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Database: UniProt
Entry: A0A0V0TBJ9_9BILA
LinkDB: A0A0V0TBJ9_9BILA
Original site: A0A0V0TBJ9_9BILA 
ID   A0A0V0TBJ9_9BILA        Unreviewed;       835 AA.
AC   A0A0V0TBJ9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like {ECO:0000313|EMBL:KRX36383.1};
GN   Name=DUS4L {ECO:0000313|EMBL:KRX36383.1};
GN   ORFNames=T05_3514 {ECO:0000313|EMBL:KRX36383.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36383.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX36383.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX36383.1};
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   -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC       found in the D-loop of most tRNAs. {ECO:0000256|ARBA:ARBA00002468}.
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:KRX36383.1}.
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DR   EMBL; JYDJ01000368; KRX36383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TBJ9; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0019236; P:response to pheromone; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 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; IPR019336; GPR180/TMEM145_TM.
DR   PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR11082:SF31; TRNA-DIHYDROURIDINE(20A_20B) SYNTHASE [NAD(P)+]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   Pfam; PF10192; GpcrRhopsn4; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        569..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        600..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        639..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        672..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        706..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        744..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        776..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..283
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   DOMAIN          534..792
FT                   /note="GPR180/TMEM145 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF10192"
SQ   SEQUENCE   835 AA;  94326 MW;  9046251B57008B36 CRC64;
     MTNDRTKINI VELFSNSAPL KISAPMVRYS KLSFRRLLRL YGCQLCFTPM IYAKCFIQSE
     KARRADFSTD ASDFPLIVQF AADNCDDFVK AAEIVYTQCD GVDLNCGCPK RKTLDTNCGS
     ALLDNASHLA ELIKQSRLRI LDSKFSISVK IRIYENLKDT VDLCQKLQSA GITFINVHGR
     TVEQRHEPVD VEVFKVIKDS LQIPVVANGD VRSLSDVHYY HQHAGVEGVM VARALLENPA
     LFTGANKTPA DCFFHWMKFA EADNVPFTRF HRHISFMLEK SLNKSQRAEL AEIRDSNQLF
     TFVSKTVALA LLNSGVPLSI PRKLLFSVHL IEDCNIISPS IDMACVGGLS NCFFTSSSLI
     LLISISSNVV ETVKISGRWH HGSGDPLLTL LTGFGFQKTD PADLEATRGF IFGNITDGMA
     KPVGYLILIA SDWIEEMKTV YRSDNASCKQ LMSRLSDLAF ERRCFPKNGQ DFFRSIPCPV
     GNICPDEDDR TNVISGYQLT FRIQDVIQAR FWYLALVNCI LDDACNWVPF NSTIDLQYEL
     WLVNGHPSRR NRNPLEHQFS VEQQDTLELY LFACCIFIGL FGAHLYSISL GRFRSHRSSV
     AMLLLVGLQV LYYSVRCGHC IAIVVGGVSI VPLLHVGDLL FSLADVLFAL LLVHFATSWP
     KSFQHFPAKR KLTTIFGPLA LTAQLTLTIC ATMSRVELLP NHFVETWPGW LILALRLLLM
     KWFLTELRIS LQRERDSSHR SKFLLHFGSG YMVWFIYLVA LGALVGEFSV LWRYKVLNGI
     CFFANFVAYA AMVHLFWPQS VLQKLLCSND DFDSTKDSAD WDEYEQAIII SSSDR
//
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