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Database: UniProt
Entry: A0A1Y0MNK4_9FLAO
LinkDB: A0A1Y0MNK4_9FLAO
Original site: A0A1Y0MNK4_9FLAO 
ID   A0A1Y0MNK4_9FLAO        Unreviewed;      1847 AA.
AC   A0A1Y0MNK4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTO09_06220 {ECO:0000313|EMBL:ARV11962.1};
OS   Gilvibacter sp. SZ-19.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gilvibacter.
OX   NCBI_TaxID=754429 {ECO:0000313|EMBL:ARV11962.1, ECO:0000313|Proteomes:UP000196054};
RN   [1] {ECO:0000313|EMBL:ARV11962.1, ECO:0000313|Proteomes:UP000196054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ-19 {ECO:0000313|EMBL:ARV11962.1,
RC   ECO:0000313|Proteomes:UP000196054};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-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; CP019333; ARV11962.1; -; Genomic_DNA.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000196054; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; 2.60.40.3710; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
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; 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; 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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000196054};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          986..1128
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1192..1282
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1847 AA;  205649 MW;  150D1FBEDAF1479F CRC64;
     MKSLFRASLV LLLLATACKP KSTQNDQLFQ YRDYLSYHTQ GVRSVHAPIV LDFLRPLANF
     DAQAQLPASS FKIRPSVTGT LKISNGRSLI FTPNEALKAD TEYSVTVNLS DFLEDLPDDK
     RQFTFSFKTI APNFKVDLGQ LQSYNKSYQF LQGSIQAADG LYLNQARELV SVSQGGAQLA
     VKWDSLGGPN KYYSFVIDSI ARAENDSEIQ IRWDGKAIGA DNKGTAPFVI PGRNNFTVLD
     VNTSEAPSTR LTINFSDPVD PDQDFRGLVN LGGNDNLRFE ADGNSLLIYP ASRPQGDLDL
     VVFAGLKNTD GYALKNSYSD TVTFDPLKPQ VNLLSKGTII PNAKNNPIYF ETVNLAQIDV
     RVVEIFQDNL LQFLQESSLN NSSDYYLRRV GRRVAKKTLQ LVDTNMVSAN SWKAHALDLT
     ELFDASPGSV YRVEFSFKPE YSLFACESIL AGEENEYEDE YYGDYASDND LESADEDALE
     SRYWDNEIYR WRSYSYNWQE RDNPCHPAYY NEDRIVQSNL MASDLGITVK AGNNGTYHVF
     TNNLISSEPM GGVKVSLYNY QQQVIASRTT NAQGQIVFDT DNKAAFVVAQ KAANYAYARI
     DDGMALSLSK FDVSGGQVQQ GLKGFLYTER GVHRPGDSIH LTFVLNDAAN PLPEDHPVKL
     ELTDARGKLV ERRVVRGSVD GFYYFPLTTA AEAPTGNWNA TVKVGGASFG KTLRVATIKP
     NRLKVQLEFE KAVLEADRPI SGALKSTWLH GAPARNLKAN VSLTLAESSS PFKDFTNFNF
     NDPVRTFSTS EFNFLDADLN SEGAFGFKEQ LQLSDKAPGM LQASFVTKVY EGSGDFSIDV
     INKPLAPYAH FVGLKPPKLG RYGSFETQRD HRFELVTVDA QGKASGNRKL TVEVFEISWR
     WWWNRGRDNL SRYENSSVYR PVKTFEITTG SNGKGSFDLN IPDEQRGRYL IRVKDPVSGH
     ATGMTTYFFK DWWQTGQAGS ESAKMLLFSS DKDTYNVGEQ AQIRFPSSAG STALISVENG
     TEVLHYQWVK TQQGNTELSL DITPEMAPNV YINISLLQPH ERTKNDLPMR LYGVVPIMVN
     NPKTELSPQL QIPSELKPET DYQVTVSESN GKAMTYTLAV VDEGLLDLTR FSTPDIHKAF
     YARQALGVKT FDIYDLVMGA FSTQVDNFYA IGGGDAAAGA KNRKADRFKP VVSYLGPFKL
     DPGQSATHTL TMPNYIGSVK TMVVAGYNQT QAYGKTEVVT PVRTPLMVLA SVPRKLSPGE
     KLTLPVTVFA MDPKVKQAQV SIETSSGLKP TGSATKTVRF DSPGEQIVNF EYEIQASDAV
     QNIKVLAQSG SHKASYPLEI DIYNPNPISR TSKTYTVEAG TQKQIDFATF GTAGTNKVTL
     ELSTIPPMDL EKRLDYLIQY PHGCVEQTTS GAFPQLYLKD LVALSSTQAR RTEENIKAAI
     RRLGQFQNTS GGMGYWMGES QSSDWGTSYA GHFLLEAKQQ GYTLPIGFLS NWTRYQRLAA
     KQWRKSSQSY NTTHAQAYRL YTLALAGQPE LAAMNRLRKS GGLTNAALWR LAGAYALTGN
     KSAALELLEK ATLKFENQRY SWYTYGSALR NMAMALEIMT LLQDENEREM ALSIAAQLSS
     ERWLNTQETA YSLLALGKMV KINGGKSFSV SLNQNGQTTA LSSEKSILLQ ELSFVMGDNS
     ISLNNTGESR IYASLIQQGR YPMWAEKAAT KNLSLRTDFL DKEGKRIDVA ELRQGTEFNI
     RINILNNSND DLRDLSLTQL VPSGWEIVNT NFTAAVQGHV NPARYTDIRD DKVNYYFDLR
     SGKSKTFELV VNASYLGRYY LAGTHSSTMY SDNYYARTQG QWVTVKQ
//
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