GenomeNet

Database: UniProt
Entry: V4AD74_LOTGI
LinkDB: V4AD74_LOTGI
Original site: V4AD74_LOTGI 
ID   V4AD74_LOTGI            Unreviewed;      1094 AA.
AC   V4AD74;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=tRNA(Ile)-lysidine/2-thiocytidine synthase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LOTGIDRAFT_230512 {ECO:0000313|EMBL:ESP01939.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP01939.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESP01939.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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DR   EMBL; KB200329; ESP01939.1; -; Genomic_DNA.
DR   RefSeq; XP_009047097.1; XM_009048849.1.
DR   AlphaFoldDB; V4AD74; -.
DR   STRING; 225164.V4AD74; -.
DR   EnsemblMetazoa; LotgiT230512; LotgiP230512; LotgiG230512.
DR   GeneID; 20248317; -.
DR   KEGG; lgi:LOTGIDRAFT_230512; -.
DR   CTD; 20248317; -.
DR   HOGENOM; CLU_003433_9_1_1; -.
DR   OMA; CATVDPQ; -.
DR   OrthoDB; 5471897at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR   CDD; cd01993; Alpha_ANH_like_II; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   PANTHER; PTHR43686; SULFURTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43686:SF1; TRNA-CYTIDINE(32) 2-SULFURTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 2.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          72..258
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          288..449
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          857..1027
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   REGION          761..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  123913 MW;  ABDEE25A83269660 CRC64;
     MLFAIEEFFK EVKKMSESNE NRLFYTIPKH ELVEKNDESL TTKEKLLSYI RDNIIGSEKI
     FGGPFGLRNV LYLDYIASGR SLKFIEDYIQ AEVLPEYGNT HTTTSVTALQ TTLYRHEARD
     IIRNACNASE HDSVIFVGSG CTGAVHKLIC ALNLKHPPIV LVSPFEHHST FLPWLEGGAQ
     VIRIKESLNG DVDLDHLKHM LQKYKESGRQ LIGCFSAVSN ITGIIVDINT ITISLHKYGA
     LAFWDYATAA PYLQIDMNPV INRLIGFYLQ IDVNNVIKSE DQAYVYKDAI FISVHKFIGG
     VSTPGVLLAK KNLFNNKRPD VCGGGTVFFV RREGHRYLQE PELKEEGGTP AIVESIRAGM
     VFQLKQALTP SFIMEKEHLL YKKAISMWSQ CPNLVILGNP SAPRLPVFSF LIYNPLNGRF
     LHHNFVSSIL NDVFGIQSRG GCACAGPYAM DLLGLSEEKA KQIEELLVED KRLDRTHLRR
     YKEYSHREII RPGFTRLNLP YFLTEVQLDF TIKAVTMVAE HGWKLLPQYI FNPETGEWKQ
     KNFQNFKDRK WLGHILYQNG QMEFKIPAAT VKGPLPTNFQ ECLKMAEVIF DKATKLKTTL
     PDQSLLFDED TKPFRWFMLP SEAQDCLHGN HTPALTLTDL PFCPNVLKQR HGFPTEILHT
     EILLNSKPLI PRENDELGNK EAFCDGMIQC LNLGYEEMDE NSQEKCNSNV YPSVKNCELT
     SNTVAEDNGS ETVTPVFYSE AKSDNFTARL SSKDLNSAEE TLEKFDSDNS KHEISQKDRT
     IGMQSDTSKE TELSSSKTNE SKAVGVVCPL LRKADNKISE EAEVKTKQVQ WFSPPRDIFK
     PSVTAIEEYN MIHNGDKLLV CLSGGKDSLS LLHTIRQYQF YAKAKGIHFE FGAVTVDPQT
     PAYDPSPLKD YLASLGVPYF FESQGILETA SNLPYECASI CSFCSRMKRG RIYACARREG
     YNVLALGQHL DDLSESFLMS FFHNGSLRTM KACYTVKQGD LRVIRPFVYV REKLLRTFAE
     KSKLPVIAEN CPACFEAPKE RHRSKQLLAS QELLFPQLYN SMMAAMKPLM AINTTKSSLS
     NIFNQNNSTE ETDD
//
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