ID M4ACV2_XIPMA Unreviewed; 491 AA.
AC M4ACV2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Dihydrouridine synthase 2 {ECO:0000313|Ensembl:ENSXMAP00000012296.2};
GN Name=DUS2 {ECO:0000313|Ensembl:ENSXMAP00000012296.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000012296.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000012296.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000012296.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR AlphaFoldDB; M4ACV2; -.
DR Ensembl; ENSXMAT00000012312.2; ENSXMAP00000012296.2; ENSXMAG00000012268.2.
DR eggNOG; KOG2334; Eukaryota.
DR GeneTree; ENSGT00550000075019; -.
DR HOGENOM; CLU_013299_3_0_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR CDD; cd19871; DSRM_DUS2L; 1.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR044463; DUS2_DSRM.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR45936; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR PANTHER; PTHR45936:SF1; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 16..254
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 460..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54485 MW; 23F23FA1694955A8 CRC64;
MFVVSLSLSF RNITALAPMV RVGTLPMRLL ALDYGADVVY CEELIDIKMA QCQRIVNDVL
ETVDFVAPDE RVMFRTCERE KDSVIFQMGT ADPDRALTVA QLVEKDVAAI DVNMGCPKEY
STKGGMGAAL LSNPDKIEAI LKKLVTGVSV PVTCKIRILP SLEETVSLVQ RIEKTGVAAV
AVHGRFKDER PTHPIHCDYI QAVAQAVSIP VIANGGSLDL VKTNSDIEKF RKATGASSVM
LARAAMWNPS VFCNQGPLPV EKVMEEYIKY AIRYDNHAFN TKYCLCQMLR DRVESPLGKQ
VQAAQTNAEI SEAYGLQTFY QEIQQDLQAK MAALQSSNQP NKPIMDGDVT TMAVKFERRD
YPPQITPKMF LLEWSRKEKL EQPQYETVRK TVTFSLCSKS KKFAEQASAI VCLRVLGVPE
GRIGEEDSGL VCKRKREGKP NCSGEEGRSK KLHVDILQEA EAPSPTVEMN SDEQNPATPL
KQVEALREAL S
//
