ID J9J6V8_9SPIT Unreviewed; 1127 AA.
AC J9J6V8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJY82145.1};
GN ORFNames=OXYTRI_20335 {ECO:0000313|EMBL:EJY82145.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY82145.1};
RN [1] {ECO:0000313|EMBL:EJY82145.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY82145.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY82145.1}.
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DR EMBL; AMCR01006188; EJY82145.1; -; Genomic_DNA.
DR AlphaFoldDB; J9J6V8; -.
DR EnsemblProtists; EJY82145; EJY82145; OXYTRI_20335.
DR OrthoDB; 5471897at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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); 2.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR43686; SULFURTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43686:SF1; TRNA-CYTIDINE(32) 2-SULFURTRANSFERASE; 1.
DR Pfam; PF00266; Aminotran_5; 3.
DR Pfam; PF01171; ATP_bind_3; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 70..153
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 245..349
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 373..532
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 865..1030
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 762..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 129380 MW; C450603453AA4F47 CRC64;
METQFNQEIT LSQADRAIRA ADVSSLSQQQ DKQERQEQNK DKLLEYIRDN IIGHHSEYLI
NTVYGEKPLI YADYTASGKS LKFIEDYISN QIMPMYANTH TLQSGTGKQT NNAREEARSI
IKRVCGGNEN DALVFVGAGA TSAVNLLVSK LRVREIADQV LIYQQYLKDQ QKQQSNGIEQ
NDKEDQKDFN MEVNDVNFCQ QNRWGSYDCI ICKTIMKSLA QYEQHGQTEL HKRNADIYKQ
KQQIYTEKPV VFMSIYEHNS NVLAWREAGA HIELISMTED GDFDYQHFES LMQKYKGYNS
LKIATISAGS NVTGNLVDVD RVAVSCHRSK TLACFDYAAV VPYVPINMNG PTLESESYFP
PIERKDYGLA YKDAVFFSPH KLVGGPQSSG VLIAKKNVLF SKKPARFGGG IVFFVNELDH
EFVANVEELE EAGTPGVIQD IRAGLAFQLR ESVSMKTIKQ KELQIHSKAL QRLSQMDNVF
LLGNNNKPKA NIYSFLVKTK FGKFLNPNYV VSILNDLFGI QSRAGCLCAA LYGQKILGID
LRLSREFKDA LFDGNEVLRV GFTRLNLNYF IDDQEINYIM DAIEFVSNYG WMLLPHYQFE
AENGYWVNRD EKEVQVRSWL GQIDYSSGKM EYQQPDLTDK KNVSFIKHGL PHVDLSSYIE
IAKNKLVKVV ENYKNLYGKS IMDQKLLIPE PYQRLIWFLF PSEVLGELMN LKYQNTLNFE
FFEHFNKNNQ IQDDVTLPFQ PKDYNKGKFQ FQFSEEYLEN LPTSSTSPIQ NKQQEENKEE
VSQQNDSIQT QQIDTQQILE DKIEKNLYEE EEDNFFSGMD IEEQSEQISD AQQKKQKLIE
IPREIKSQVG SAIRDFDMIK DGDRVLIAVS GGKDSLSLIH ILKYFQSVAP IKFDIGAVTV
DPQVYEYNPR PLLPYMVEID VPFFLESDAI VERAQTCMQK NSICSFCSRM KRGMIYNCAR
REGYNVIAMG QHLDDLAESF VMSSFHNGYL RTMKANYTID KGDLRVIRPL VYCREALFKE
FSNKNKLPII TENCPACFSA PKERHRVKLM LAQQENLFPS LFSSILKAIT PLMKRNMRDF
LKGDDKLGKI GVESSDEEDS VPIQRFDKKN SSKQSQVPTN MPCCNFN
//
