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A2MG_RICCN
ID   A2MG_RICCN              Reviewed;        1892 AA.
AC   Q92HD6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000250|UniProtKB:P76578};
DE   Flags: Precursor;
GN   OrderedLocusNames=RC0835;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
CC   -!- FUNCTION: Protects the bacterial cell from host 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; AE006914; AAL03373.1; -; Genomic_DNA.
DR   PIR; C97804; C97804.
DR   RefSeq; WP_010977442.1; NC_003103.1.
DR   AlphaFoldDB; Q92HD6; -.
DR   SMR; Q92HD6; -.
DR   EnsemblBacteria; AAL03373; AAL03373; RC0835.
DR   KEGG; rco:RC0835; -.
DR   PATRIC; fig|272944.4.peg.952; -.
DR   HOGENOM; CLU_000965_2_0_5; -.
DR   OMA; LDRYPYG; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR041203; Bact_A2M_MG5.
DR   InterPro; IPR041462; Bact_A2M_MG6.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR001434; DUF11.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 1.
DR   Pfam; PF17972; bMG5; 1.
DR   Pfam; PF17962; bMG6; 1.
DR   Pfam; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   TIGRFAMs; TIGR01451; B_ant_repeat; 1.
PE   3: Inferred from homology;
KW   Protease inhibitor; Signal; Thioester bond.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1892
FT                   /note="Alpha-2-macroglobulin"
FT                   /id="PRO_0000036244"
FT   CROSSLNK        1441..1444
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000250|UniProtKB:P76578"
SQ   SEQUENCE   1892 AA;  213784 MW;  10265949C00D7623 CRC64;
     MKNIFRKFVF TIFVCLINLQ LIAASFNEKI PLYFKLTNEN LLAGQNALNI DLCDSRIKEW
     CTKPQRELGL NGKKINDYIS ISPDIKGEWR FGWWYNINFT PESNFVAHQT YKITIEDYIF
     PNFVGLKSNN ISFTTLPLLP IIKEMNYLQD NIDISKKFVQ TKIAFNYPID PKTLEERIEF
     IKSSTKEKLP FSIKFNTNNT EATIITNIPP LTDKEDTISV IIKDGVKPLH GGEVFTYKNV
     KDPNNKTPNN IRYSYKENVL IPSLSSYLKI TNSTATIVKD DKLKPEQIII ITTNTPVSGE
     EIKKHLELFL LPQDKPAFLG VAGKKNYKWQ NPKEITDDIL KSSEKINFEL LSSVPSITTM
     HSFKVDTFAS RALLVKVNQG VKTSDNLTLG SDYFQIVQIP DNPKEVKLMS DGSILSLAGK
     RKLPVYSLGI DKLYLEIDRI NQQEVNHLIS QTNRYNIFQN PTFINEYTFN EYNISEVFQE
     EVIVNSQNLN LPHYTDLDFS KYFNLEEAGS YSKGLFLAKV YAKDNNNIIS QDKRLILVTD
     LGCIVKTDKT GTHHIFVSYI SNGKPAGGVK ADIIGLNGEV LVSSKTDSKG HAVLSNINDF
     SKEKTPVAYI LTTKDDFAFM PYSRIDRQVN YSRFDVAGAV SSDQGLKAYL FSDRGIYRPN
     EQGHIGIMLK QTDWQGKFDG LPLEIQVTNP RGKVIDKSKI VLDAEGFGEY LFSTLDDALT
     GLYNISLYLV GDKGSNNYLN SVSVRVGDFQ PDRMKININF NNSQDELWTN PKDLKATVNL
     INLYGTPAEN RKVSGFIDIR PTEFFVPRFK EYKFYSSKGN KEFFYERLGD ITTDSKGTAN
     FDLNLEKYYN ATFNLTFSAE GFEPDSGRSV NASKSLIVSP LPYIIGFRSD SDLKYIKTKT
     SAAIEFIAIS NKAEKVAAPN LTLNLKKINY VNNLVADSNG NYSYSSVPIE TNISSDKINI
     TANESYIYKV PTKEAGDYVI YLTDKEDTIF AQAEFSVIGE GNVTANLTDK ANLKVKLDKD
     DYTAGDTILL NIITPYTGYG LITIETDKVH NFEWFKADEN NSIQEIKIPD GFEGKGYVNV
     QFIRDIEATE IFISPFSYAV VPFTAGIYKH KQDIGLTLPA KIKSGEKLAI RYRTTNPGKI
     IIFAVDAGIL SFAGYQTPDP LNYFINDKAL EVRTSQIMDL ILPERPLLMK AYMAAPAGDG
     CINVARNLNP FKRKSQPPIA FWSGILEADL DEREVTFDIP SYFNGTLRVI GVASSLDSIG
     TSKADLLVQS DLIINPNLPL FVAPNDEFTV PVTIFNNLKD SGNAQVFLNI ETSEGLKILD
     YPKEIPIDEN KEATINVKLK ATDQLGSADL KVVASINHLK PDIISMAVVH SSELTSTTSV
     RPASPSVTTV NTGFITDNKA NLKILRDVYP EFAKLQISAS KSPLAIISGF KDFLDNYPYG
     CTEQLISQNF ANILLYNEQE LVQILKTDRK NMDESLSKIF QTLSERQNYD GGFRYWNNFN
     DDSDPFISVY AMHFLSEGAT RYLAVPSDTF NQGIYYLENM ANRSINSLDE AREKAYAVYI
     LTQNSVITTS YIANILKYLD EYHKNTWQDD LTSVYLAASY KMLQMNEEAE KLLDRFTLNK
     PISKTDYQYY NPLIKYSQYL YLIAMHFPER LKDFDPKIVQ DIALFAKDNY NSLSASYAIM
     ASLAYADKIN HVDEATIKVT STDKEVTLKG NKVMIAELSV ENKNIDLTSS SNGFFYQLLT
     SGYDKQLTEN KEIVKGIEIT KKYLDENNKE VSKVKLGDNI TVEITMRSGS NKTLSNMVLI
     DLLPAGFELL PDNNHINILE RTQEVMIWKP IYINNRDDRV MIFGTISDQK MTYQYKIKAV
     NKGIFSTPAI YSEAMYDPQT YYRGVIGNII VE
 
 
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