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Database: UniProt
Entry: A0A0V1MYZ6_9BILA
LinkDB: A0A0V1MYZ6_9BILA
Original site: A0A0V1MYZ6_9BILA 
ID   A0A0V1MYZ6_9BILA        Unreviewed;       545 AA.
AC   A0A0V1MYZ6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE            EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
GN   ORFNames=T10_4852 {ECO:0000313|EMBL:KRZ77016.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77016.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ77016.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77016.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha
CC         subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-
CC         inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-
CC         COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29;
CC         Evidence={ECO:0000256|ARBA:ARBA00035981};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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:KRZ77016.1}.
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DR   EMBL; JYDO01000023; KRZ77016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MYZ6; -.
DR   STRING; 268474.A0A0V1MYZ6; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd00051; EFh; 2.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR12907:SF27; HIF PROLYL HYDROXYLASE, ISOFORM C; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          9..50
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   DOMAIN          270..366
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          404..439
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          440..475
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          477..512
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          513..545
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   545 AA;  61590 MW;  48D11E974EC18492 CRC64;
     MVNRSVLFCS FCGKLSSDNV PLFKCSGCLK VCYCNRLHQQ QHWNDHKKHC DNMHSSLLLK
     CHQSTGTGFL NDPNSRMKFN TTTTTTTTPI TTTKICEQLN KQMPNSSKAL DHLISSDVCT
     MACDLCKQKT NSNSSYAKEL LDSCGVIQGS SVSLSMNLIQ MDNLELRTKR LAHHVLCSLN
     HLGWTVVDDF LGYSHAAAVL NDVLNIYNSG RFVDGQISHK GSLSRQWRSD LIYWYSGVDD
     YLESIAYLLH QIDDLILSIS SSLTDCRIDQ KSKAMLSCYK VGSYYVKHVD NAERDGRLIT
     CVYYMNRDWI AKLGGLLRIF PTNTKSQVDI EPLFDRLIIF WSDRRNPHEV TPTLSDRFAI
     TVWYFDGLEL GCQNDANAAF HSNCIRSISI QSHTTAPADQ LTEEQIAEFK EAFSLFDKDG
     DGTITTKELG TVMRSLGQNP TEAELQDMIN EVDADGNGTI DFPEFLTMMA RKMKDTDSEE
     EIREAFRVFD KDGNGFISAA ELRHVMTNLG EKLTDEEVDE MIREADIDGD GQVNYEEFVT
     MMTSK
//
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