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Database: UniProt
Entry: A0A0V0TJ58_9BILA
LinkDB: A0A0V0TJ58_9BILA
Original site: A0A0V0TJ58_9BILA 
ID   A0A0V0TJ58_9BILA        Unreviewed;      1261 AA.
AC   A0A0V0TJ58;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   Name=Tkt {ECO:0000313|EMBL:KRX38998.1};
GN   ORFNames=T05_5662 {ECO:0000313|EMBL:KRX38998.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38998.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX38998.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX38998.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:KRX38998.1}.
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DR   EMBL; JYDJ01000247; KRX38998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TJ58; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR   PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR   Pfam; PF00806; PUF; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00025; Pumilio; 4.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          952..1116
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   COILED          117..144
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1261 AA;  140929 MW;  90F1EECBCE3E28FD CRC64;
     MSHKFDSFLT LRIPSEPEKK FFDCKNSAVL HSKTGHKLCS SSFALSLFIA FSEVGNIGWQ
     VGWEKLKMQF IKFNNEGNEN FSTHARKRKN FTGRYFTHPA VEESKKSPSS NEYFGKFEEL
     KHYIEQLSRK VQSDEANMSE EEKSILFKNL LSECHGHEIS VLREKDCFNN LLIIIGNNAS
     IAMELLWKIV KIRKKVILTL MTSYGGALEK LLAVALNESE GSRKASVLLK LSEIALENVD
     SLSVQHGGSH LLRRLGSAIS GVEKCAHNGA TPIFSAKNEN EPKRFEANFL NQAEFISIYN
     NLAGRVLNWK SIREFANREP FSLLVQDFIA YDSSFNCTFV NGLLPSILEE NKKTVYSMLT
     NKQASRVWDQ YIRFSSIENV LKLYENCFRG SVARLISDQY ANYPLQQMIR KVDDSVLAKE
     LYEEVLQCFD EIWKARLYGV VHSLCIFVRE KPQLETILVE KIKTVLNCRD PKICEAHFLR
     CLLSMQRYVQ DKVFLQCYHL QKKIKYFGSV LTQTLATFST KEFFFEQMLN LPYEDFLQIS
     STSLGSYAVE ALVKAAETLD QRRAVVNKIL PITFKLANGR FGSRVLECVW ENCDVEERLP
     IMDAMLKCSL NSQTVSTFNM KHDKCWSTAR MPNALPDLHT IQELKDIAHK LRIHSIRATN
     ASNSGHPTSC CSMAEIMSVL FFHTMKYDPK NPRDPYNDRF ILSKGHAGPI LYACWVEAGL
     IPESELLNLR KIDSDLEGHP TPRLSFVDVA TGSLGQGLSC AAGMAYVMKF MDKIDSRVYC
     VLGDGESAEG SVWEALHFAG MYELDNLVAI FDINRLGQSQ PASLGHRIDV YQQRFEAFGW
     NVECVDGHDV EALCRSFSSA AGVKHKPTAI VAKTFKGFGI PKVEDQENWH GKALGKEAAA
     ALEAINSRIK NFDHHKLSIN LPRIDPSKPL KANDFSNVKL SEPPNYKIGE KVATRLAYGT
     ALVKLGKSCD RVVALDGDVK NSTFADKFKN AFPDRFIECF ISEQNMVGVA VGCSTRSRTL
     PFCSTFATFF TRAFDQLRMG AISGANVKCC GSHAGVSIGE DGPSQMGLED IAMFRTLPGS
     TVFYPSDAVS CERAVELAAR VNGICFIRTG RPNTPVIYSN EEQFSIGQAK IVRHSDKDRL
     MIVTAGVTLF EAFTAADVLA KEKGLHVCIC DLFTVKPIDK RTLAEQAKRV GGKVLTVEDH
     YPEGGIGDAV ASALAEYSDI QLTSLAVNAL PRSGPPDSLM DMFGISAKHI IEACVQLAGH
     A
//
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