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Database: UniProt
Entry: A0A2S8ESF0_9RHOB
LinkDB: A0A2S8ESF0_9RHOB
Original site: A0A2S8ESF0_9RHOB 
ID   A0A2S8ESF0_9RHOB        Unreviewed;      1832 AA.
AC   A0A2S8ESF0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=PAN domain-containing protein {ECO:0000313|EMBL:PQO22802.1};
GN   ORFNames=C2I36_11125 {ECO:0000313|EMBL:PQO22802.1};
OS   Rhodobacteraceae bacterium WD3A24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO22802.1, ECO:0000313|Proteomes:UP000237945};
RN   [1] {ECO:0000313|EMBL:PQO22802.1, ECO:0000313|Proteomes:UP000237945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WD3A24 {ECO:0000313|EMBL:PQO22802.1,
RC   ECO:0000313|Proteomes:UP000237945};
RA   Wang S.;
RT   "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL   Submitted (JAN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PQO22802.1}.
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DR   EMBL; PUHN01000036; PQO22802.1; -; Genomic_DNA.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000237945; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02891; A2M_like; 1.
DR   CDD; cd01100; APPLE_Factor_XI_like; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR   InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR   InterPro; IPR049120; A2M_bMG2.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR000177; Apple.
DR   InterPro; IPR041203; Bact_A2M_MG5.
DR   InterPro; IPR041462; Bact_A2M_MG6.
DR   InterPro; IPR041246; Bact_MG10.
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; PF21142; A2M_bMG2; 1.
DR   Pfam; PF07703; A2M_BRD; 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   Pfam; PF07678; TED_complement; 1.
DR   PIRSF; PIRSF038980; A2M_bac; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237945};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1832
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015782953"
FT   DOMAIN          964..1108
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1170..1259
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1832 AA;  194680 MW;  96BB841F5B024D41 CRC64;
     MVAFVNRCLA LVLAVLASGA PALAQEDSPV PARRAAIIDD MDYPGADLRQ LFDTTFPACL
     QACRDDDACA GFTYNTRNGS CFPKAGLGAP QPYQGAVSGR MIPTDPAVLS RAEALRERMD
     FLPASDFDAA RALAEELPTL YTANEWSAGD HAAAAEDALR RNAYAAAARS YGAALTVGDA
     ADHWLAYAEA TRRITGSDRA DERRMRARAR AAALNAALRA GDATLRAEAL VAFAVLLEPA
     GRGRDMIPVL RLAQEIAPGR RGAALLERAV REYGFRVVDH RVESDSARPR VCAVFSEPLV
     QAGLDYAPYV RVSTGGIAVE AEERALCVDG LAHGTRYQIT LREGLPAASG EVLARSVPLD
     VYVRDRAASV RFPGRAYVLP AAGDLALPVE TVNTDALELE LMRVSDRNLV RAIRDDQLAR
     PLSRWEEMQF SEEMATEVWE GEAEVGMDLN AEVTTRLPLA EVMGDLPTGV YVLHAAVPGT
     DPFDVPAATQ WFVVSDLGLS TMQGADGLHV VVRSLETADA RADVEVALVS RVNEVLATAT
     TDSRGYAHFP PGLTRGTGSD APALVTAEAG AGETVEDIAF LSLTDPEFDL SDRGVEGRAP
     APPVDVFLTT ERGAYRAGET VHVTALARDG DARAIEGLPL TARFLRPDGV EYARMQAGAT
     AAGGHVFEQE LGGGVPRGAW RVQIHADPDE PPLAEQSFLV EDFLPERIDF EMALPDAPIR
     PGDRPRLSID ARYLFGAPAA DLPIAGRVTL RPAEEGLADW PGFGFGRHDA DVTPARTVFP
     SGVTTDADGA ARIPLTLPEI ETRDRPLEIE VVAEISEGSG RPVERDLTRT LAPDAPMMGL
     RPAFEGGVVP EGGEAGFDVI ATGPDGAAVP ARAEWTLNRV RTRYQWYSVR GDWFWEPVTT
     RTRVAGGEIA LDGTGPARIA APVEWGRYEL VVARTDGDSH AAASTTFDAG WYAPAGVLDS
     PDMLELSLDS ESYRPGDTAR LRVVPRAAGT ALVSVLSNRL IDMQVVEVPE GESVIELPVT
     EEWGTGAYVT ASVLRPMDPD AGRNPARALG LAHAAIDPGP RRLEAEFEAP AEADPRGPLD
     VALRVDGMAE GETAWATIAA VDEGILNLTG FEPPDPEGHY FGQRRLGMGL RDVYGRLIDG
     MSGAMGVVRS GGDAMATMRR EAPPPTEELV AYFSGPVEVG PDGLARASFD LPAFNGTVRL
     MGVAWSRGGV GQASADVLVR DPVVVNASLP RFLAPGDDSR LLLELTHTSG PAGRMAIDVD
     APPALRLGDV PGQVELSAEG RARLSIPLTA QKPGTHRIAV TVTTPDGRRL DRRLTLPVEA
     HDPEIARTST LTLDPGETLR FGADIFEGLR PGTGSATLAA GPLARLDIAG LMRRLDAYPY
     GCAEQVTSTA TALLVMPELA ADMGIAGPDE ARTRIEAAID RVLTYQAPNG AFGLWRAGTG
     DLWLDAYVTD FLARARERGF EVPDTAFRAA MDNLRNRLNY APDFEEDGGP WAYALMVLAR
     EGAAAVGDLR YYADVKASAF DTPLAAAQLG TALAAYGDTG RADAMFSQAA RLAREGGDEH
     GGGWREDYGT PLRDTAGLLA LAAESGSGAV DRSALAQSLA EGLTSRRAAR GMSPQEAAWS
     LRAAGALTDA AADSGLAVNG APVSGPVVRM IEDTVRGGRP VTVANTGTGP AEVMLTAFGV
     PVTAPPAEGR GYRIERSHYT LEGEPITLES VPVGTRVVTV LRVTPLGTGG GRLMVDDPLP
     AGFEIDNPNL LRAGDIAALD WLDLDDVAEH TEARDARFLA AVDWREDESF RLGYIARAVT
     PGSYRHPAAS VEDMYRPMRR AITDTGRATV VE
//
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