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Database: UniProt
Entry: A0LH86_SYNFM
LinkDB: A0LH86_SYNFM
Original site: A0LH86_SYNFM 
ID   A0LH86_SYNFM            Unreviewed;      1628 AA.
AC   A0LH86;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:ABK16788.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sfum_1095 {ECO:0000313|EMBL:ABK16788.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16788.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16788.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA   Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) 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; CP000478; ABK16788.1; -; Genomic_DNA.
DR   RefSeq; WP_011697959.1; NC_008554.1.
DR   STRING; 335543.Sfum_1095; -.
DR   KEGG; sfu:Sfum_1095; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_002018_1_0_7; -.
DR   InParanoid; A0LH86; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000001784; Chromosome.
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   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF01835; MG2; 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:UP000001784};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1628
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002626218"
FT   DOMAIN          696..842
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          903..993
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1628 AA;  178711 MW;  E9CFD269ECEB6B8B CRC64;
     MKIERLVFLF AVLGLLLPVV AAPPAHAGSP FYLTVDRSFS HNEKPQLRID YTDPSKPMLL
     RVLRPKDLDR FLDGQFNVSR SYERPVSQLN PGHYFVKGLN QAESPLKTWR GMLSAEFRKN
     FKDTAFNKAL LDTTPGDLAA PPHQVVHGPP TGLGVVREYY VDLEHAGTDA KDIGWWFADS
     GWQERSYKVR TIALDPLPDG VYLIQAVSGT AEGQCLMQVS SLAAQVKQST EQLVVRVIDR
     EQQPVRGAAV SYRDGRGKWI DVGRKTDGAG EVFFSNPAGN LDGKLLVRAQ TGDGRQALTD
     TDFLPAVSND DSVFIVTDRP IFKPGETFFY KGMVRALANG ELKTPDFAGK QARITLVRSD
     GKDTGLQAAV PVTDFASFSG SFGLDEAQTP GLYRLIAELE GKPYGGEFRV RDYVKPVFYM
     ELIERSPTVV PGEPFAVKFR TRRYSGGVPR DVKYEVYLYQ KKFEAPQWVA EAGGGLGTGT
     DYFGQVRSAS ALTEPRRIYS SVEERLADAA REYGMNTWDS APLIDESGET SFSFTVPKTD
     SAAQGEWIYT VMVRALDRAG SQAILTENIY MTVSEAQPSI RFSKTIAQVG EKGLTVSVRS
     TYPDGKPAPN AGGVLDIGIE RGGDPAAGFV KLPFTTDARG NRDIELPELT GRGRLRAVAT
     LETLDGKPMK HPAASQPVAM VVGGAQGEAV LDNRELELYT AGTILSPGEK AKVFALLPGD
     WGRNGKGTVW ETISGRKIYG VNSRECQGRS WWFEVEARPE YGTGFYHTVT VPVSGGKYRE
     QTLGFRIIPR AKRLTVDIRP EREEWEPLKP FRIDLEVKDA EGRPSPDTEL TVTIVDRAVY
     AVQSELRPGV FDFFYPLPRL NLATFYSDEL QGYGYADLLK KPNFSLGALK SRSKLPKKAM
     RDTAGWFPHV VTDGMGRASI TVDLPANVTE WLVTAIAADK TGRVGEATGR FRTVTDILRE
     VIAPQFLRLG EEALVHLKTV NQADRTVSLK TRIELDGGVS LKQGRQEEEF TIEKQGERLS
     PLVLEAAGGQ GTATLRVASE AREDIHVGGA EEFDIPLRPA STRLVFPGVA DKDRLIARLP
     KAGKVGEVKV QVVSGLLGAA LNAAAVLVAY PYGCTEQLVH STVPNLVLMD LVRRAGLTRE
     DLGPLADVLS RAESNAVFGI RKLIRNQKTD GGFGLWPADP EPSIGVTVTA LYALKFAGDL
     KVEGAQGAYF KALDWLRNAR RAPEYRRQGG TVVGYELARL AELRFYDSQF EEQIAYVENL
     LGDKTVPVPD LVNGLALFAG YRKNSWYRFN ERFKDSGAME ELIEKLKKAL EAFDPDVYLK
     AAGEDWEAID SLGFGFGVPS IVSAAMGVME ELDALPQELE AKLTRILLAR MKNGYWTSTF
     DTAQVIFNTR KILEKQARAV AEEAKTGRPA LVVRKADGQV LGELARIPAG FVGTFADPGT
     PEQVSELRLE GLGPTDSAYS ATAVDVPYEA TAPGSTGLSV ERTFRRITPG GSEPLDLSRP
     LRKGDTVVSE IRVRRNPVEE VTYIPSRFLV IEDSVPSLAR PVDDDRVALA DAGIRLENET
     YWGLVMDTQR HPDRTVRIAK VLPRGEITIY QVWQAAFGGT AAVPPAVAFD MYDESVRGNT
     GAGRIRVE
//
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