ID E2AWB7_CAMFO Unreviewed; 1435 AA.
AC E2AWB7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=tRNA 2-thiocytidine biosynthesis protein ttcA {ECO:0000313|EMBL:EFN62277.1};
GN ORFNames=EAG_03988 {ECO:0000313|EMBL:EFN62277.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN62277.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; GL443280; EFN62277.1; -; Genomic_DNA.
DR STRING; 104421.E2AWB7; -.
DR EnsemblMetazoa; XM_011266906.3; XP_011265208.1; LOC105256721.
DR InParanoid; E2AWB7; -.
DR OMA; DMIRDND; -.
DR Proteomes; UP000000311; 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:UP000000311};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 6..368
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 1136..1311
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 575..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1092
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 158753 MW; 486B78AD2B6509D3 CRC64;
MFCRHEARDI VRHAVGAGEQ DAVLFTGQGT AAALRTLLRH LDLSKSTVVF VGPFEHHANL
RPWRELDVKI VRVSETREGF LDLNDLERGL TRMRGEGVTQ MIGCFSAASC ITGVLADDVA
TTLLLHQYGA LSVWDYTTAA PYVQIDMNPH LPGVGETAVH KDAIIFAGHK FIGGVQSPGI
LVTKRWLLRE DVEAEDMRDS HRYHRDPELR EESGTAGVVE SIRCGLAVQL KENVTPRAIV
ARQDKISRQV LSHVRTIPEL ILLGSSSQNV KRLPIFSFMV RHPRGTFLHH NFVCAVLNDV
FGIQARGGCA CAGRYAHDLM GIDRELAKEY ENILLEEQRN GSEETTAEGL RPGFARLSFP
YFMTEAEVAF VLEALKMVAT EGWKLLPQYV LNPDTGEWRH HTNSVFKERK WLGAIRYTDG
RMSATERRVS GSGVFPQTYG DCLQTARNIF NRARKMAQRY PLQIDKSFNF VCQRMEALRW
FMLPSEAQDL LLGNSQNVKQ DVPFNPLLAS NRFSRTNAVT CHDSLVNCLT LTNGIRRLNS
DIPRTGNTLI STSPRHRSLP ALSTVKRAMI ATTIELNQPS SSSNSEEESS NQNEHGTFFG
GHRSPATCPN SPMPVRFAVG EAVTTSVLGS ISRTAVRPTK EQRELIDATN AGRARCNSLG
STTDGCNVPG NRVGTASASS PIPPLPLSPQ TLTSLGLSTI NGSSKHKRLH CSCSSQTELN
SLEMDSAGSP SHSISSLSYN HNPASPPSSY SSTSDYTERL VGGGRLSPVS TSQRSEDDLS
AYVKEMTKEL ATEIKSEIRE VISKVDDALS ETNTSENTPQ HHSRAHSMIN QTFVEDKQLR
HDSFTASDIA EYLMEFSKEM ASEVKSEIRC MVNAVDGLHR YSPDASTSDV SSNGCGSPDR
GRVVLPSSPR LSNSRKSGQI EITSKVGELS QQESKMSSEC SSDETVIYVM KPENEQIVRN
RSKTEDEEVE NDVDDYVDDD PQEGRGGLDI GDTRKILPKI YSAVNSVSSQ DSGINLSFHE
SDKSIDSLDL KRSSSAESNS ANSHGRKPRT TSMMSLSTKG GNKQHARQND NLSEDEECTG
DLREEEGDGQ ENNFEDNESR LEFSRTQWHC PPKNIWKPSV EAMQEFDMIR DNDRVLVCLS
ANGKDSLSLL HTLHQYRFYA RSKGIDFEIG AASVDMGGSD PLEIMSYLKA LDVPYFYEEH
MTDSANTNVD NPLDASVASG TCSFCDKSVR TQLYSLAKRN GYNVLALGQH LDDLTESFLI
SVLHGGILKT MKAHYYIRRE DLRVVRPFIY VREKALRQFT ESKKLPISQD LKTSSEKQNK
RKELMLQQER AYPRLHWSVR TALRPLITAH GQITAFDLTC GGNGGNNIVN SPSSSTSSSI
SSTCSSTSGG GNSNGSNTSN QQKRHRRTKT SNSMATTSSS QQTDVNDETD EEPVL
//