ID   A0A182K0E2_9DIPT        Unreviewed;       893 AA.
AC   A0A182K0E2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0008006|Google:ProtNLM};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR004224-PA, ECO:0000313|Proteomes:UP000075881};
RN   [1] {ECO:0000313|Proteomes:UP000075881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACHR004224-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR004224-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   AlphaFoldDB; A0A182K0E2; -.
DR   STRING; 43041.A0A182K0E2; -.
DR   EnsemblMetazoa; ACHR004224-RA; ACHR004224-PA; ACHR004224.
DR   VEuPathDB; VectorBase:ACHR004224; -.
DR   OrthoDB; 1815533at2759; -.
DR   Proteomes; UP000075881; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF291; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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          35..395
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          399..454
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          456..738
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          771..856
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   893 AA;  100890 MW;  B0DEC2DADF070826 CRC64;
     MWNKILRTVP GARSRNTQDV VRMGSSEAAT SHQARVVVAG AGLLGNSVAY HLADNGWSNV
     VVLDQSKVGS GTSHFGSGTI GLFKPTPERN IVMESLKLYQ RLHDQGHDIG LRRCGSLNLA
     QTHDRVIALQ RRAAYILPTG MHCELVDSET ARKLHPFLYP DDLQGAVYVP DDCIADPASV
     VQVLASEAKR KGVKYFEGCQ VKYINTKNER VHSVETDVGT ITCEYFVNCS GMWARELGLK
     CKPSVRVPAY PAQHYYALTP SLNLPTDDDN LLPCIRDYDS NLYARQYDQS LLVGWFEKDA
     KPAFEETKDI PKAWQDHLQE DHGHCGALWE KAVDRLPVLR DLSMPTMRNS PDNFTPDGRL
     IFGESAEVKN YFVACGMNGN PLQGSGGVGK ALAEWIVSGT PTIDMLPFNI QRFLDLHNNR
     QYLQQRIREV VGRQYAILYP NQSEYKFARK LRCSPLYSVL EARGAVFGTK MGYERALYFD
     ADYRRGDPLP TLPEGSFYKP KFFQNMEKEY QACAQHVGII DISSFSKIEI KPGIQSDTVS
     GENAVLRYLQ YMCANDVNIA VGHIVHTGML NEHGGYENDC MLIRQTEDSY FMISPSSQQT
     RIYEWMSRNL PSDASVQLND VTSMYTVINV VGPKSTLLMS ELSNSDVRLA PFSYRKLNIG
     YASDVMIMSF THTGMPGYCL YVPSEYALHV YDRLITRGRD YGTRDVGTLT QRFLRIDKFI
     PFWGDELTSM TTPFEAGVFY SVRLDISQLK KKENFIGRQA LERQKRDGLR KRLVLFHVED
     IDIDKDVWPW GGEPLYRNNE FCGTVTSAGY GFASEKLVCL GYISRAESSP VRTITTEFIM
     DKDAVYHIDI AGKRFRLTQH IHPKAAMASA IERQDLSKSY RPTVVKEKKQ QKS
//