000305|PubMed:26593719, ECO:0000305|PubMed:28475872}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas13a
CC family. {ECO:0000305}.
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DR EMBL; FN557490; CBH27300.1; -; Genomic_DNA.
DR RefSeq; WP_012985477.1; NC_013891.1.
DR PDB; 6VRB; EM; 3.00 A; A=34-1120.
DR PDB; 6VRC; EM; 3.20 A; A=1-1120.
DR PDBsum; 6VRB; -.
DR PDBsum; 6VRC; -.
DR AlphaFoldDB; P0DPB8; -.
DR SMR; P0DPB8; -.
DR GeneID; 32489497; -.
DR KEGG; lsg:lse_1149; -.
DR HOGENOM; CLU_280435_0_0_9; -.
DR OrthoDB; 1059045at2; -.
DR GO; GO:0004519; F:endonuclease 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.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease; Repeat;
KW RNA-binding.
FT CHAIN 1..1120
FT /note="CRISPR-associated endoribonuclease Cas13a"
FT /id="PRO_0000442270"
FT REGION 354..496
FT /note="HEPN-like fold 1"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4,
FT ECO:0000305|PubMed:26593719"
FT REGION 908..1120
FT /note="HEPN-like fold 2"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4,
FT ECO:0000305|PubMed:26593719"
FT ACT_SITE 445
FT /evidence="ECO:0000250|UniProtKB:P0DOC6,
FT ECO:0000305|PubMed:26593719"
FT ACT_SITE 450
FT /evidence="ECO:0000250|UniProtKB:P0DOC6,
FT ECO:0000305|PubMed:26593719"
FT ACT_SITE 1016
FT /evidence="ECO:0000250|UniProtKB:P0DOC6,
FT ECO:0000305|PubMed:26593719"
FT ACT_SITE 1021
FT /evidence="ECO:0000250|UniProtKB:P0DOC6,
FT ECO:0000305|PubMed:26593719"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6VRC"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 180..202
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 240..247
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6VRC"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 323..341
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 356..387
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 428..432
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 433..449
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 502..512
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 513..518
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:6VRC"
FT HELIX 548..559
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:6VRC"
FT HELIX 584..598
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 608..622
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 644..657
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 661..664
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 670..689
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 693..696
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 724..728
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 733..747
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 759..770
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 787..794
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 795..797
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 809..812
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 820..822
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 831..838
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:6VRC"
FT HELIX 848..852
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 855..857
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 860..875
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 877..881
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 883..906
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 907..909
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 910..945
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 995..1002
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 1003..1006
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1010..1020
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 1021..1024
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 1025..1027
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1034..1043
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1044..1046
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1048..1052
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1054..1064
FT /evidence="ECO:0007829|PDB:6VRB"
FT TURN 1074..1078
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 1094..1097
FT /evidence="ECO:0007829|PDB:6VRB"
FT STRAND 1103..1105
FT /evidence="ECO:0007829|PDB:6VRB"
FT HELIX 1107..1117
FT /evidence="ECO:0007829|PDB:6VRB"
SQ SEQUENCE 1120 AA; 132264 MW; E6011368BA0B9ACB CRC64;
MWISIKTLIH HLGVLFFCDY MYNRREKKII EVKTMRITKV EVDRKKVLIS RDKNGGKLVY
ENEMQDNTEQ IMHHKKSSFY KSVVNKTICR PEQKQMKKLV HGLLQENSQE KIKVSDVTKL
NISNFLNHRF KKSLYYFPEN SPDKSEEYRI EINLSQLLED SLKKQQGTFI CWESFSKDME
LYINWAENYI SSKTKLIKKS IRNNRIQSTE SRSGQLMDRY MKDILNKNKP FDIQSVSEKY
QLEKLTSALK ATFKEAKKND KEINYKLKST LQNHERQIIE ELKENSELNQ FNIEIRKHLE
TYFPIKKTNR KVGDIRNLEI GEIQKIVNHR LKNKIVQRIL QEGKLASYEI ESTVNSNSLQ
KIKIEEAFAL KFINACLFAS NNLRNMVYPV CKKDILMIGE FKNSFKEIKH KKFIRQWSQF
FSQEITVDDI ELASWGLRGA IAPIRNEIIH LKKHSWKKFF NNPTFKVKKS KIINGKTKDV
TSEFLYKETL FKDYFYSELD SVPELIINKM ESSKILDYYS SDQLNQVFTI PNFELSLLTS
AVPFAPSFKR VYLKGFDYQN QDEAQPDYNL KLNIYNEKAF NSEAFQAQYS LFKMVYYQVF
LPQFTTNNDL FKSSVDFILT LNKERKGYAK AFQDIRKMNK DEKPSEYMSY IQSQLMLYQK
KQEEKEKINH FEKFINQVFI KGFNSFIEKN RLTYICHPTK NTVPENDNIE IPFHTDMDDS
NIAFWLMCKL LDAKQLSELR NEMIKFSCSL QSTEEISTFT KAREVIGLAL LNGEKGCNDW
KELFDDKEAW KKNMSLYVSE ELLQSLPYTQ EDGQTPVINR SIDLVKKYGT ETILEKLFSS
SDDYKVSAKD IAKLHEYDVT EKIAQQESLH KQWIEKPGLA RDSAWTKKYQ NVINDISNYQ
WAKTKVELTQ VRHLHQLTID LLSRLAGYMS IADRDFQFSS NYILERENSE YRVTSWILLS
ENKNKNKYND YELYNLKNAS IKVSSKNDPQ LKVDLKQLRL TLEYLELFDN RLKEKRNNIS
HFNYLNGQLG NSILELFDDA RDVLSYDRKL KNAVSKSLKE ILSSHGMEVT FKPLYQTNHH
LKIDKLQPKK IHHLGEKSTV SSNQVSNEYC QLVRTLLTMK
