ID A0A498MD60_LABRO Unreviewed; 364 AA.
AC A0A498MD60;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB-like protein {ECO:0000313|EMBL:RXN17234.1};
GN ORFNames=ROHU_008092 {ECO:0000313|EMBL:RXN17234.1}, ROHU_022771
GN {ECO:0000313|EMBL:RXN23365.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN17234.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN17234.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN17234.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN17234.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:RXN17234.1}.
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DR EMBL; QBIY01012752; RXN17234.1; -; Genomic_DNA.
DR EMBL; QBIY01012561; RXN23365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MD60; -.
DR STRING; 84645.A0A498MD60; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR031521; DUF4695.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF15766; DUF4695; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase {ECO:0000313|EMBL:RXN17234.1};
KW Oxidoreductase {ECO:0000313|EMBL:RXN17234.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MD60};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 118..244
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 214..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 41200 MW; E8C80CA8550C2DF5 CRC64;
MSGQYQPIRE IPMEKVIEKA GDYEISQGPT GVSRLRLIPG FLQQEEADWM FSKLLAELPW
SQKTNYRMMG DAYDEPRLTC WYGELPYTYS RSTMEANAQW HPVLNTLRLA VEEKSGHTFN
SLLCNLYRDG KDSIGWHSDS EPSLGPQPII ASLSLGDTRV FSLRKQPLSE DKGDYTYVER
IRIPLTHGTL LLMEGCTQAD WQTSKSRQEG YKESHFTEEE LEKCKPLQTS QKPNAQPLPS
RHMAARPMET VGFAVLPAHI LASAMEEFPQ QLPVPKCLAR GRNRPRRPRD ARFKTQPVTF
AEIAEVEEEG ASPLEEERAR RSFLQSLESL RRSTQTLHHA GSTQSCRTAS AQASLDSSDS
DSAH
//
