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COPA_ARCFU
ID   COPA_ARCFU              Reviewed;         804 AA.
AC   O29777;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Probable copper-exporting P-type ATPase;
DE            EC=7.2.2.8 {ECO:0000269|PubMed:16495228};
DE   AltName: Full=Copper-exporting P-type ATPase A;
DE   AltName: Full=Cu(+)-exporting ATPase;
GN   Name=copA; Synonyms=pacS; OrderedLocusNames=AF_0473;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   FUNCTION AS AN ATPASE, ACTIVITY REGULATION, INHIBITION BY VANADATE, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11756450; DOI=10.1074/jbc.m109964200;
RA   Mandal A.K., Cheung W.D., Arguello J.M.;
RT   "Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the
RT   extremophile Archaeoglobus fulgidus.";
RL   J. Biol. Chem. 277:7201-7208(2002).
RN   [3]
RP   CHARACTERIZATION, ATPASE ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751
RP   AND CYS-754.
RX   PubMed=12763798; DOI=10.1111/j.1749-6632.2003.tb07162.x;
RA   Arguello J.M., Mandal A.K., Mana-Capelli S.;
RT   "Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus
RT   fulgidus.";
RL   Ann. N. Y. Acad. Sci. 986:212-218(2003).
RN   [4]
RP   MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754.
RX   PubMed=12974640; DOI=10.1021/bi034806y;
RA   Mandal A.K., Arguello J.M.;
RT   "Functional roles of metal binding domains of the Archaeoglobus fulgidus
RT   Cu(+)-ATPase CopA.";
RL   Biochemistry 42:11040-11047(2003).
RN   [5]
RP   REGULATION, AND INTERACTION WITH COPZ.
RX   PubMed=18417453; DOI=10.1073/pnas.0711446105;
RA   Gonzalez-Guerrero M., Arguello J.M.;
RT   "Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly
RT   transfer Cu+ to transmembrane transport sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5992-5997(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 214-326.
RX   PubMed=16906753; DOI=10.1021/bi0610045;
RA   Sazinsky M.H., Agarwal S., Arguello J.M., Rosenzweig A.C.;
RT   "Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-
RT   ATPase.";
RL   Biochemistry 45:9949-9955(2006).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 407-671, AND CATALYTIC ACTIVITY.
RX   PubMed=16495228; DOI=10.1074/jbc.m510708200;
RA   Sazinsky M.H., Mandal A.K., Arguello J.M., Rosenzweig A.C.;
RT   "Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-
RT   ATPase.";
RL   J. Biol. Chem. 281:11161-11166(2006).
CC   -!- FUNCTION: Probably involved in copper and silver export.
CC       {ECO:0000269|PubMed:11756450}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC         Evidence={ECO:0000269|PubMed:16495228};
CC   -!- ACTIVITY REGULATION: Activated by Cu(+) and Ag(+) and inhibited by
CC       vanadate. Activated by CopZ in its Cu(+)-bound form.
CC       {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.25 mM for ATP {ECO:0000269|PubMed:11756450,
CC         ECO:0000269|PubMed:12763798};
CC         Vmax=14.9 umol/h/mg enzyme with Ag(+) as substrate
CC         {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC         Vmax=3.7 umol/h/mg enzyme with Cu(+) as substrate
CC         {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC         Note=Shows higher affinity for Cu(+) compared with Ag(+).;
CC       pH dependence:
CC         Optimum pH is 6.1-6.5. {ECO:0000269|PubMed:11756450,
CC         ECO:0000269|PubMed:12763798};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC   -!- SUBUNIT: Interacts with CopZ probably in the CopZ Cu(+)-bound form.
CC       {ECO:0000269|PubMed:18417453}.
CC   -!- INTERACTION:
CC       O29777; O29777: copA; NbExp=2; IntAct=EBI-9016967, EBI-9016967;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; AE000782; AAB90763.1; -; Genomic_DNA.
DR   PIR; A69309; A69309.
DR   RefSeq; WP_010877980.1; NC_000917.1.
DR   PDB; 2B8E; X-ray; 2.30 A; A/B/C=407-671.
DR   PDB; 2HC8; X-ray; 1.65 A; A=214-325.
DR   PDB; 2VOY; EM; 18.00 A; F=214-326, I=410-663, J=432-549.
DR   PDB; 3A1C; X-ray; 1.85 A; A/B=398-673.
DR   PDB; 3A1D; X-ray; 1.85 A; A/B=398-673.
DR   PDB; 3A1E; X-ray; 1.95 A; A/B=398-673.
DR   PDB; 3FRY; X-ray; 2.00 A; A/B=736-804.
DR   PDB; 3J08; EM; -; A/B=93-737.
DR   PDB; 3J09; EM; -; A/B=15-737.
DR   PDBsum; 2B8E; -.
DR   PDBsum; 2HC8; -.
DR   PDBsum; 2VOY; -.
DR   PDBsum; 3A1C; -.
DR   PDBsum; 3A1D; -.
DR   PDBsum; 3A1E; -.
DR   PDBsum; 3FRY; -.
DR   PDBsum; 3J08; -.
DR   PDBsum; 3J09; -.
DR   AlphaFoldDB; O29777; -.
DR   SMR; O29777; -.
DR   DIP; DIP-46021N; -.
DR   STRING; 224325.AF_0473; -.
DR   TCDB; 3.A.3.5.7; the p-type atpase (p-atpase) superfamily.
DR   EnsemblBacteria; AAB90763; AAB90763; AF_0473.
DR   GeneID; 24794013; -.
DR   KEGG; afu:AF_0473; -.
DR   eggNOG; arCOG01576; Archaea.
DR   eggNOG; arCOG02763; Archaea.
DR   HOGENOM; CLU_001771_0_3_2; -.
DR   OMA; HWMLPAW; -.
DR   OrthoDB; 21472at2157; -.
DR   PhylomeDB; O29777; -.
DR   BRENDA; 7.2.2.8; 414.
DR   SABIO-RK; O29777; -.
DR   EvolutionaryTrace; O29777; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd00371; HMA; 2.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006122; HMA_Cu_ion-bd.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00403; HMA; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 2.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   TIGRFAMs; TIGR00003; TIGR00003; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell membrane; Copper; Copper transport;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..804
FT                   /note="Probable copper-exporting P-type ATPase"
FT                   /id="PRO_0000350601"
FT   TOPO_DOM        1..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..364
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..680
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        681..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        702..704
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        726..804
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          16..82
FT                   /note="HMA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          740..801
FT                   /note="HMA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        424
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         30
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         457..462
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         490..501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         618
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         622
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         751
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         754
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   MUTAGEN         27
FT                   /note="C->A: Reduction in ATPase activity; when associated
FT                   with A-30."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   MUTAGEN         30
FT                   /note="C->A: Reduction in ATPase activity; when associated
FT                   with A-27."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   MUTAGEN         380
FT                   /note="C->A: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   MUTAGEN         382
FT                   /note="C->A,S: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   MUTAGEN         751
FT                   /note="C->A: No effect on ATPase activity; when associated
FT                   with A-754. Reduction in ATPase activity; when associated
FT                   with A-27; A-30 and A-754."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   MUTAGEN         754
FT                   /note="C->A: No effect on ATPase activity, when associated
FT                   with A-751. Reduction in ATPase activity; when associated
FT                   with A-27; A-30 and A-751."
FT                   /evidence="ECO:0000269|PubMed:12763798,
FT                   ECO:0000269|PubMed:12974640"
FT   HELIX           215..222
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          225..231
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          248..251
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          268..271
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   HELIX           273..276
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          301..307
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   HELIX           313..325
FT                   /evidence="ECO:0007829|PDB:2HC8"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           411..417
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          420..424
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           425..429
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          435..444
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           446..456
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   TURN            457..459
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           463..474
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          485..488
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   TURN            489..491
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          492..495
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          498..501
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           503..508
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           515..526
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          530..536
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          539..547
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           554..563
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          567..571
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           576..586
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          589..592
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           597..599
FT                   /evidence="ECO:0007829|PDB:3A1D"
FT   HELIX           600..607
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   TURN            608..610
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          613..617
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   TURN            619..621
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           623..628
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          629..635
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          646..653
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   HELIX           656..663
FT                   /evidence="ECO:0007829|PDB:3A1C"
FT   STRAND          740..750
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   HELIX           752..754
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   HELIX           755..764
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   STRAND          768..772
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   STRAND          774..782
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   HELIX           783..785
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   HELIX           786..795
FT                   /evidence="ECO:0007829|PDB:3FRY"
FT   STRAND          799..802
FT                   /evidence="ECO:0007829|PDB:3FRY"
SQ   SEQUENCE   804 AA;  86432 MW;  610EB948C1D6B16F CRC64;
     MVKDTYISSA SKTPPMERTV RVTGMTCAMC VKSIETAVGS LEGVEEVRVN LATETAFIRF
     DEKRIDFETI KRVIEDLGYG VVDEQAAVSA EVEHLSRMKR KLYVAAFAGV LLLFLAHFIS
     LPYEDFVQLL IALPAIFYSG SSIFKAAFSA LRRRTLNMDV MYSMGVGAAF LASVLSTAGV
     LPREYSFYET SVLLLAFLLL GRTLEARAKS RTGEAIKKLV GLQAKTAVVI RDGKEIAVPV
     EEVAVGDIVI VRPGEKIPVD GVVVEGESYV DESMISGEPV PVLKSKGDEV FGATINNTGV
     LKIRATRVGG ETLLAQIVKL VEDAMGSKPP IQRLADKVVA YFIPTVLLVA ISAFIYWYFI
     AHAPLLFAFT TLIAVLVVAC PCAFGLATPT ALTVGMGKGA ELGILIKNAD ALEVAEKVTA
     VIFDKTGTLT KGKPEVTDLV PLNGDERELL RLAAIAERRS EHPIAEAIVK KALEHGIELG
     EPEKVEVIAG EGVVADGILV GNKRLMEDFG VAVSNEVELA LEKLEREAKT AVIVARNGRV
     EGIIAVSDTL KESAKPAVQE LKRMGIKVGM ITGDNWRSAE AISRELNLDL VIAEVLPHQK
     SEEVKKLQAK EVVAFVGDGI NDAPALAQAD LGIAVGSGSD VAVESGDIVL IRDDLRDVVA
     AIQLSRKTMS KIKQNIFWAL IYNVILIPAA AGLLYPIFGV VFRPEFAGLA MAMSSVSVVA
     NSLLLRNYVP PIRRGGDSVE KIVLELSGLS CHHCVARVKK ALEEAGAKVE KVDLNEAVVA
     GNKEDVDKYI KAVEAAGYQA KLRS
 
 
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