ID A0A182WH70_9DIPT Unreviewed; 953 AA.
AC A0A182WH70;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RRM domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN009722-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN009722-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN009722-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR AlphaFoldDB; A0A182WH70; -.
DR STRING; 112268.A0A182WH70; -.
DR EnsemblMetazoa; AMIN009722-RA; AMIN009722-PA; AMIN009722.
DR VEuPathDB; VectorBase:AMIN009722; -.
DR OrthoDB; 2321660at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; 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 GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd08248; RTN4I1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039210; OGFOD3.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR037397; RTN4I1.
DR PANTHER; PTHR14650:SF1; 2-OXOGLUTARATE AND IRON-DEPENDENT OXYGENASE DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR14650; PROLYL HYDROXYLASE-RELATED; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50102; RRM; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 99..172
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 819..923
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 104327 MW; C8B719F4DFE31380 CRC64;
MNNQKRKSAA NASATNGNDS DGSDYEVEWQ VKPTPPKVTK ADLFPLPAQV AKNIQKSARG
ARRVSSSEDD SDDDGEDLPT LTSAQISAIL ETIKNNKRLV LIVKNVNFST AKEEIAMHFD
QAGRVKSVRI PKHRSSGFAF VEMENADGFQ KAFLLDGSVL DGRKINVDLS ESGSKKSATR
IQLLEKKNAE IRKLRKKNRK TAGKFGQRDL LGNFRNLSTA TVTSAPQSSS TQEQQRRQHA
SYGKMSGWQI HAYGVPQEEI QFNDGIKMPI LRSPTQLLVK VKASSVNPID VAMINGYGAS
VLNAMRCKDG GIEFPLVLGR DFCGEIVQKG LGISSRELEV GDEVWGVVPL HLQGCHADYV
VVEKYCLFKK PSNLSKIDSS AILYAGLTAW SGLYITGHLG DLLGAISPVG GGAGKKVLVL
GAAGGVGTLA VQMLLAEGVE VFATCSPDAM QMVHNLGVKY VLDYTDPAHV QNVASVGRFD
IVLDCAAKGT DYANEIPWLF DQYITFNSPV LKNIDAEGFA GGMYQNAVNL VRNNAASLST
RQGVVKWGYF VPAPQGIAYL QRLAEKGKLL PVVEKVYPFA SIPEAYERGR ISLSILFHNS
IAYWKTVLFG ENAAMSDGGG SVRQRKKSAG DGSGNRARKS KTTSSSGSSA PSTAQQHQMW
ARIVLMVGIA AIVYFTTFRT REKKFATQRE VLELRTQPLD CSRPYLDEIS KFAGCIPNQC
GRFVSDKIVS PAEAGILLDL ARAGFELGQS AGGASILDLH SGALSKGTQF VNVYRLPEAK
KLFTSQHINV YRHVKAKVQQ AVADQFRLSV DALHLTHPTF FSRLTNATAK TIHDEYWHEH
VDKETYNSFH YTTLLYLTDY GKDFTGGRFV FIDNEGKHNR THVYIEPKRA RVSGFTSGAE
NMHHVEQVTG GVRYAITISF TCDREYAMAD PKFALDDDEE EAGGTNDGRM GEP
//
