UniProt: A0A2T7PJI4

Database: UniProt
Entry: A0A2T7PJI4_POMCA

LinkDB:  A0A2T7PJI4_POMCA 
Original site:  A0A2T7PJI4_POMCA

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Ontology (4)   
   GO (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (28)   
   InterPro (19)   
   Pfam (6)   
   PROSITE (2)   
   SMART (1)   
All databases (33)   

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ID   A0A2T7PJI4_POMCA        Unreviewed;      1306 AA.
AC   A0A2T7PJI4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=C0Q70_04858 {ECO:0000313|EMBL:PVD33601.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD33601.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD33601.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD33601.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD33601.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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:PVD33601.1}.
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DR   EMBL; PZQS01000003; PVD33601.1; -; Genomic_DNA.
DR   STRING; 400727.A0A2T7PJI4; -.
DR   EnsemblMetazoa; XM_025229497.1; XP_025085282.1; LOC112558811.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 6.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          332..514
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          304..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1306 AA;  143649 MW;  223A4C7D6B1FE5CB CRC64;
     MCLTATGEPT VPLSSVAVFA IKHAVEAARA EIGQDTYFTL NSPALVQHVQ TACQPDSCPG
     VFTQTWIFVN FSDIEMATLS SSQDIPPGLA GREEYGRTCI SCGFSMKLRL QQGASEGVTF
     TVNGTQLTVR DEFNPATSLN EYLRRTGVSR GTKQLCIEGG CGVCLVAVKL YEPVSATSQV
     YAVNSCLVQL YMCDGWEITT IEGLGNVRTG LHAIQKRLTK YNGAQCGFCT PSQVMNMYGL
     LQRNPTPTMQ QVEDAYDVSI CRCTGYRPIL DAMKSFASDA PPNLQGGMID IEDLNPKMCK
     KTGTKCEGKC DNKKDKKRCS SDRQEDSSSI PNVGARAVWF KPTTLQELYT LLHQHRTDNY
     RLVFGNSGFG VYKEIGPWMY DILIDIRGIQ ELYKIEFTPS LVWGANLTLT NIHDLCDKAR
     SNASLPYAAV FAEHIKKVAN NGVRNLASWA GNLMLKHKHP EFLSDIYTML DVVGTRLLIG
     DETGNRSQCT LKEFLSLDMQ GKVIEAALLP TYTDTNYYIR LYRVSQRLQA DHGHVIAGFN
     MKIDKTNNCT VLQRPTIVFQ GISGTLNRAE NTEAFLEGKQ LGDPQDVFFF FFADSLSMLN
     MELTPASSPL LASADYRRST AMSFFYKYVL DVCGDKVAQR YRSGGASLVR PVSSARHSYD
     TRQEEWPLNQ PITSIDADYL VSGVARFLDD LPLESDELHA TLVISTEGNA EIASLDAQVA
     LSLPGVLKFI QASDFPAGGK NSFSLFGPTP EEILSSGRVE YAGQPIGIIV ADDPQMASTA
     ASMVRVTYKN VQPPLLDLRT AINQKSFFPH QTDPVIRGDP DSAIRQSPRR LTGSVEVGDQ
     YHFHLESQSS RCAPNDTGGI DMRATTQWVD GTVKVVAEAL NIPVSSVNLE VERLGGAFGG
     KAFRNSIVSG ACALAAYIMQ KPVRLVLDLH TNMKALGKRH PVIADYEVGF TEEGYLNGIK
     ITYYSDCGHA DVDWTLVFLS MFIDSSESFI LVLYTDLFCT SFTCTSFDAV PSQFVFDTVL
     EHVAKALNKD PTDIRKLNLY QRGQANRWKK RGISLVPTRY GMGWSGGHYS VFVAIYNSDG
     SVAIEHGGID MGQGINTKNS STANANSVYT AGSMGSELCS MGVIQCCQRL KANMAPVRMR
     MPTAPWKDIV SECYRSGIDL SAHAFTNPFS EYQTRYSVYA AALAEAEVDI LTGQSQINRV
     DILYDCGESL SPEIDIGQVE GGFMMGVGCH LLEESKYDPK TGVLLTDGTW EYKPPLPKDL
     PIDFRVAFLR NAPNPIGVLR SKDSPALVEH VQKACQVTPD QFTFGN
//

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