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A2MG_THEMA
ID   A2MG_THEMA              Reviewed;        1536 AA.
AC   Q9X079;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000250|UniProtKB:P76578};
DE   Flags: Precursor;
GN   OrderedLocusNames=TM_0984;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Protects the bacterial cell from peptidases.
CC       {ECO:0000250|UniProtKB:P76578}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000512; AAD36063.1; -; Genomic_DNA.
DR   PIR; E72310; E72310.
DR   RefSeq; NP_228792.1; NC_000853.1.
DR   RefSeq; WP_010865234.1; NC_000853.1.
DR   AlphaFoldDB; Q9X079; -.
DR   SMR; Q9X079; -.
DR   STRING; 243274.THEMA_09430; -.
DR   PRIDE; Q9X079; -.
DR   EnsemblBacteria; AAD36063; AAD36063; TM_0984.
DR   KEGG; tma:TM0984; -.
DR   PATRIC; fig|243274.5.peg.997; -.
DR   eggNOG; COG2373; Bacteria.
DR   InParanoid; Q9X079; -.
DR   OMA; EYFPDTA; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   3: Inferred from homology;
KW   Protease inhibitor; Reference proteome; Signal; Thioester bond.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1536
FT                   /note="Alpha-2-macroglobulin"
FT                   /id="PRO_0000036245"
FT   CROSSLNK        919..922
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000250|UniProtKB:P76578"
SQ   SEQUENCE   1536 AA;  175956 MW;  71D493908F0CC1F4 CRC64;
     MGMKRLIFLV FLLISFSLFG GYAYFSRYPV LHPDEGLSFV ISDLENITLN VWKISEEDFL
     KAVFDPESFN FSLLEITRPI YSKKFSSEEW KEFSFPLKDR GFYFATLVSN EGTVFRRVID
     RSLFIVTDLE AIYFSDSEKL RLHVFDSDGD FVEGAEVLLF EDSKLIDRVF TGKDGVVSIT
     KHFDTFYIRY GDSRFFGGVY FSGGGLEREK LFFVTDRPIY KPSDTVHFRG QIFSFEEGLY
     KAFEKTKVTV SIFDTKKNEV YRSEFETDEL GGFSGSMKLP DTASVGLYKV NVDHGGRRYY
     EYFLVEEYRK PEYKVEIETD KDVYISGEVV NYLVRVKYFN GQPVAKAQVA YYVRAFPEEG
     SGYLVYRGTD FTDEEGNLRL GVKTEEGFQG SYRLEVIVTD ESQRQIEETR SVKVYADNVL
     ISPLDRYVST SPGKQVRVKV KVTDLSGNPL NGLLTTSSED STSTVAVENG EAIVTFTPKE
     PKSYRIELSF GKANTHFYVY AYCGAGTSSE FVINPATNTV KPGDELSVQI LAPGKVMGVL
     GIVSNRVYDT IPVSFTGSVN LRVRIPKDIP EKNLFISFVG LDDNGRIYKL ERLNVLLDTN
     FTTMKILFDK DQYEPGEMAQ ITIESNVDRV CLFLVDEAIY AMVGAEPPVL ENFLYPYMNY
     PRTRGGFPHY WRLYVSRNSF RNKLASLPEE KTFADFKQNA LPSKLNVREY FPDTALWIPS
     LKLHNGTARV SFKVPDSITS FRATAYGFSK DRFSQTESEM VVSKKFYLMP HLPSFLRESD
     VIKISATVFN RTSKTLPVQL TVELPENIEL LEGSSSRHFL MEANSSHTET WTVKAVSASE
     GSFVKFVAVG EDLNDAVSMR LPVERFAFER EFYRIMLLDG KETLEIPGQF ISSRIRFLDS
     IVPLVEDSLK RLIDFPYGCV EQTMSRFFPA VVAASAGIEV ENLEEIIQRG LFKLYSYQHN
     DGGWGWFRFG ESDDFMTCYV MEGLYFTMKA GYDVAESVLQ RGIEYLRKHP SAYGSYVLDL
     YGVNHEPFKP ESEADLVFLS LSSKEALKQL MNYVVQDEQK AYLNVYSNNP LISEIQLNSV
     FLRALAKWKE FPELERKVTN YLLLKKDSAF WTSTKDTSFV ILALLEAMPE YASTTLKVIN
     SENTFELKPG EERSLVPGSL TVSGKGIVEV EVVYIEVPKE AVSEGLEIKR EFYKRYELLI
     EENKMIVDAF VPIGRGYVPR SIHPVEKEQT EELYILPYKY WKKTIEYRGV PLEINGAEVK
     IKGETYTFFR IETFNGLILV FFRNEALIYD TEKNTITRYL DVTDAGFMRS GPVFLMKGFV
     LVGDEKIPVP EDVTGLSCTM DEILLRGENK TYWYRNGEFV DLPFVARRVF FWDGKKLVAE
     NIRFSGSSKT LRNRVFEVVF DVGDVKIELG DIIKTVVRVK GDGNYLIVED FIPSCAQVLS
     NYREKGIEEN KFSYSWYSSW NAWYSGREIR TDRVALFARY LYGNSFDYVW RATAEGVFHL
     LPARVYPMYS RGLYAHTDPD VLFIGADFID GRDDQP
 
 
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