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Database: UniProt
Entry: A0A0S6VY97_9BACT
LinkDB: A0A0S6VY97_9BACT
Original site: A0A0S6VY97_9BACT 
ID   A0A0S6VY97_9BACT        Unreviewed;      1832 AA.
AC   A0A0S6VY97;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:GAK50873.1};
GN   ORFNames=U14_02114 {ECO:0000313|EMBL:GAK50873.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50873.1};
RN   [1] {ECO:0000313|EMBL:GAK50873.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
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; DF820456; GAK50873.1; -; Genomic_DNA.
DR   STRING; 1499966.U14_02114; -.
DR   HOGENOM; CLU_002018_0_0_0; -.
DR   Proteomes; UP000030700; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd02891; A2M_like; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 2.60.40.3710; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR032812; SbsA_Ig.
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; PF13205; Big_5; 3.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 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   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1832
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006631579"
FT   DOMAIN          959..1113
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1178..1268
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1832 AA;  204217 MW;  30398CDCFA049C53 CRC64;
     MKIMMTKLSF LLLFALLAGL TGAAEQPLDI ISATPQGDLN SLDDAQAITV TFNLPVVALS
     GVEADVKEGM ITLDPTANGT FRWMGTSTLS FTPDAPLAYS TRYVATVKAG LKAVTGETLA
     KDYTFSFVTP RPQVKDSFPY QEQQYVTLQQ PLYLQFDQPV DPAEVTKFAT LIGEGSKKGV
     PIAAAAIQQA DVDQGQAYWL EAGNAAQVKI LPQQPLDMEK VYTLKLKAGL PGKGGNLGMA
     QPYELKFTTY NHFRVEGVFP ARDFECGTTY YPEQGLRLVL SNAASGDAIM QHLKIVPEVA
     FEKDETYETS EFYLQPKFEP NTKYSLTVTA GLQDIFGNEL KEDQNFEFTT SDFAPYITMP
     SGRMISEAYL GTRFPIKVMN VTDAPLQMKT YRTPEDALKA AKAMGNYEFD LADPDIDRTY
     RPDIIHNKVA MMPFDLKEAL NKGEETGIIG MKLGYNWCDG SQHDYKSLIF LTNMSVSAKF
     SAINNLFWVT KLQDSSPVAD ADVELYDENQ QFLWKGKTDA NGFAESPGWK ALGLKVTSSW
     EQPWVFALVR SGKDQVIVHS KDGTGLWPYR FGISYEQAAE HQTNDGYLFT ERGIYRPGEE
     VRVVGIIRDK QAGEFVIPKA MKVDVIVRDP DGKEVFKQEL PVSEFGSIHF PMTLASSAKL
     GEYGIECKFP MPAYIELPKE DAEYFNRSIY GTFQVEQFRP VEFEVKVDLP QAEYIKGDAA
     SGKIGATYLF GGAVRNVPLD WNISRSYYLF EPESPALKGF SFNIYDRNWG GSVAQQTAAL
     DDKGEYQFNY TLKDEDVGAY TYTIEATVTD TNKRQVSNRQ QVVVHGGEYY IGLKPASFFA
     SINKDFAIST VAVNPQEQPI AGQNYTVQVK RIWWESARRA GNGGRLYWES EQKEEVAQEF
     QVTSAKAAQD LKLSLDKVGY YKVVADGKDS RGNPIKAEDY FYAVGDGYAA WMRSDDDYVE
     IVADAKAYRP GDTAHILVKS PYEAATALVT VEREGVIERW VEPVNGSADT IDVPIQANYI
     PNVYVGVILI QGRVAYDKIE DDLDLGKPGF KIGYAGFKVN PSERRLTVNV ATDKEEYRPG
     NEVEIQLDVT DANGKGREAE VVVSVVDVGV LNLIGYNTPD PFDYFYRERP LCVLTSELRN
     NIVGQRNYSE KGEKQGGGGL DMAEMMKLIE MREKFRPTAY HNPEVRTDAN GKATVKFTLP
     DNLTAFKVMA TAHTKDAHFG AGDKRFKVNK NLMLTSSLPA FMRIGDTIKA GVMAHNRTEQ
     DGQAAIQAEA DGVELTSEDV QQATLPKSDK EEVLFSYTAK EERDATFMFR GKMGEETDGV
     KITIPVLLHR LPLTTALFGS TTENVHRETV AVPDDATPGW GNVTVSLAST IFTDIKGGVE
     FLFDYPYGCL EQKTSRILPI ILAEELIKGF NLDVFKDDDY RKVVQSTLDE FADYQHESGG
     FGYWKTPRWP SPFLSAYAVF ALKMAQEKGY AVDTDMEQKA VTYLENVLKG QNERATAYRY
     NDLAWNATDA FILYTLSLYD KYEASYATRL YNVRERMPVF GKALLLKAVA QGKGDKLIRS
     TLTKEILNAA RVDARTASFD ESDNGDLAWI HHSNVRTTAA AAQALMETQG ATKETESFIP
     KAIEWLLLER KNQAAWRTTQ ENLFVFYALS TYLNTFEGTA PNFTGKVLLN GQEILSEMFK
     GRTVKLVGVE KPLDDFAKTP QNDLEFVKEG DGRLYYTATM TYLPSGEPEP IDYGMAVQKK
     MTVVKGQGVG TDMFYRGDLV KIELTVTTPR DRLFVALDDP LPAGFRALNF GLQTTDQSLR
     DLIKGETPFV FRSRSTSSSI RLSSSCVALR SP
//
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