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Database: UniProt
Entry: A0A212PXV4_9CHLR
LinkDB: A0A212PXV4_9CHLR
Original site: A0A212PXV4_9CHLR 
ID   A0A212PXV4_9CHLR        Unreviewed;      1982 AA.
AC   A0A212PXV4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN02746019_00022130 {ECO:0000313|EMBL:SNB51925.1};
OS   Thermoflexus hugenholtzii JAD2.
OC   Bacteria; Chloroflexota; Thermoflexia; Thermoflexales; Thermoflexaceae;
OC   Thermoflexus.
OX   NCBI_TaxID=877466 {ECO:0000313|EMBL:SNB51925.1, ECO:0000313|Proteomes:UP000197025};
RN   [1] {ECO:0000313|Proteomes:UP000197025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAD2 {ECO:0000313|Proteomes:UP000197025};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) 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; FYEK01000003; SNB51925.1; -; Genomic_DNA.
DR   InParanoid; A0A212PXV4; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000197025; 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; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 2.60.40.3710; -; 3.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
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; 4.
DR   Pfam; PF17973; bMG10; 1.
DR   Pfam; PF11974; bMG3; 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   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1982
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012442727"
FT   DOMAIN          1052..1204
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1266..1356
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          1882..1901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1982 AA;  218965 MW;  4DDE6E8D5CB0AF56 CRC64;
     MRSTSRPWRR IGGAFILLLL LLDACRPAPT PTPTPVISRL PPVLVARTPE PGQEATPEMP
     LRLVFSEPMD RASVEANFRV IPAIAGRFAW EAGDRILRFI PQAPWKPDAE YEVRLENARA
     RNGQALARPV AFRFRTASPL AVVEVIPSPD ARDVDPRASV TVIFNRPIVP LRSDLAPGDL
     PQPLTFDPPI RGTGRWINTS IYTFQPEGSW EAGRTYIARV AAGLKDLSGV TLERDYTWTF
     TIRRPAVVDY TPRPGRAMDL DLNTPISITF NMEMERSSTE AAFALREGAE DGPAIPGRFE
     WISRTMVFWP AQPLKMETRY FVRLEARAAA PSGATLEGPL AWAFTTPAYP RLRSASLSPE
     GPNRLDTDSS IELRFSSGLI RPETIWPNLR FDPPISVTRV VTSWNPEGGE FIIYADWKPG
     AVYTLTVGPG IEDRYGNRLD RQHVFTFTVD HLDPLAYLNI GSPYTPIALV GTYTGTTAFL
     STRNLNRVDL TLARLSLASF VTMTQNPEAV SRYIAPPSQV FARWTFTVPE VITDVIMLNR
     IPLAGPGWPT LPTGLYHLRL DAPVSLQDRP ARYLIAATDL HVAIKVAPQE ALVWVTDLAS
     GRPVPGIPVQ LFEVVEERLE ARGSGTTDAD GIVRFTWAEP TPLWRMRVAV AGTPGGRFGI
     GASTWSDGIE PWSFDIPADY EPMRFRVYWQ TDKLIYRPGQ TVRFKAIVRV DDDARYTLPT
     TPILPIRIQD PEGREVYSAT LPLSDYGTAE GAFALAEEAL LGSYTLMADL PPGPYAHTIS
     FLVAAYRRPE FQVTLTPDRP AYVAGETIQA LLQATYYFGG PVADAKVEWT ARMRPFFFEY
     TGPGYFSWSD VDPYSAYEGE GEEVVASGSG TTDAQGRFRI RLPADLGKRT GSQVVILEAS
     VTDLNDNVVA GRTEAVVHAG RFYIGLQAER YVGEAGQPLT LTVRTVDWES RPVAGIPLTW
     TAYRREWFSV MQETDRGPMW TWTYSDTAIF SGTLQTDAEG SGRFAFTPPD PGTYVVKAEG
     IDGEGHRIRS AEFVWVSGRG TVAWRQENND RIELIADRRE YAPGDTATLL IPSPFSGTVT
     ALITLERGRI RRYEVRTLEG NAPTLSIPLT EDEAPNVFVT VLLVQGVTRE NPAPSFKMGM
     VSLPVKPVRQ QLRIELIPDR DVEAGAHYGP RETMTVTVRT ADADGRPVPA EVAVAVVDAS
     VLALVDPNAP PILEGFYARR PLSVLTGVAM VYNLNRVTVR IARERKGGGG GMEQAFGEIR
     REFPDTAYWN ARLRTDASGT ATFSVRLPDN LTTWRILAKG VTADTRVGEA TRDVLSTKDL
     LIRPSVPRFF VAGDRVTLGA VVHNATTRTL SVAVRLEARG LALESPAAQE GTIPAGGVAR
     FEWTGVVQPV EAVDLTFFAE GGGFRDATKP TLARPDGTIP VLRYVSLETV ASAGMLETAE
     PRLEIIAIPP EPEVVGGRMI LRLSPSLAAA TLDSLTWLQH FEYECTEQTI SRFLPNIATY
     QALIRLNRMR PELEEPLRQQ IAIGLQRLYA GQHADGGWGW FTSMGSDPLT TAYAVFALAQ
     ARAAGFAVAD EVLARGVSFL RRSLEAPADL PEWKANRQAF MLFAMAEAGA GDAGRIVALW
     EAQKDRLALY ARAFLAMALA RVQPDHPLIP TLQSAVLERA EVTATGAFWQ EQKMDDFNWN
     TDTRTTAIAL LSLLRLDPDH PLAFQAVRGL MAARRADRWE TTQETAWALM ALTEWMVQTG
     ELEGNYTWTV RLNDAFLGSG TVDPAHIQET VTLQQDIAGL LREVGNALEL SRSAGPGVLY
     YTVHLALEEP VERIAPRARG LTVSRQYVRA DDPCLRDRRQ PCTPVTSARV GDLLTVRLTL
     IAPRAVHHLV LEDPYPAGAE AIDPSLKTSP TAGRPPELQR VDPSDPFGGY GRWGWWWFGH
     AALYDDRAAL FANYLPPGTY EYTYLIRAGW AGRFQVRPAR AYAFYFPEIY GQSEGTIFEI
     TR
//
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