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Database: UniProt
Entry: A0A160T6A6_9CHLR
LinkDB: A0A160T6A6_9CHLR
Original site: A0A160T6A6_9CHLR 
ID   A0A160T6A6_9CHLR        Unreviewed;      2028 AA.
AC   A0A160T6A6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 2.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Putative Alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:CUS05059.2};
GN   ORFNames=CFX0092_A3181 {ECO:0000313|EMBL:CUS05059.2};
OS   Candidatus Promineifilum breve.
OC   Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC   Candidatus Promineifilaceae; Candidatus Promineifilum.
OX   NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS05059.2, ECO:0000313|Proteomes:UP000215027};
RN   [1] {ECO:0000313|EMBL:CUS05059.2, ECO:0000313|Proteomes:UP000215027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cfx-K {ECO:0000313|EMBL:CUS05059.2,
RC   ECO:0000313|Proteomes:UP000215027};
RA   Oliw E.H.;
RL   Submitted (JAN-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; LN890655; CUS05059.2; -; Genomic_DNA.
DR   KEGG; pbf:CFX0092_A3181; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000215027; Chromosome i.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 2.60.40.3710; -; 3.
DR   InterPro; IPR011625; A2M_N_BRD.
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; 4.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 1.
DR   Pfam; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215027};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1093..1242
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1314..1404
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          1277..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2028 AA;  217292 MW;  E8A20D8A0CE70495 CRC64;
     MSSRHITRSL LILVAFLLLL AACRRGQPEA VPTLASPAEI EPTEAAAPAE PTAEPAAEAE
     PTAAPIVARP VPVEDIDWPP QVIASDPRPG QEVGLETPIT VRFDQPMDQS SVEAAFTLDP
     PVAGELSWPE PDTAVFTPAE PLELGQTYNV RIADSAGAAN GQTLSQPVEF AIQATGPLQV
     TQVIPADNAG TVQTDAIITV VFDKPVVPLL SSGEQSGLPQ PLTFDPPATG TGEWTATSIY
     RFMPDPPLAG ATTYTVSVDP ALTDLTGSPL ADAPTWSFTT LPPDVVLTEP ENEKARVAPD
     ASILVIFNMP MDMGGVEAAT SLANSDGAAV PVTFAWRDNR SVDITPVDPL PLGDEYTLTV
     AAAATDINGA ATMEDDHVST FSTIPLPAIL NTYPADGAVA DMFGNGFSIE FASPMNDETI
     EDQLIITPTP EDVDYFISQW DEGYSVYVQF TLTPDTEYTV TVPASAADPY GNTLGEDFTF
     TFTAAPIPPM ASFNLPREVA QLSTSFPSDV QVLSRNIGEV TVELYDIGVD TNLVFNTYLM
     YEQEPTGEPI FRTTITPTGP ADELSVSPVQ LAAGGVLPTG LYRLRVTSPE LSSDTNWWQN
     RNVLLVVGDT NLVIKEMYGE VNVWATDLAT GEPVGGLDLT LYRRSGEEAG TAVTDANGFA
     RFDYDPAESY LEGVAVVANE PGAPGFGLAS TLWTGNISVW NLGLTVDTGP EQALFAYIYT
     DRPIYRPGDT VFFKGIVRHP QFGRYELPDV TELELSVNPN FFMGEEGFSE TFTVTLDEDG
     VFAGEFALPD DMPLGTYSFN ITGDFWLSSR TFTVAEYRAP EFEVLVTPEQ PELLRGAATN
     VTVNATYLFG GSAAGLPVTW NITAVEFVPT FEVNPPFTFG DSADFNYVVD PFVFGGGGLE
     ENVGSGNGET DAAGNVTIPL PAEMLDELEA GSRQVTVEAT VGGLGEFPVT GRATVTFHSA
     DAYVGLRAAN TLVDAGDEVT IDLLSVDWAG EPLGNQAVEV VFYEREWESE RVAEFGMRTT
     RWTPVDTEVG RQSVTTDAGG EATATFTPES GGMYLAVATL TDGGGRQQLS SLGLWSVDET
     FAGWRTDPNM RTMEVTPDRN EYRAGETARV LVQSPFAQPV NAWLVIERGN IIDQQVVTVS
     GSQVLEIPIT EAYAPNVHIT VVAIKPVDPA DADFPYADIR IGFAELTVPP DQFDLNVTIT
     PGAEEYAPGD TATFDVVVTD QAGAPVQAEV SLSLVDLAVL LLKEDNAPHI LEAFYSPQPL
     RSTIGSGLLV TGEGLEIEEP LPGGGGGGGG GADEGLESLR LPGEDDVRRD FRDTAYWEAK
     VLTDADGRVS VEVPLPDNVT TWRMHSKAAT TDTRVGQASA DILARLPLII RPVTPRFFTV
     GDTLSLGANV NNNTDAAIEA TVTLEASGLA IDGPTEQTVT VPADGRVLVT WPVTVEDVAS
     ADLTFRVAGG DYSDASKPTL GIGPDALLPI YRYDGRDFVA TAGELDEAGR RVEAVVLPQG
     VNQTQGEVLV RLQPSLAAAI VESFEVINDP VVPFIECAGS LADRLLHNTA VEMAIRDLDL
     DMADMATTLA ERNAADAAKL AALQMAGGGW GWCFSAESDP WISAQSLLAL TRAAELGYEV
     DATVIDSGAE YVSGRLAPVN QLGDASEANR QAFFLYVVAQ AGEDILEDAD ELVAEHRALL
     DPYAKALLAL AYDAAGATGD NQDALLTDLN DEVIMSATGA HWEDDETDFL NLSSDIRGTA
     MVVEALAQLQ PDSPLLPPAV RWLMVARQAE TWSTLHTTAW SVSALSKWMA ASGELEPDYA
     YELLVNLQSR AAGSFTPDDP TAAETVEIPL SELLTDDTNF FDFQRGEGDG RLYYTLRLNS
     AIAVEQLDPI SRGFTVARRY FDAACDPATE TCEPIAGIAA GERVRVELTV IVPNDRVYVL
     VEDPIPAGTD AIDPNLLTSE SGRGGSIVPA ENEFADGFWG WWYFDHIQYR DEKVVFLSQF
     LPAGTYQYTY FLQPNIPGTY QVMPATARED YFPEVFGRSE GAIFTITE
//
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