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Database: UniProt
Entry: A0A0Q5T189_9BACT
LinkDB: A0A0Q5T189_9BACT
Original site: A0A0Q5T189_9BACT 
ID   A0A0Q5T189_9BACT        Unreviewed;      2018 AA.
AC   A0A0Q5T189;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:KQS24839.1};
GN   ORFNames=ASG33_24140 {ECO:0000313|EMBL:KQS24839.1};
OS   Dyadobacter sp. Leaf189.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS24839.1, ECO:0000313|Proteomes:UP000051810};
RN   [1] {ECO:0000313|EMBL:KQS24839.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS24839.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS24839.1, ECO:0000313|Proteomes:UP000051810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS24839.1,
RC   ECO:0000313|Proteomes:UP000051810};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS24839.1}.
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DR   EMBL; LMPS01000008; KQS24839.1; -; Genomic_DNA.
DR   RefSeq; WP_056291573.1; NZ_LMPS01000008.1.
DR   STRING; 1736295.ASG33_24140; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000051810; Unassembled WGS sequence.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR   PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 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:UP000051810};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..2018
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006262371"
FT   DOMAIN          1249..1339
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   2018 AA;  229711 MW;  F54CBE615E7A6609 CRC64;
     MKTSYSATIL LSTLFLILNT MHANSQNPIK TYDANWKKVA DLQATGLAKS ALTGVREIYR
     LARQEKQDAQ VIKAAIAMVN LQSEFREDNE IAAIKDLEAE LANSSGVVNS IFSSLLASYY
     YNYYQQKRWQ LYQRTETTGF LKEDIDTWST TDFHHRIAEL YLASLSNENE LQQTKLEPFD
     AIITKGNARQ LRPTLYDLLA HNALRYFSSD EPELKRPGYA FEINSASAFD PAADFIHRHF
     ETKDSTSLEL YALKLYQKLI AFHMHDPVAD ALIDVDLARI QYVKQKSVHE NTDELYYLAI
     NHVANQYQQT PAAAQAWYLL AQYHFDLGTA YKIREDSTNR FAKVQAVSIC KEIIRQNPTS
     EGGVNAANLL SRIRQKALQF NAEQVLVPAK PFLIFVEYQN INKLYLRLVN STPSLLKDFD
     RRNSDAFWRT VSKATAIRNW EQTLPDTKDY QEHSVEIKAD ALPAGEYMLL ASSSPDFSDT
     QSIGGVRLLY VSNISYIQRE RDYFVLHRDT GQPLAGATVK RWDSAFDYQT RTYKKSLAAH
     YTTDKNGYFK ESMPSQSKVQ SESFEMLHGN DRLFIQESIN TYYNDEEEKE DAGTTIYLFT
     DRSLYRPGQT VYFKGIVAEG TSVLKDKTRK IEVKLQNANY EEVETVTKTV NDFGSFSGSF
     VLPGTSLNGE FSILADDDYS VSFQVEEYKR PRFAVSFDTL RNTYKLGDTI RVTGTGTAYA
     GNRIDGAKVV YRVVRNERFL YPWTRRASYF PLSPPKEITH GETVTDQEGH FYVSFEAIPD
     AKSDRNFDPV FNYTIYADVT DTNGETRSAE TSVSVGYKSL LIKAEIPERV SADDFTQLKI
     RTENMNGEFV SAEAKVKLTR LIPESRLIRS RYWAQPDMFV MTKSEFIASF PNDEYNNETE
     KENWPEQKVV FEKSQALTAD KELAFPGGKV AAGFYKIDIA ATGQDGDEVK DTRYIELTEE
     TNPKLLKPEY QWTKSGPAVE PGEKTNVQFA TSAPDVFLIS TSGRTENPAN FSFLKLNDEK
     RTFPILAKEA DRGGYAIDYV FVKHNRVHQA QNFVNVPWTN KELTIEYATF RDKALPGSKE
     QWKVKISGYR KGQVAAEMLA SMYDTSLDQF YQHQWTKPGH WPTGRTLNRW GNGINFTPKD
     ATIVNFLFTS EKAFEKSYDQ LIDPDIIRMS SGGGRNARYR RSLSMDQLSY KKGEMHEEEI
     ATSVPAPPML GDATRELQEV VTVGYGQTKP KSPAAEPEKT KVRKNFNETA FFLPDLKTDE
     NGAITFSFTL PEALTRWKFQ ALAHTPELAF GYSKKEIVTQ KELMVQPNAP RFLREGDQIL
     FPAKIVNLSD RTLNGNATLQ LFDPATNENV TAHFGLISNE KAFSITAGQS ATVDFNLNIP
     AGYHHALTWR VVAKAANLSD GEENTLPVLS NRMLVTESLP LTMRGSGKKE FRFEKLINSA
     NSKSLAHESV TVEYTSNPAW YAVQALPYLI EYPHECAEQT WNRYYANAVA SNIVSKSPRI
     AAIFNSWKTV DTAALASNLQ KNQELKSLLL EETPWVLAAK SESEQKRNIA LLFDLIKMKG
     ELDTYLAKLR EMQNESGGFP WFKGGHKDRY ITQYIVTGIG RLLQKKVIAE NRDINAIIEK
     AFPYLDRQIK EDYDRLIKNQ VNMQEYVPGP QQVQYLYMRT CFDDAPIETT AFDAYEFFLQ
     RARASWPKQS KYMQGLIALM LHRSKDAATP KAILKSLRET SISNEELGMY WKNTRSWWWH
     EAPIEQQALL IEAFHEIAGD SATVDKLKTW LLKNKQTNRW ESTRATAEAC HALLLTGNNW
     LVEEKAPTVR IGSEVIKPDN VESGTGYFKK AFESSVVNAE MGKIEVDISS SSNSKSPSWG
     AVYWQYFEDL DQITFSETPL KLSKKLFIQT NTDRGPVLSE VKEGDSVKVG DKIVVRIELR
     VDRDMEYVHM KDMHAAALEP VNVLSGYKWQ GGLGYYESTK DASTNFFFDR LRKGTYVFEY
     QLFVNHQGNF SNGITSIQCM YAPEFTAHSE GIRISIRK
//
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