ID K2AX07_9BACT Unreviewed; 2186 AA.
AC K2AX07;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACD_49C00060G0068 {ECO:0000313|EMBL:EKD66226.1};
OS uncultured bacterium (gcode 4).
OC Bacteria; environmental samples.
OX NCBI_TaxID=1234023 {ECO:0000313|EMBL:EKD66226.1};
RN [1] {ECO:0000313|EMBL:EKD66226.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD66226.1}.
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DR EMBL; AMFJ01021646; EKD66226.1; -; Genomic_DNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1210..1357
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1423..1515
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 2186 AA; 257744 MW; A832FBC331F061C3 CRC64;
MQNFKLFFDN LVISAKLKLK NKKVLYLSIW VLVIMLWIWW YYLSDFLSKR LEVPQVIWAN
FSIEYRKIPF DTKTLEVSFS TDLRSDSINN KTISLSPFIE WNTTLKDGNT IVYTLKSNLE
IGQEYSFTVN ENTESKYWIK IWKPFSIIFE AISGAKVTKI FPEKTLDNIS QNLLVLFNIP
LIPLTSLDNK DNLPCPVEIT PKIAGKCRWT GWNVVEFVPE KYWEWATEYK VSVKSDDKFL
YPLKETKEIS FRTPNLTFKT DENFSPKNWI SLVANFPVNP TDIEKSIDLK NWNNKINVKL
EPVEWSETRF AIKPINWNFN YNKSYTLAIP AWISPKYWNI PTKYLISNTS ISSAYLSSIE
VYQNALSSTG AIEDTPLFSD TTKIPTKNVF FKLYFEEEVA LNESLFSFTW KGKQTPFSLK
YGIESIYENG KTIDKESKKI VILTLKNELD YDSDYDLKIL KKANENLDKD EIHSFKTVKA
FKIADFKYID NTLACVYLTN DLFSQSENSS YYDYTYWDKK DANQTQIKLT PNAPVRSIAR
DIKNYETNKY ICPQKSGLIS YLLNFRLAPF TSYGVSVLSG LKDDFGNTLD KSYSYNIKSG
DIKESDKYLY SSFSKIVNVI PSDLPTVIDI QSINLNKASL EVCEMNVIWY NDYLTRTSDT
NFKPKCIQNY NWEITLKNKN WTLSHNRFDI EKDVIWTKII SPIYLITGRI WAKNEGIYFE
NIIIKSNLSL TLENAWNKNL LFASSLDGKD IPSDISFEWF NINSSNNLTS AWKIKANWIK
DKKVYEIPWF YNIIVAKSDK YYWIINTSSD ATSNYDFKYI SGLDSSTSDF LYLYTERPIY
RPGDTVFFKW ILRNFNFDWY HKSDTKKAKL KILDAEYNFF KEIEVSVDKN SNFSGKFELP
RDMKLGRFNF EFYPNWSQIS VYNDWNFFVE EYKKPVFKIN LISDKKDAVI WENISLNFDW
EYYFGWKLNW AHFYKWVLTQ NYFFDAKDYS DYQFSTWFDW FNCVYWGYCD YGDETVFSEQ
WDMKAWEASI WNYSFPTDTA DENKEALWEK IYSFSVTLED PDTKKQVSKT TEVILHNTDA
YVWVKAPYYS VQKDWIKFDG IVLNYSAEPL SWKKVKVELI KKEWKNVKKQ WVDGIFYNDY
AIDEKVEDTK EYSSSSNWEF SDTLMPKTSG EYDIKTTYTW SNWKTFVSST SVYIGWEEVF
YWWDWNNSVT DLVADKSILK VGDTANFTLK SPVSTWKMFV TVEKDNGILD YFTQDIKSTG
ERISIPIKDT YYPNFYVKVF LIWKSWSNPL PIYKRALSVV KVVTDYKKLK VSIAPAKNHY
KPGEKVILNI KTTDIDGKPI PYANGSVSIV DESLLALKWN PKKNPFAFFY EMKRYLGVNT
YLSLLNLVEK LEIKDISDGE KWWAWEWAKW WDSKKKRWVF KDTAFWQADY TTDANWKATI
TTDALPDNLT TWVIESVAST PLDNKIWVWE ATIVTTQKVI INENVPRFLG SNDTIVLSPV
VFNKTGKNSI FTVSLTWENI DIENSSQEIK INNWEQKTVE FRVKVKDIWV SSLTNPTSKL
TIKAVSKDTQ DSDEIEKFLP IEETSTKETV ATVGKTDKVS YTEKIDLTNT ILSSAKLTIN
FSPTILSNIT SGIDFLANFP YGCIEQKQSA ILPNVYIKKL YTSAWLPFDL TKKMVKVWVD
GDTWYKNISE DEIIKNFIAE SITFQKNSLW FWYWTNEPSN APADFHLTSM VVDGMSEIKS
IGYTINDKSI KSAVSYLKTR FYANKIEWCS NPDYYNNFCK YPETERLDVI SAILSYDPND
YEAYKMWKLL DTKKEELSTK ISKVDVIAKL TKNKNISEWD KKTLKTQAVE LVNNMIWEFI
VYHPRWAFLW KDSYNSRILN TTNFIGAVSN LWLDNFKDIS QIIDNMNRWI ISEKKDWSFG
STQENNYAIK NMTKYIVSSG ELKNIKSNIK LLLNSDLIDE KNIDDKNKLE IFTKIIEWNK
LKTQNDFVIN KQWNWSVYYD LSLSYFLPIE KVIPRDEGFY LEQTYFDYNA YRKIENLKNL
EWVNYMSWTI DYKDLKYPKN TTEYLNEVRD FKVGQLILAY NKVVTAEPRD QVAFEWFIPA
WCELVNTNLS TENKSLKFTN FFDREEFRDD RYFGFASRMD SWLYEFNYVI RITHKWDFNL
KPSQISEFYK SEVFWRNKGK LIGVTK
//
