ID A0A2S7WSS1_9FLAO Unreviewed; 1853 AA.
AC A0A2S7WSS1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN ORFNames=BTO18_14785 {ECO:0000313|EMBL:PQJ80362.1};
OS Polaribacter porphyrae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1137780 {ECO:0000313|EMBL:PQJ80362.1, ECO:0000313|Proteomes:UP000238882};
RN [1] {ECO:0000313|EMBL:PQJ80362.1, ECO:0000313|Proteomes:UP000238882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108759 {ECO:0000313|EMBL:PQJ80362.1,
RC ECO:0000313|Proteomes:UP000238882};
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}.
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:PQJ80362.1}.
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DR EMBL; MSCN01000001; PQJ80362.1; -; Genomic_DNA.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000238882; Unassembled WGS sequence.
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 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; 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; 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:UP000238882}.
FT DOMAIN 990..1132
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1195..1286
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1853 AA; 209613 MW; B40DEBCA2B63BB59 CRC64;
MKTKYILSAF VIFLLISSCK KEKIKTDNIY KFKEYISYTT SGEVSISQNI EVNLAKEVEG
WETNQEISAE ILFIKPFVNG TIKTINKHAF VFIPDDRLQP DTEYAITVKL KDIYKNIQKG
YENYTFQFKT ITPNFKIETN VLQSYSKDYQ YLEGIVKSAD VININDVKQL IKATQEGLSK
NIVWNEANTT SKVFEFKIDS IQRFVEDSKL KVTWSGKAIN SDNEGENEIT IPGKNNFKVL
SIGISNTAEK FISINFSDPL KKQQNFNGLV SLKGVKSPRF IVNGNQLKVF SNESFQGSIL
VSVFEGIKNS SNYKLKSAFN EAITFEQKKP QIRAISNGTI LPNSKDLKFN FEAINVRKVD
VRIIKIYEDN VLQFLQENRI NSDNEYDIKR VGRRVAKQTI TLIDKKENNT QNWKAYSVDI
SKMMAAEPGA IYRVELSYTK NQTFYTCGDN DNTETSSEEE KYYEEDYEEY DDYSEVEDQE
VREELYWDNK LYSYKNYSYN WRERDNPCND AYYSSNRMIA QNVLASNLGI IAKKGEDNTY
FFAITNILTT NPELNATVKL YNYQQSEIAN GITNSEGFVT VKSDKNVAFA IVSKGNNKGY
IRLFDGNSLS LSKFDVSGSE TQKGLKGYIY GERGVWRPGD TLHLSFILND ADNKLPKNHP
VKLEVTNPRG KLVYKKVTIQ NVNNFYKFTF KTNTEALTGN YSAKVAVGGA KFYKNLKIET
VKPNRLKIKI DFDDEILSSK KPINGTLDVK WLHGTPAKNL KAEIKAKVSS SNYSFESYKN
YVFSDPSRSY ASEEINVFEG KVDENGFAKI SSDLKVGKNA PGMLNVQFLV RAFENGGDFS
IDAFSKKYAP FSTFVGLQSP EGNRYGSFFT DDNQEFSVVS VDENGKPVQR DEIEVEVYQI
QWRWWWSSSS DNLSKYTSST YHKPFKKIQL KTNSEGKATF NLNIPDRNRG RFLIRVIDKK
SGHATGRTAY FYKNWWQNAD SGNKEAAKML VFAADKEKYN VGETAKITFP SGSNGHALIS
IENGTKVLQT KWVQTQKGKT SVEIPITKEM TPNVYVNISL LQPHQITEND LPIRLFGVVP
IFVENASTRL SPEIKMPKVL APEKGFTVKV SEKNNKAMTY TLAVVEDGLL DLTRFKTPNA
YNTFYAREAL GVKTWDIFDD VMGAYSGSID QVFAIGGDGS LAKGKNRKAN RFKPVVKFFG
PFTLDKGTTK SHKITLPNYI GSVRTMVVAG DIKTEAFGNA QETTPVQKPL MVLATLPRKL
VPKEKVILPV TLFAMDKKVK NVAVQVKASS GIQVVGNATQ SISFEKPDEK MLYFELDVLK
ANGFNTVEVI ATGNGEKSTY KVELDISNPN PITNKIIDKT IQGNQSKDIT FNTFGVAGSN
GAKIEFSTIP AINFTGRLEY LIQYPHGCVE QTTSSVFPQL FMNDIFDLTS KKKREIQSNI
EKGIKRLGNF QKANGGLSYW LGENYISDWG TTYAGHFMLE AEQKGFVLPL TFKSNFIKYQ
KQAARNWRQK YNRYTSDLEQ AYRLYTLAFA GSPDLSAMNR LREFKKLSND AKWRLAAAYA
LVGQNEAAAE IMAKATLNFS EYQYYNYGSV TRNKAMALET MLLLNNQNAK DIAKSIAKKL
SSNSWMSTQT TAYSLLAIGK MVVKNGGKAI DIKFTNDGKT ERLKTSSAMI QRTLTIQKGT
NTITIQNQQN NVVFARIINS GKLPLGDEIS ERRGLSFALN YVDLKGSKID VNQLKQGQDF
VAKITVSNPK NETVKDIALT QIFPSGWEIV NTRFTDFGTT AKSTARYTDI KDDRVNFYFD
LNYHQNKSET KTFSVLLNAA YLGDYYLPGV QVEAMYDNDY FVRTKGKWIK VVK
//
