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ACDA1_METBF
ID   ACDA1_METBF             Reviewed;         806 AA.
AC   Q46G04;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            EC=1.2.7.4 {ECO:0000255|HAMAP-Rule:MF_01137};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   OrderedLocusNames=Mbar_A0204 {ECO:0000312|EMBL:AAZ69188.1};
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
RP   INDUCTION, AND PATHWAY.
RC   STRAIN=MS;
RX   PubMed=6425262; DOI=10.1128/jb.158.1.231-237.1984;
RA   Krzycki J.A., Zeikus J.G.;
RT   "Characterization and purification of carbon monoxide dehydrogenase from
RT   Methanosarcina barkeri.";
RL   J. Bacteriol. 158:231-237(1984).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS EPSILON
RP   SUBUNIT; IRON-SULFUR (4FE-4S); NICKEL-IRON-SULFUR (NI-4FE-4S) AND CARBON
RP   MONOXIDE, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=18621675; DOI=10.1073/pnas.0800415105;
RA   Gong W., Hao B., Wei Z., Ferguson D.J., Tallant T., Krzycki J.A.,
RA   Chan M.K.;
RT   "Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of
RT   the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9558-9563(2008).
CC   -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC       cleavage of acetyl-CoA, allowing growth on acetate as sole source of
CC       carbon and energy. The alpha-epsilon subcomponent functions as a carbon
CC       monoxide dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137,
CC       ECO:0000269|PubMed:6425262}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2
CC         reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC         ECO:0000269|PubMed:18621675};
CC       Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC   -!- COFACTOR:
CC       Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC         ECO:0000269|PubMed:18621675};
CC       Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC   -!- ACTIVITY REGULATION: Carbon monoxide dehydrogenase activity is
CC       inhibited by KCN and is rapidly inactivated by O(2).
CC       {ECO:0000269|PubMed:6425262}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 mM for CO (at 37 degrees Celsius) {ECO:0000269|PubMed:6425262};
CC         Vmax=1300 umol/min/mg enzyme for CO dehydrogenase activity using
CC         methyl viologen as electron acceptor (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:6425262};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:6425262}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits
CC       (PubMed:6425262). The ACDS complex is made up of alpha, epsilon, beta,
CC       gamma and delta subunits with a probable stoichiometry of
CC       (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:6425262,
CC       ECO:0000305|PubMed:18621675}.
CC   -!- INDUCTION: Up-regulated during growth on acetate.
CC       {ECO:0000269|PubMed:6425262}.
CC   -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster
CC       C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation.
CC       Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges
CC       the two subunits of the CODH dimer. Contains two additional 4Fe-4S
CC       clusters, dubbed E and F, that probably transport electrons from
CC       ferredoxin to the B cluster. {ECO:0000255|HAMAP-Rule:MF_01137,
CC       ECO:0000305|PubMed:18621675}.
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01137}.
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DR   EMBL; CP000099; AAZ69188.1; -; Genomic_DNA.
DR   RefSeq; WP_011305243.1; NC_007355.1.
DR   PDB; 3CF4; X-ray; 2.00 A; A=1-806.
DR   PDBsum; 3CF4; -.
DR   AlphaFoldDB; Q46G04; -.
DR   SMR; Q46G04; -.
DR   STRING; 269797.Mbar_A0204; -.
DR   EnsemblBacteria; AAZ69188; AAZ69188; Mbar_A0204.
DR   GeneID; 3626295; -.
DR   KEGG; mba:Mbar_A0204; -.
DR   eggNOG; arCOG02428; Archaea.
DR   HOGENOM; CLU_361186_0_0_2; -.
DR   OMA; LCIGHNV; -.
DR   OrthoDB; 1404at2157; -.
DR   UniPathway; UPA00642; -.
DR   EvolutionaryTrace; Q46G04; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR   CDD; cd01916; ACS_1; 1.
DR   Gene3D; 3.40.50.2030; -; 2.
DR   HAMAP; MF_01137; CdhA; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004460; CDHA.
DR   InterPro; IPR004137; HCP/CODH.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF03063; Prismane; 2.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00314; cdhA; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW   Nickel; Oxidoreductase; Repeat.
FT   CHAIN           1..806
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   alpha 1"
FT                   /id="PRO_0000436851"
FT   DOMAIN          407..436
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   DOMAIN          446..475
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         84
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         94
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         117
FT                   /ligand="CO"
FT                   /ligand_id="ChEBI:CHEBI:17245"
FT                   /evidence="ECO:0000269|PubMed:18621675"
FT   BINDING         250
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000269|PubMed:18621675"
FT   BINDING         278
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000269|PubMed:18621675"
FT   BINDING         323
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   BINDING         417
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         420
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         423
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         427
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         455
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         458
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         461
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         465
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675, ECO:0007744|PDB:3CF4"
FT   BINDING         523
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   BINDING         552
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   BINDING         587
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137,
FT                   ECO:0000269|PubMed:18621675"
FT   TURN            50..57
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           98..132
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           148..154
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           165..180
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           190..218
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           253..264
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          271..277
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           278..283
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   TURN            284..287
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          296..301
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           305..311
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          315..319
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           328..334
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           358..366
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          369..374
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           378..398
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           407..416
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           422..426
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           433..441
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           446..454
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           460..464
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           471..478
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           480..484
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          488..491
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           499..511
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          517..520
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           532..542
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          546..550
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           551..557
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           568..571
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          575..577
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          581..586
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           587..590
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           591..603
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           613..623
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          626..630
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           636..647
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          652..654
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           656..661
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          662..666
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           672..674
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          675..679
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   TURN            680..682
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          685..687
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          692..698
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           702..712
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           720..737
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           745..748
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           752..754
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           760..771
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          774..776
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   TURN            777..780
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          781..784
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   STRAND          796..798
FT                   /evidence="ECO:0007829|PDB:3CF4"
FT   HELIX           800..802
FT                   /evidence="ECO:0007829|PDB:3CF4"
SQ   SEQUENCE   806 AA;  88775 MW;  25620ACDA618E9CA CRC64;
     MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELV NAGPTLFAGL ESYRDDWNFK
     LLDRYEPVIT PMCDQCCYCT YGPCDLSGNK RGACGIDMLG HNGREFFLRV ITGTACHAAH
     GRHLLDHLIE TFGEDLPLNL GQSNVLTPNI TISTGLSPKT LGEVKPAMEY VEEQLTQLLA
     TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDIVQVTAYD FPRADPEAPL IEIGMGTIDK
     SKPFLCVIGH NVAGVTYMMD YMEDHDLTDK MEIAGLCCTA IDLTRYKEAD RRPPYAKVIG
     SMSKELKVIR SGMPDVIVVD EQCVRGDIVP EAQKLMIPVI ASNPKIMYGL PNRTDADVDE
     TIEELRSGKI PGCVMLDYDK LGEICIRLTM EMAPIRDASG ITAIPTDEEF TNWVMKCADC
     GACMIACPEE LDIPEAMGFA KEGDYSYLDI LHDQCIGCRR CEQVCKKEIP ILNIIEKAAQ
     KQISEEKGLM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYPEGT KDVYYIAEEF
     LKRNFIVVTT GCGAMDIGMF KDEDGKTLYE RFPGGFECGG LANIGSCVSN AHITGAAEKV
     AAIFAQRTLE GNLAEIGDYV LNRVGACGLA WGAFSQKASS IGTGCNILGI PAVLGPHSSK
     YRRALIAKNY EEDKWKVYDA RNGQEMAIPP APEFLLTTAE TWQEAIPMMA KACIRPSDNN
     MGRSIKLTHW MELHKKYLGS KPEDWWKFVR NEADLPLATR EALLKELEKE HGWEIDWKRK
     KVISGPKIKF DVSAQPTNLK RLCKEA
 
 
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