ID A0A142XI75_9BACT Unreviewed; 1915 AA.
AC A0A142XI75;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=A-macroglobulin complement component {ECO:0000313|EMBL:AMV26723.1};
GN ORFNames=VT84_20150 {ECO:0000313|EMBL:AMV26723.1};
OS Gemmata sp. SH-PL17.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV26723.1, ECO:0000313|Proteomes:UP000076098};
RN [1] {ECO:0000313|EMBL:AMV26723.1, ECO:0000313|Proteomes:UP000076098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV26723.1,
RC ECO:0000313|Proteomes:UP000076098};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011271; AMV26723.1; -; Genomic_DNA.
DR STRING; 1630693.VT84_20150; -.
DR KEGG; ges:VT84_20150; -.
DR PATRIC; fig|1630693.3.peg.4280; -.
DR OrthoDB; 97821at2; -.
DR Proteomes; UP000076098; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF136; GH01829P-RELATED; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 954..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 990..1010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1206..1298
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 70..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 147..181
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1073..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 208023 MW; 9E19734DFB0286D5 CRC64;
MNPESNVIAE LQPLLDALCE EVISPDQLRR LEELVLMHPE AEEHYIRFMS FFADLIGHVA
GLPEPKALAQ APPESVAAPA TRPAPVPRAP AEVSPAHVSP NPSPKQQENV MRRPRSLKSV
VWLAVFGTLG ALVGSQGYGW YSRSHDVAEK QRALQIQLEE VARAEAEKAE AQRESRKHIE
AALAAENALQ AEYQAAYESA RKAIEDKDFV VRLTGPAHIQ PGAPNKWQIE TLRHGAVGRP
QKMDVVVKDA KDQELLRQTH DKPVGAATLE LPVAFWEKVK PGSDLFLEVT AFTDDRKSVL
AERLPLARPV FVTHLVTDKP LYKPGETIRF RSLTLDRSTL RPPATDTHLK FRLRDPGDAV
TTLDEGNGRL LQEIRPVLGP DNKPLRGIGV GEHTLASDAP GGEYKLDLFE ASAETGKEVL
LETRKFIVNR YVPDTFEKKL EFDGKSYGPN EFVQARIDVS RTAGGPMKNA TANVVASTGS
SDFFQQSNSR FTTDSTGKVF LDVRFKLSAE VFEKVAPGAA PAATLSVNIR DGSDSETIVR
PIPLVTKTLR VEFFPEGGDM VEGVPGRVYF MVRTPNGKPA DLKGVITDGT TTFAEVSTLT
DAENPGVNRG HGVFTLKPKA RTQYFLKLTS PNGITEPTKD GFPLPEAKAD GVALDAATEK
GGAIRVRLQT ARGPKTVHVG AYVRERLIAQ QKVTLNAHQS TEISLKSDDT AGGVTRITVF
EERRDDAGQA ALLPRSERLV FRGQGQHLVL NANPDRVRYT PSGKVRLDLS ATTETGAPTP
AVLMVGVVNR SVIAMADNKN DRLLPTHFLL SGEVKNSAEL EHADFLLTDH PKAAVALDLL
LGTQGWRRFA EQDVPPAKPV DQADVNTMLV AHGQRPTAPL QLLELEKQRV SAEFTPRLEM
ARIQVATTEA QWSAIPAALT EKLAQAQAHV SAAQALKTEA QSALSDYKER YQRFGAALVP
LLAAALVAIF IFIVVSSAMS ATATKPAGRL RPFIAGITTL AICGMLVLLV NNMGSNSNST
FSFVGSSIKP PGGMVDQTVS GPVPRLGTVE GGRGTRTPRP IDDSGSMPDL DNPLRPPGAP
AGPKASPPGP PTVGMPGAGG APPRGGKPSP KPDAGRGTSF PNHDGTFTGD VQKRLSSARS
DKTRAALRSW SLRSPDGFAD RMPEGLIHKS DGRRSALPVI MPFMVREYAH ERDPQLGEVR
SDFTETVYWH PVLVLPENGK STIEFQLSDD IARYQVLVAG HTLDGRIGAI TTTLEARKPF
SVDPKLPLEI SHTDTVDAPI RVTNDSDVTR SVTFNTTATG FKTKGPLQET IELAANAKGR
KLLRLNADQL QGDASLLIEG RSAGGDPDVI RRMIRVVPDG FPRVGSVSDM LEKGRVRGSI
TLPKDVVPGS LRVRLEMYPT TMADLVKGLD GLLREPYGCF EQTSTTNYPN ALILDYMNQT
NQTNPAAAAR AKGLLDKGYG RLISFECPDT PERTKHGFEW FGAADRQHEA LTAYGLLQFK
DMARVHPVDP VLIQRTQAYL LSRRDGKGGF KRGPDGHSFG SAPKHTVDAY IVWALVESDP
DDQEKLDLKT EIATLKAEAL NENSAGGKDA YFVALVANVM LQRGDRETAH KLLDRLKEKH
FKNGAVTGAE TSITRSGGRD LEIEVTALAL LGWLRANDPA YGTAIKDATK WIAQQRGGYG
GFGSTQSTIM ALKALALFAK KNAHPSESGD LGMLVGGAAV CSRQFTEQDV EVIALDVPNP
EAIFKFGART ELEITTTAKH PYPIALSYSY TTLTPLSAEK CAVQISTKLA KNEATEGDTV
PVAVTLENRQ KQGQGMTMAI VGIPAGMRVP TDMKQLTDLR EKGQISYFET RDRELILYWR
ELAPEQKIAL AVDLVCDVPG TYRGPASRGY LYYDADHKHW VEPLSIKIAP MPETK
//