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Database: UniProt
Entry: A0A2T7PZB5_POMCA
LinkDB: A0A2T7PZB5_POMCA
Original site: A0A2T7PZB5_POMCA 
ID   A0A2T7PZB5_POMCA        Unreviewed;       558 AA.
AC   A0A2T7PZB5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=C0Q70_01372 {ECO:0000313|EMBL:PVD38749.1};
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:PVD38749.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD38749.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD38749.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD38749.1};
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   -!- 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:PVD38749.1}.
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DR   EMBL; PZQS01000001; PVD38749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PZB5; -.
DR   STRING; 400727.A0A2T7PZB5; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 3.30.390.50; 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; IPR016208; Ald_Oxase/xanthine_DH-like.
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; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SMART; SM01092; CO_deh_flav_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; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023014};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          224..408
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          185..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  60586 MW;  CB5D76335AC3E763 CRC64;
     MACILPPNSV AGDGERWTAR SSLNEYIREA AGLSGTKVMC RESGCGCCAV TVTIPNPLGS
     NLSTVSINSC LCPLLSVDGW QVTTIEGIGN DKEGFHPIQK RIADFNGTQC GYCTPGMVMT
     MYGLLHSSSQ PTEQEVENNF DGNICRCTGY RSILDSMKSF AKDTSIAGGG LIDIEDLNKK
     LCPQTGQPCK DHSSNGSLNG AAKNGAAKNG ASNGSSAHPT GLHLRYGGVH WFRPNSLQEL
     STILRKCVDD QVRMLFGNTS AGIFKDEGPF EVYVDLRGVK ELYDITVTET SAKFGANTSL
     TSLIQHLTSL KDTQPGFQYF GHLVRHLNLV GNVLMRNAAS VAGNLMIKHA HPDFPSDVFT
     MMEAAGGKVE VFDTKDESLK AYTVQDFVMK VNMKGKVLTA LEIPAFEPLD HFRSFKITPR
     SQNAHAYINA GFRFKISQEG KQVLGRPAIV IGGVNNKFIH AEKTEEFLRG KTLKDEIVRD
     ALALMKSEIA PRLTCAVLRA LYADTTLLEF TGNADPRLAS GAPNIQRPLS SGLQTYEEKK
     EEFPLKQALP KKDCLAAG
//
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