ID A0A195DC95_9HYME Unreviewed; 1511 AA.
AC A0A195DC95;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000313|EMBL:KYN10511.1};
GN ORFNames=ALC57_17116 {ECO:0000313|EMBL:KYN10511.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN10511.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN10511.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN10511.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN10511.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; KQ980989; KYN10511.1; -; Genomic_DNA.
DR STRING; 471704.A0A195DC95; -.
DR Proteomes; UP000078492; 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:0016740; F:transferase activity; IEA:UniProt.
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; 1.
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:UP000078492};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 80..403
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 1222..1404
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 167469 MW; 67B16B3859BCBD4E CRC64;
MNLPRPEEAY SNGLSADSAA LAGGLLTPPS RERERERDTF KEREMVYCDY TASGRSLQFL
EDYIAKEVLP CLGDTRASTS ICSLQSSLFR YEARDIVRHA VGASEQDAVL FTGQGTAAAL
RTLLRHLDLS KSTVVFVGPF EHHANLRPWR ELDVKIVRVS ETREGFLDLN DLERGLARMR
SEGVAQMIGC FSAASCITGV LADDVATTLL LHQYGALSVW DYTTAAPYVP IDMNPHLPGV
EETAVHKDAI IFAGHKFIGG VQSPGILVTK RWLLREDVEP EDMRDSHYYH RDPELRGESG
TAGVVESIRC GLAVQLKENV TPRAIVARQD KISRQVLAHV RTIPELILLG NSSHNVKRLP
IFSFMVRHPR GTFLHHNFVC AVLNDVFGIQ ARGGCACTGR YAHHLMGIDR ELAKEYETIL
LKRQQNGTEE TIAESLRPGF ARLSFPYFMN ETEIAFVLEA LKMVATEGWK LLPQYVLNPD
TGEWRHHTNS VFKERKWLGS IRYTDGRMNA TERRASGAGI FPQNYGDCLQ TARNIFNRAR
KMAQRYPLQI DKSFNFMCER MEALRWFILP SEAQDLLLGN SQNVKQDVPF NPLLAWNKYN
TSTITTSHDS LVNCLTLTNG MRRLNSDIPR TGNAPISTTS PRHRSLPALS TVQRTLMATS
AELNQPSSSS NSEEESPNQN EQFSGHRLPA TCPNSPMPVR FMVGEAVTTS VLGSTSRATV
RTTKEQRELM EATNAGRARC NSLGSTTDGC NIQGNRTGAP TASSPIPPLP LSPQTLTSLG
LSTSNGSSKQ RRLHCSCSSQ TELNSLELDS AASPSHSISS LNYNHNPASP PSSYSSTSDY
TERLIGGGRS SPISTNMGQD DLSAYVKEMT KELATEIKSE IREVISKVDD ALSETNTSEN
TPQHHSRAQS VVNQTCVEDK QSRHDSFTAS DIAEYLMEFS KEMASEVKSE IRCVVNAVDG
LHRYSPDAST SDVSSNGCGS PDRGRIVLPS SASPRVSSSR KNGPIEITSK VGELSQQESK
MSSECSSDET VIYVMKPSET EQIVRTRSKT EDEEVENDVD DYVDDDSQEG RGGLDIGDAR
KVLPKIYSAV NSVSSQDSGI NMSFQESDKS IDSLDLKRSS SAESNSAHSH GRKPRTSSMM
SLSTKCGGKQ QARQNDNLSE DEECTGDLRE EEGDGQENNF DDNESRLEFP RTQWHCPPKN
MWKPSVEAMQ EFDMIRDNDK VLVCLSAIGK DSLSLLHTLH QYRFYVRSKG IDFEIGAATI
DTGGSDPMEL MSYLKTLEIP YFYEEQVTDS NSVNVDNPLD ASIASGTCSF CDKSVRTQLY
SLAKRNGYNV LALGQHLDDL TESFLISVLH GGVLKTMKAH YYIRREDLRV IRPFIYVREK
ALRQFTESKK LPISRDSQTL SEKQNRRKEL MLQQERAYPR LHWSVRTALR PLITAHGQIT
TFDLACSGTG GNSPSGSTSS SISSTCSSNS GGNNTSSQQK RHRRTKTNSS ANTASSQQTD
ENDETDEEPV L
//
