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Database: UniProt
Entry: A0A3M2SN98_9HYPO
LinkDB: A0A3M2SN98_9HYPO
Original site: A0A3M2SN98_9HYPO 
ID   A0A3M2SN98_9HYPO        Unreviewed;       647 AA.
AC   A0A3M2SN98;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=CDV36_001262 {ECO:0000313|EMBL:RMJ19044.1};
OS   Fusarium kuroshium.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ19044.1, ECO:0000313|Proteomes:UP000277212};
RN   [1] {ECO:0000313|EMBL:RMJ19044.1, ECO:0000313|Proteomes:UP000277212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ19044.1};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC         [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC         Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC         Evidence={ECO:0000256|ARBA:ARBA00001792};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the TPA1 family.
CC       {ECO:0000256|ARBA:ARBA00007443}.
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:RMJ19044.1}.
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DR   EMBL; NKUJ01000012; RMJ19044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2SN98; -.
DR   STRING; 2010991.A0A3M2SN98; -.
DR   Proteomes; UP000277212; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR   Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR043044; TPA1/Ofd1_C.
DR   InterPro; IPR039558; TPA1/OFD1_N.
DR   PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR   PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR   Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR   Pfam; PF10637; Ofd1_CTDD; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
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:UP000277212};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          143..268
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..635
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  72566 MW;  411F93D60BEE7F05 CRC64;
     MKRKAGSRAH ASAAISKKPK PSLSAEVAQE RFRAGLFDKD VLDSYTTQYA ESAPYKHAVI
     NGLVNDELLR SVRAEIKANV EFTPKETDIY KIHQSGDLAN LDGLDDESLS KLPSLLKLRD
     AIYSESFRDY VSHITACGPL SGRKTDMAIN IYTPGCYLLC HDDVIGSRRV SYILYLVDPD
     NSWKPEWGGA LRLFPIQELK DKDGEVAKTP LPDVTKVIPP AWNQLSFFAV QPGESFHDVE
     EVYHAATKKQ LEKDGGRVRM AISGWFHIPQ LGEEGYIEGE EERNAKNSGL MQLQGNPAQY
     DMPQPQVIKV DSSQSGQEGF DEADLEFLLK YLSPTYLVPD TLDQISSHFN EVFEITLTDI
     LCKKFAKRLR DYVEAEEKKP TPEDTPTIEK TSSWRVAKPP HKYRYLYQQP SGPDQLRTSQ
     EESPITELLD IFLPSRQFRQ WLQMATNTTI ESADLLARRF RRGLDYTLAT GHEGKARVEI
     NLGFTPTPGW GDDEEEEEEK EETKKNDKEA KTNGKGKGKA VEKDEPAPKE ADEVGGQEIF
     MSGDDDADED AAVYKTGSDD DNILFFQAAT WNKMTIVLRD SGALKFIKYI SKSAKGDRWD
     ISGAFEIEEQ DDSDDEMADA GEGPAPDEES EEEFQGFSPD AAQSDSD
//
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