ID A0A0V0W761_9BILA Unreviewed; 2645 AA.
AC A0A0V0W761;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
DE EC=3.1.3.78 {ECO:0000256|ARBA:ARBA00012936};
GN Name=HIP1 {ECO:0000313|EMBL:KRX71567.1};
GN ORFNames=T06_7254 {ECO:0000313|EMBL:KRX71567.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX71567.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX71567.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX71567.1};
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=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:25674,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456; EC=3.1.3.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001261};
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}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004107}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. 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 SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00243}.
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:KRX71567.1}.
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DR EMBL; JYDK01000236; KRX71567.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0W761; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
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:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR CDD; cd17006; ANTH_N_HIP1_like; 1.
DR CDD; cd15733; FYVE_MTMR4; 1.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR CDD; cd14507; PTP-MTM-like; 1.
DR Gene3D; 1.20.5.1700; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_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; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR019178; PtdIns-P2-Ptase.
DR InterPro; IPR030224; Sla2_fam.
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; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF09788; Tmemb_55A; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
DR PROSITE; PS50945; I_LWEQ; 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 Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03180}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03180};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00243};
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:UP000054673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03180}; Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00243};
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 TRANSMEM 1159..1181
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00243"
FT TRANSMEM 1193..1214
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00243"
FT DOMAIN 20..148
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 727..967
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT DOMAIN 1798..2188
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 2578..2638
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 993..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2317..2385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2409..2428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2524..2563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 385..562
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 729..756
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 926..962
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1002..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2322..2347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2348..2365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2531..2562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1373
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1377
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1394..1398
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1394
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1426
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1441
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1445
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1529
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
FT BINDING 1557
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03180"
SQ SEQUENCE 2645 AA; 297754 MW; C3202A0C87D3773F CRC64;
MTAANIPKNL LRRPSTMMMD REEYEKLQSA ALLKCINAQE CAVKEKHLRT LILGTYNDRG
AGLFWANLTK IQLESNLVIS WKFCHVLHKL LRDGEPHVLT DSLKYVSKLS ALGQLWGHLK
EGGGMLIKHY CAVLVKKLIF HQHNQQIPGN VSLTESQLEA LGSEGVDNWF ELSVEVMDYL
DAILQLQQSV FNSLDKSRAS SMTPSGQCRL APLILCILDS SSLYDILVKL MFKLYACLPE
KELVGHSDRF IPIFGKLKQF YASSSNLQYF KFLVSVPSLP ENPPNFVIAS DIGNYVCPQV
LVHERQGNES PSDSQSVEDV KLVDFNDFRT VETDPSITSS ISASQETEKD RIINTLRHEL
DDTKATVFRI NQEYALMNQQ SRAQMLELEE SVAHSKEMLN QMLEENERYR LKNEQLENEK
NQLIDEQREN TQNQIVVLEE KFQKMKDAYR NLREEHIKTL KNLSQAQKQL EDGNVDKLET
ELCKSEQEFA NEIHQLKLEN EDLHARVCFQ EKEMQVMQIN IDQMAEQHAK LESKAKDTDA
CKVELEKQIT SLDQQLTVLK RDCELNRAML NDHFLTFCKL LSDAMNDTLK EIESPAFEQQ
VTCSAEYFFS KIQPVQEDIE NMRSLVAEKI SGSKLSDESA VLTNLFNLCY SFSTFFRLGQ
AALRILSTSS SSNVETFGAN ISNAVVEAEK FFINFGEGGK NCLLHLQTIS DCVESLKLAV
KSAGEMFSNI DAEELAELYE KEMKIMEEAI QEAASKIQVI LDKNRCSNSG VSLEVNEKIL
ESCTKLIREV MKLVVSAKKL QNEIVQLKGG AVSAKEFYKR HHEWTEGLLS AAKAVGSRAN
LLVDAADRVV SRAAKLEELT AASKEIAAST VQLVVASRVK ADRESNYLKE LGSCSRSVSG
AVAEVLQTVK VGKECLEEED MDFSKLSLHQ TKRLEMEKQI RLLELESLLE KERKSLGELR
KHHYQLDESF EEQDALNMSV RSWDTRDVDE NTPLIQDSHE SVADPVPDEP RADVEDKPEK
PVQRTITCRI CQEPISIERK LLHNVVRCKH CNEVTPIRQA PPGKKYVRCP CNCLLICKQS
SNRIACPRPD CNRVIMLNTM SSGTAVRAPP GTARVSCIHC KEIFMGNDFH LQFQYNTLSK
TLARCPHCRK VSSTSQRAAW IRALILLLLG LLFLISGFGL AAGTWTTVVD HPILYLSWGV
MFVLSLLFVF RGIYFMNVKT SKIEGLLFLH HMCNFYTDEF TYLMNTEEML EQEGDRLEMN
CSQKALTAIG IEGSANKIGV GIVRQGEVLS NCRRTYVTAP GQGFQPSDTA VHHRQHVLGL
VEQAISEANV DVGQIDLVCF TQGPGMGAPL VSCAVVARTL AQLWNRPLVG VNHCVAHIEM
GRLVTGADDP VVLYASGGNT QVIAYSDHRY RIFGETLDIA VGNCLDRFAR LLNLSNDPSP
GLNIEIQARN GRKFVQLPYC VKGMDVSFSG ILSSVEQQLS LLKRGEIQPA DLCFSLQETV
FAMLVEVTER AMAQCGSKDV LLVGGVGCNG RLISMMRSMA EDRGARLHAS DDRYCVDNGA
MIAHTGCSLR SHNVRNDFVP MKFWSHGVTE KASSNNPFNN ANLKLSTSTV NLYSRPYWME
EQPPLPPDSV AVANSEFPGV ENVSRTEAFS RKPLHKLTVH GKFEPYEEEN YPFPVPFLPG
EYAEYFSEPF EDSVRSSFVV LTNFRIFVTA SGNGSFYNIP LLCIESVDYR ENAYVSIFCK
DGRTAKVTLE NNDFTLAWYR LLNSVAVPPA KLEDVFAFAF YAWCLDEKKK PSFASLQNKI
NNDQAQELNR MGFPKEHWRI TEFNKNQEFC PTYPSYWIVP ALVTDADIEG SCRFRALQRV
PVTVWRHPKE GCVLVRCSQP ESGILGWRSD SDETLLNMIN STASLKATPK DGALLTPVET
NKPVKPMLIL DARSYTAAWA NRAKGGGFEI CEYYNKCDIQ FLGLPNIHCI RVSFQKFRSS
IMEANESTWF QNLETCQWIH NLCALMTSAL RAVEALQVEK RSVLVHCSDG WDRTTQIVSL
AKLLMDPHYR TVKGFTELVE RDWICFGHKF RERLGMQNGD QNQRSPVFLQ WLDCIHYLLH
EYPCSFEFNE IYLVKLAQHA YSGLFGTFLC NSIAERRQLT IPQRSFSVWD YLNVSNGQFR
NILFSHDDSV LWPRLGLREM AALWRAIYFP GNGDTVNGGG RRLCIAGSAT VSALHANNDE
DDDHDAGFVG HCRLTVDRSI PTVLIRSHSY DSVPLADFQR PGFFPEPAFH RLGSQPCLVT
NSSTSAFRLL EKSQQSDTAD VGFLDCAQVA GSDRPTRLAL LSNGDSGPQT PQRCRRAMLN
GSKSSSTSVD FDHERDDDTD GERTTDVESS GVAQTCDHST STTEISDPRA IRPEICIRNV
VHYHRIQPNR QLVNGNNSGD GQSDQNQRCR SDDCCVGGLS SNQRQALAEM LDRDGLIRVR
DGAQERMQKI MHGYEKRIAF LQTELFRAQT ACAYGKCPTC DQRTATVVDF SSSTDPIMAV
VMEGRDQTRT RNSESQSALS ENGAEPRSCD SRTTTQSDAS SWEAVDCEDG TPTLWVPDHA
ARRCMGCDSE FWMVNRKHHC RSCGKIFCGS CSNYECPVPE EQFYEPVRVC NSCFSALKYQ
QKVEA
//
