ID   A0A3S0QV89_9SPHN        Unreviewed;      1940 AA.
AC   A0A3S0QV89;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 11.
DE   SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:RUN75835.1};
GN   ORFNames=EJC47_14010 {ECO:0000313|EMBL:RUN75835.1};
OS   Sphingomonas sp. TF3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN75835.1, ECO:0000313|Proteomes:UP000275325};
RN   [1] {ECO:0000313|EMBL:RUN75835.1, ECO:0000313|Proteomes:UP000275325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF3 {ECO:0000313|EMBL:RUN75835.1,
RC   ECO:0000313|Proteomes:UP000275325};
RA   Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT   "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL   Submitted (DEC-2018) 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:RUN75835.1}.
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DR   EMBL; RWKS01000015; RUN75835.1; -; Genomic_DNA.
DR   Proteomes; UP000275325; Unassembled WGS sequence.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
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; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000275325};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1940
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018732977"
FT   DOMAIN          1022..1199
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1260..1350
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          815..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1940 AA;  205799 MW;  E0C48AF3A7EC1FD1 CRC64;
     MKLAFRVALL ALALAPITAF GDSSPQVILA TPGIGDGAIE RFTARFSQPI VPLGDPRAAS
     PFDVTCAVSG QGRWVDPQTF VYDFANGLPG GTVCKFKLRS GLKSVSGYAV TGQQEFSVDA
     GGPVARAVLP SQYDSEIEED QVFLVAANLP ATPASVAANA YCAVKGIGEK IPVEVLAPDL
     PGKLLGEMGT ENWNVRNFLE SAGLPATIPA AADRAKAYAG VTALKCRRPL PPGTDMALVW
     GANIAGASGK IAGTDQRFDY TVRKPFTARF ECGRVNAQAG CNPVEKAWVR FSAPVASDLA
     RQIRIQTADG KLLTPTLFDD SSEDSGHGDA KSKATVSSIG FKSPLPESQT AKLLLPAGVK
     DESGRPLANA ERFPLDVRFD AAPPLVKFAA PFGILESKQG GVLPVTVRNV EPALQGTNLS
     IAGQSLRIDG SDGKIAEWLR TVGHADDTAS HEETRGKDKV RINDTGATSI LGKQGASLKI
     GLPGKGKDFE VVGMPLGGGK PGFYVVELAS PVLGQALLGR KVPRYVAAAA LVTNMSVHFK
     WGRARSLAWV TALDTGKPVA GAEVRVSDSC TGEVLARGVT DKSGGVYAPP GLPEPETWGS
     CEGTSSHPLM VSARAADDFS FTLTAWGEGI RPYDFDLPYG YQARGEMLHT VFDRMLVRQG
     ETIHMKHILR TSIADGFGMA PAVSGTLRLQ HRGSDTQFDL PLTIDANGIG ENEWTAPAGA
     PMGDYDLSVI VDGRRIETTQ SFKVDEYKLP TMRASVTGPK DPAIRPANLL LDLFVGYLSG
     GGASNLPVDM RIGYFAHDTK PDGYESYSFG GKAIAEGTKP LNGDGEEEQT ALPPTQTLPT
     TLGGDGTGKQ TVAVPQTLDG VTDMLVEMDY QDANGEMLTA SKRIPIFPSA VQLGVKTDGW
     LMKQDDLRLR FVALDTSGKP IANQAISVAL YSRQILTARR RLIGGFYAYD NRMKTTKLAQ
     SCTATTDAQG LATCKIAPGI SGEVYAVATT KDANGNEARA TQSVWLAGND DWWFGGDNGD
     RMDVVPEQQA YKAGDTARFQ VRMPFRKATA LVTVEREGVL SSFVTELSGT DPVVEVKMPG
     SYAPDVFVSV MVVRGRTESG FWTWLHGIAQ SVGLASSPPE GQEPTALVDL AKPSYRLGIA
     KVKVGWEAHQ LQVAVKADRA RYAVRDVAQV DVAVKTPDGK PARTADVAFA AVDEALLQLA
     PNDSWDVLTA LMGERPLSVL TSTAQTQVVG KRHYGKKAVE AGGGGGGDSS GLNRENFQPV
     ILWKGRVALD ENGHARIPVT LSDALSSFKL VAIATDGAQL YGTGMTSVRT AQDLSIYAGI
     PPVVRTGDFY ASSFTLRNGS DKPMTVTATV DLTPAIAQGK PLTVTIPAGG AVPVAWNLTA
     PANIDRLRWH VSAKASNGKA VDQITTDQAV VPLYPVEVWA GTLARVGADT TIPIQPPAGA
     IAGRGTVDIR LDDTLAPPLA GVREFMARYP YDCFEQRLSR AVALGDAGLW QSLAGDLPAY
     QADDGLLRYW PSGSLTGSEA LTAYVLAMTS DAGLPIPAGP RAKMIEGLKA VLDGRLRHED
     YGDVRWQRVY AFNALARAGA ATPAMLGQLS MTPKEMPTAL LADYLVSLDH LQGLANGAAL
     KSAAEAVLRT RLVYEGTRLD LSDSSNQPWW LMSSGDEASI KTVIATLGRP GWQDEAAKMM
     VGVALRQSHG RWDTTTANAW GTIAARKFGA LYPASAIIGT TTLGLGTQTI SKSWPLAATA
     RTASFALPTT QTPLKLAQSG GAGPWATVSV SAAVPLTKPL FAGYEMQRRV EVVQARTKGV
     LTRGDVVKVT ITVKASAERN WVVINDPIPA GATIIGDLGG QSQILAGQAQ AGPGTKFEAR
     DADGKLWDIQ VGVVPAYVER RNDTWRAYYG WVPRGAFSAS YMLRLNGAGR FNLPPSRVEA
     MYSPAIRAQL PLDTMTVVQR
//