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Database: UniProt
Entry: E2AWB7_CAMFO
LinkDB: E2AWB7_CAMFO
Original site: E2AWB7_CAMFO 
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
//
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