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Database: UniProt
Entry: A0A0N4VIN9_ENTVE
LinkDB: A0A0N4VIN9_ENTVE
Original site: A0A0N4VIN9_ENTVE 
ID   A0A0N4VIN9_ENTVE        Unreviewed;       841 AA.
AC   A0A0N4VIN9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=DAO domain-containing protein {ECO:0000313|WBParaSite:EVEC_0001069201-mRNA-1};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001069201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0001069201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   AlphaFoldDB; A0A0N4VIN9; -.
DR   WBParaSite; EVEC_0001069201-mRNA-1; EVEC_0001069201-mRNA-1; EVEC_0001069201.
DR   Proteomes; UP000038041; Unplaced.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF9; SARCOSINE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          12..375
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          382..433
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          439..711
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          750..819
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   841 AA;  94101 MW;  F6963C7F6C3C5F3B CRC64;
     LFNCCASALS ADVVVCGGGI AGTSVAYHLA ERGKKVFLFE RDRIGSGGAT GLAAGQVTAP
     MHWQDPTKQY MAKRSIDLYH EIASASNFRK ILLDSEISLR RMYSRSILYN EGAELVDDAS
     EMLYRWPFLR TDDIKLALVS PNDLFLDPVG LCNAFAERAK EMGTLTADAL LGVKIFENSS
     VQEVIVGEDN RIKCVDTGAG LIETANFVDA AGIWCGHIPV RNLSTTTFRI AVYPAMYTYL
     NTQKIPSMNV SDQTPIFTHV DDKIFIKPTA GNTYCGGFSE EQAKPLSLPD ENDFKWTIPP
     PDWDAFYPSL SKLLSRCECL GSVGHGNLVG GPEAYTSDKN PVVGETAQVD GYYVAGGLSG
     QGLALAGGMG EALADVICNK VPKVDMSRME VTRFIPLHSS PQYLLERVPE VAGMLFTNSY
     EYHQFRTARN LRTAPIFQLL KNKGAVFGEI MSYERPLWYT KQSDRDNFYK GQYKLIGKPE
     WFDRVEKEYE ACRERVGLID MSSFSKFDIF GPDVVELLQR LCSADVDEPV GSTVYSGMQN
     QNGGYVTDCT LSRLSHNHYF VVAPTYQQLR LQRWVNKWIN EWKYKATCQD VTGLYTALDI
     VGPASRYLMQ DVTGYPMTSS NFPTFRVKEM NIGIATGIRV ISVSHCGELG CVIYIPSEVA
     QNVYERLVDS GEEYSLKHVG YYALRQLRIE KFYVYWGQDI GPLVTPLECG RAFRVNFSKD
     FIGREALLRQ KETGIRKRFV QVLVGNHDLE IDPWPQGGEV IFRNGVPAGR TTSAAYGFTL
     ECQVCIGYIE NQDSYLTADY INRADYEIEI AGKRFPVQVN LHSPTLPMIS SEHPMHYRPT
     Q
//
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