ID   A0A133YIL8_9BACT        Unreviewed;      1854 AA.
AC   A0A133YIL8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Alpha-2-macroglobulin family protein {ECO:0000313|EMBL:KXB43038.1};
GN   ORFNames=HMPREF1870_01427 {ECO:0000313|EMBL:KXB43038.1};
OS   Bacteroidales bacterium KA00344.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB43038.1, ECO:0000313|Proteomes:UP000070254};
RN   [1] {ECO:0000313|Proteomes:UP000070254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-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:KXB43038.1}.
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DR   EMBL; LSCT01000120; KXB43038.1; -; Genomic_DNA.
DR   STRING; 1497954.HMPREF1870_01427; -.
DR   PATRIC; fig|1497954.3.peg.1448; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000070254; 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   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; PF17973; bMG10; 1.
DR   Pfam; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070254};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1854
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007460398"
FT   DOMAIN          1108..1198
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1854 AA;  208937 MW;  B032DBF6F06F688A CRC64;
     MKKVIYLLIL LLMPASIYAE SYTSLWKKVA EAQSKDLPQT EMECLGRIIS KAENEKQYGH
     LLKAQLQQAA VQTQISPDSM TIEIDRLVQK AENAKDEVLR AVYASVLGKV YQQQEDTDAE
     QKSKMWFAKS MANPKLLAEH KSEEYSPAIA EGIDSKIFYD DLLHVIGFEA EDYNTLHQYY
     SQSGNRAAAC ITALCQLREN SDENVMDARK SKYLQKVDSL INVYGDLREA GELAIEHYNY
     ISECEDSKAE DRINYINYAL SRWGAWPRMN ILRNAQSELQ RPAFNINIGD YMLLPDTERE
     VRINSIRNIN ELNVSLYRLN VKGNTELNPD NKEDYAKLQK LILPGIVQNV TRKYIGQPAW
     KENSDSITLK GLPIGVYLME ATTDNKDIAP QRTLLRVSNL YVMHEGQPDK RIRFVVVNAT
     TGKPVPGAHL VLSSKWGDRY EKAKKINLTS DKNGEIIHRC DGRTTYQIYA YTNEDHACGN
     FDINGYYSHW DGNTVQQILN VYTDRSIYRP GQQVHVTAIA YETNSETLRS NAIGSRKITF
     SLCDANGKEV ITKDVMTDDY GTAATTFSLP QNGLTGRFSI YAKGERLFGG ISFNVEQYKR
     PTFQVRFDAY NEKYTPGDTV QVRGRVESYA GVPVQGAKVE YTVERRRSIW WYWRIDESAP
     TLITDSTITA DDGTFTAKMP MLFPDDIEPG MPLYYNVVVN AKVTDGAGET HEGSFSLPLS
     NKSAILLCDM PKKSLRDSLK TFTIIRKNIA GENIAGTIRY QIDGSAWKTA AANQQISIDR
     KLASGKHRIV GICENDTVTH DFIIFSYNDK KPVVETHDWF YISGNRFSDD GKPVYMQLGS
     SDEDVNIYYS VFTGDKILSQ GRKVLSNSVM TEKLTYKEAY GDGITVNIAW VKQGRLYTHN
     FTLERPVPKK ELTLSWKTFR DKLIPGQEEE WTLQILGPDG KPSKSQLLAT MYDKSLDDII
     KHHWDFTVNF NLELPYVQWY GGSNETLGLY GFQNFKSLAE HPLKFSHFDS TMFEFAAPLI
     SLYTRAEALG KLSSPNVRIR GSKTLAKVAM EQDAEVLADS TIDNADMNVS SDQTSEMKKS
     ENTEVTEQQY GKNGQDGAIL LRENFNETAF FFPALLADSQ GNVKIKFTLP ESVTTWHFMG
     LAHNEQIDYG MISADAVAKK TVMVQPNLPR FIRMGDKANI SSRIVNTSDK NITGTARLQI
     VNPETEVVVC EWSKPYAIEN GKTGHVDFSV DGDNIAALGK GAELYIVRIT AEGDGYSDGE
     QHYLPLLPNR EYVTTTVPFT QNGPGVKTID LSKLFPTNSA QNKLTVEYTN NPVWLMIQAL
     PSVANPYEKD AISLAAAIYA NCIGYGIVKS VPKIKQTIKL WQQEQGKETS MMSNLEKNEN
     LKTMVLSETP WLAVAEKETD QKHQLINFLD ESTIGYRTDN FIQKLRSLQN ADGSFSWWPG
     MHGSAYVTIA VTKILTRLNT MMGTVQATSG ILDNAFEYLD RRIAEEVTEL KKQEKKGEKN
     LIPSELACNY LYCNALANRK ETKNMTYLVG LLEKMPTKLT IYGKAGSAVI LAQYDRKQRA
     GEYLQSVGEY AVYTEEMGRY FDTPRAQYSW SDHKIPTQVA AIEAMKLIKP NDSKTIEEML
     RWLLQEKRTT GWNTPINAAD AVFTFLTDEH SKIDKDKLSS GEQTTLKIDG QTLALPQATA
     GLGYVKTSAF DGNNTTFTAE KTSNGTSWGA LYAQFWQENT EVKSASSGLT VRREIISADG
     KKNATRLRVG DKITVRITIK ADRDYDFVQV QDKRAACLEP VGQISGYHWG YYCSPQDNVT
     SYYFDRMSKG THIVETQYYV DREGDYTTGI CTAQCAYSPD FSAREAATRL HVVK
//