ID A0A0V1DCZ9_TRIBR Unreviewed; 1410 AA.
AC A0A0V1DCZ9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|ARBA:ARBA00030439};
DE EC=2.3.1.234 {ECO:0000256|ARBA:ARBA00012156};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=OSGEP {ECO:0000313|EMBL:KRY59190.1};
GN ORFNames=T03_2416 {ECO:0000313|EMBL:KRY59190.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59190.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59190.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59190.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000256|ARBA:ARBA00001866, ECO:0000256|HAMAP-
CC Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03180};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03180}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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:KRY59190.1}.
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DR EMBL; JYDI01000014; KRY59190.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR CDD; cd15733; FYVE_MTMR4; 1.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR CDD; cd14507; PTP-MTM-like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR046978; MTMR4_FYVE.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR NCBIfam; TIGR00329; gcp_kae1; 1.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF75; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03180};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03180}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03180};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03180};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03180}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 563..953
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1343..1403
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1102..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 146..150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 309
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 706..709
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 731..732
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 792..798
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1410 AA; 157665 MW; A2D5883367E20D23 CRC64;
MLEQEGDRLE MNCSQKALTA IGIEGSANKI GVGIVRQGEV LSNCRRTYVT APGQGFQPSD
TAVHHRQHVL GLVEQAISEA NVDVGQIDLV CFTQGPGMGA PLVSCAVVAR TLAQLWNRPL
VGVNHCVAHI EMGRLVTGAD DPVVLYASGG NTQVIAYSDH RYRIFGETLD IAVGNCLDRF
ARLLNLSNDP SPGLNIEIQA RNGRKFVQLP YCVKGMDVSF SGILSSVEQQ LSLVKRGEIQ
PADLCFSLQE TVFAMLVEVT ERAMAQCGSK DVLLVGGVGC NGRLISMMRS MAEDRGARLH
ASDDRYCVDN GAMIAHTGCS LRSHNVRNDF VPMKFWSHGV TEKASSNNTF NNANLKLSTS
TVILYSRPYW MEERPPLPPD SVAVANSEFP GVENVSRTEA FSRKPLHKLT VHGKFEPYEE
ENYPFPVPFL PGEYAEYFSE PFEDSVRSSF VVLTNFRIFV TASGNGSFYN IPLLCIESVD
YRENAYVSIF CKDGRTAKVT LENNDFTLAW YRLLNSVAVP PAKLEDVFAF AFYAWCLDEK
KKPSFASLQN KINNDQADDY FFFDSKEFVQ QELNRMGFPK EHWRITEFNK NQEFCPTYPS
YWIVPALVTD ADIEGSCRFR ALQRVPVTVW RHPKEGCVLV RCSQPESGIL GWRSDSDETL
LNMINSTASL KATPKDGAPL TPVETNKPVK PMLILDARSY TAAWANRAKG GGFEICEYYN
KCDIQFLGLP NIHCIRVSFQ KFRSSIMEAN ESTWFQNLET CQWIHNLCAL MTSALRAVEA
LQVEKRSVLV HCSDGWDRTT QIVSLAKLLM DPHYRTVKGF TELVERDWIC FGHKFRERLG
MQNGDQNQRS PVFLQWLDCI HYLLHEYPCS FEFNEIYLVK LAQHAYSGLF GTFLCNSIAE
RRQLTIPQRS FSVWDYLNVS NGQFRNILFS HDDSVLWPRL GLREMAALWR AIYFPGNGDT
VNGGGRRLCI AGSATVSALH ANNDEDDDHD AGFVGHCRLT VERSIPTVLI RSHSCDSVPL
ADFQRPGFFP EPAFHRLGSQ PCLVTNSSTS AFRSLAKSQQ SDTADVGFLD CAQVAGSDRP
TRLALLSNGD SGPQTPQRCR RAMLNGSKSS STSVDFDHER DDDTDGERTT DVESSGVAQT
CDHSTSTTEI SDPRAIRPEI GIRNVVHYHR IQPNRQLVNG NNSGDGQSDQ NQRCRSDDCC
VGGLSSNQRQ ALAEMLDRDG LIRVRDGAQE RMQKIMHGYE KRIAFLQTEL FRAQTACAYG
KCPTCDQRTA TVVDFSSSTD PIMAVVMEGR DQTRTRNSES QSALSENGAE PRSCDSRTTT
QSDASSWEAV DCEDGTPTLW VPDHAARRCM GCDSEFWMVN RKHHCRSCGK IFCGSCSNYE
CPVPEEQFYE PVRVCNSCFS ALKYQQKVEA
//
