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Database: UniProt
Entry: A0A1W6E3R3_9BACT
LinkDB: A0A1W6E3R3_9BACT
Original site: A0A1W6E3R3_9BACT 
ID   A0A1W6E3R3_9BACT        Unreviewed;      2189 AA.
AC   A0A1W6E3R3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A6C57_06305 {ECO:0000313|EMBL:ARK09983.1};
OS   Fibrella sp. ES10-3-2-2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK09983.1, ECO:0000313|Proteomes:UP000193660};
RN   [1] {ECO:0000313|Proteomes:UP000193660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA   Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC       {ECO:0000256|ARBA:ARBA00010556}.
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DR   EMBL; CP015317; ARK09983.1; -; Genomic_DNA.
DR   STRING; 1834519.A6C57_06305; -.
DR   KEGG; fib:A6C57_06305; -.
DR   Proteomes; UP000193660; Chromosome.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR   PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF13715; CarbopepD_reg_2; 1.
DR   Pfam; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193660}.
FT   DOMAIN          1011..1155
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1392..1482
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          352..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2189 AA;  241449 MW;  3AD7DB4DB3AA62F1 CRC64;
     MRNPAIYICA LTLFLLPLLG QTRKKSSSSS SPPMTDYAAS WKTADSLMAR GLPQSALVIA
     DRVYTEAKRT GNDPQLLKAA MRRVVYRTNG AKDEETYLTL LSSLKTDIDA TTGPTRAVLQ
     SVMADVYWQY FQQNRYKFYN RTATAPDEPT AQSATTDALD PRTWDARRLQ QTVTELYTAS
     TQEATNLQQV PVAAYDAVIS KGNEAGLALR PTLFDVLAHR AIDFFTQAQS DVIKPIQAFT
     VNNPAYLGRP EAFATMALPA TDPLSGAYQS LRLYQQLLAF HRNDAGGVAY AANDIERLAL
     VKRLGTLPNE DDLYRQTLTQ QIAATRGKPA EAEYMLALIQ HLAETGEVRP LPRGRFQATD
     QETPDPSPAD TTRRWDRKRA ADLARDLIAR FPNTISAQSA ASLLANLLQP ALGVEVEEAT
     EPGKPFRARV TYQNTKTLYY KVLRLSATEA RALTRFDNYR NDPKYDKWFA AVQNHPVVAE
     EEVTLPDDGD LRNHSVEIAM KALPLGHYVL LVSNEGKWAT PSAKTAEIVS LGTFAVSNLS
     YVTVGGNMEY TGTRTFYVTH RMTGQPLAGV SAQLFVQDSQ SDALSVAGTY NTDAKGKLTI
     AITTDRSAFL RLTIGNDVLD TDSFYGYPNF RNPEAPTDNR YSVVFTDRAI YRPGQTVYWK
     VLQYSGKDNE FAVVPNAPMV VRLTDVNGEE VTKAEVKTND FGTASGTFTA PVGRLTGQMT
     IATANGQATI RVEEYKRPTF TVVADSLKQA VVLGQNVPVK AIAKTLAGAV VDGAAVSYRV
     TRTYYRPYWG WHWWRPIRPT SEQEIANGTA KTNAEGVVNF SFLAQPDLSI AASEKPQFTF
     TITIDVTDVS GETRSTTQTL RIGYTALTAE LVLPSPVLTT EPKPYVVRLL NASGNKVGIK
     SGSVAISRIT PPRPGLRRRL WARTDRNLLT REAYVAQFPL DIYANEDDPT TWPKTPVRST
     SPTSVSLAGL ASGMYVADIN AIDSTGVSVQ QAVFFEVIDP GKPTAPIRAG AFVQVQKATA
     QPGEEAIFWV GTSTASATRP DAVLMAVEER GKIVREEWLT VTGQPIRVAL PVQEKHRGNF
     VVHFATVQNG RLLSQSETIT VPFTNKELTV ETETFRDKLK PGQPEQWTVR ISGPKQDKVL
     AELAATLYDA SLDAFARLEW PTSFYSVNYT NSGYWQSQAF GTIITQQYWN RSMPAPVRSA
     LQQRMVPRLT WGPYNYDQYR GRFTLNLSTL TIHVKRDKSV LTGRAFLGDI EAPAPGVNVV
     VKGTKQGTVT DAAGNFTIQM EKPTKKVALL VAFVGYKPAT IELADKQSII TVLQADDQLL
     YESVVVGYGT QNRRDMTGSV NIRGAAPMAM AKMAAAAPDV ADASAVQVEQ PNVPTKVPVA
     TPPLIRKNFN ETAFFFPQLQ TDKQGRVVLN FTMPEALTRW RLVTFAHTKT MQTGTMEREI
     VTQKELMVTT NVPRFLREND TLRLTARIDN LSGKPLTGTS QLNITDAITG ESLNAKMGLA
     VMNQTVSVKA GQSSLAAWTL VVPQDLPPVA FRVTATAGTF TDGEERVVPV LPNRTLVTDV
     QPFWINGGDK DRTFRLGPLV DHNPELPLNT ERLTVEVTSN PAWYALQSLP YLMEYSYDCA
     EQVFSKMYAN SLGAHILASR PQFRQVVDVW KQTPPRSPLA SNEELKAVML ENTPWLADAK
     SEADRTAKLG QFFDQSRLAA EQRRAIDKLR QLQDASGALT WFSGMRPNLS MTLHVLAGLG
     HLQKLGVAFD PGVRADVATL QAGLIRYADA EIVRQIAEQK RRAAEQKTTP GTPYWAAQYL
     YARSFYLGTN AVAKEVETYL LPVLTTGWQQ SSLQSQALAA TTLHRFKKVS EAHAILQSVT
     ERSKVSEELG MYWPENTSGT YWYQTPIETQ AYLIEAYDEI CRTESVASTA TAGQLDCFAW
     LRTMPQHKNL VGSGPFIDKM RQWLVQQKRT QSWPSTKATT EAVYALLLRG SDWLDTKATM
     TVLVGGKDIA PRVTKTETLT GYQKVTFAPS EVTTAMGVVT VSKPAKTGPG WGAAYWQHFE
     PLDAIAGNGT NLTLRKTLFR QRNTDAGPVL EAITPKTILK PGDLLKVRMV LTADRNMEYV
     HLKDGRASGF EPVAALSGTK YQNGLSYYEA PRDASTDFFI EYLPTGTHVF EYALRVVHTG
     DFGAGLATVQ CFYAPEFAAH STGGRVQVR
//
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