ID A0A0V1A913_9BILA Unreviewed; 1416 AA.
AC A0A0V1A913;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
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 Flags: Fragment;
GN Name=mtmr4 {ECO:0000313|EMBL:KRY21328.1};
GN ORFNames=T12_4477 {ECO:0000313|EMBL:KRY21328.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY21328.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY21328.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY21328.1};
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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:KRY21328.1}.
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DR EMBL; JYDQ01000017; KRY21328.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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: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:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 569..959
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1349..1409
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1088..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 798
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 712..715
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 737..738
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 798..804
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY21328.1"
SQ SEQUENCE 1416 AA; 158584 MW; 42383865807051A2 CRC64;
LMNTEEMLEQ EGDRLEMNCS QKALTAIGIE GSANKIGVGI VRQGEVLSNC RRTYVTAPGQ
GFQPSDTAVH HRQHVLGLVE QAISEANVNV GQIDLVCFTQ GPGMGAPLVS CAVVARTLAQ
LWNRPLVGVN HCVAHIEMGR LVTGADDPVV LYASGGNTQV IAYSDHRYRI FGETLDIAVG
NCLDRFARLL NLSNDPSPGL NIEIQARNGR KFVQLPYCVK GMDVSFSGIL SSVEQQLSLL
KRGEIQPADL CFSLQETVFA MLVEVTERAM AQCGSKDVLL VGGVGCNGRL ISMMRSMAED
RGARLHASDD RYCVDNGAMI AHTGCSLRSH NVRSDFVPMK FWSHGVTEKA SSNYPFNNAN
LKLSTSTVNL YSRPYWMEER PPLPPDSVAV ANSEFPGVEN VSRTEAFSRK PLHKLTVHGK
FEPYEEENYP FPVPFLPGEY AEYFSEPFED SVRSSFVVLT NFRIFVTASG NGSFYNIPLL
CIESVDYREN AYVSIFCKDG RTAKVTLENN DFTLAWYRLL NSVAVPPAKL EDVFAFAFYA
WCLDEKKKPS FASLQNKINN DQADDYFFFD SKEFVQQELN RMGFPKEHWR ITEFNKNQEF
CPTYPSYWIV PALVTDADIE GSCRFRALQR VPVTVWRHPK EGCVLVRCSQ PESGILGWRS
DSDETLLNMI NSTASLKATP KDGAPLTPVE TNKPVKPMLI LDARSYTAAW ANRAKGGGFE
ICEYYNKCDI QFLGLPNIHC IRVSFQKFRS SIMEANESTW FQNLETCQWI HNLCALMTSA
LRAVEALQVE KRSVLVHCSD GWDRTTQIVS LAKLLMDPHY RTVKGFTELV ERDWICFGHK
FRERLGMQNG DQNQRSPVFL QWLDCIHYLL HEYPCSFEFN EIYLVKLAQH AYSGLFGTFL
CNSIAERRQL TIPQRSFSVW DYLNVSNGQF RNILFSHDDS VLWPRLGLRE MAALWRAIYF
PGNGDTVNGG GRRLCIAGSA TVSAMHANND EDDDHDAGFV GHCRLTVERS IPTVLIRSHS
CDSVPLADFQ RPGFFPEPAF HRLGSQPCLV TNSSTSAFRL LPKSQQSDTA DVGFLDCAQV
AGSDRPTRLA LLSNGDSGPQ TPQRCRRAML NGSKSSSTSV DFDHERDDDT DGERTTDVES
SGVAQTCDHS TSTTEISDPR AIRPEIGIRN VVHYHRIQPN RQLVNGNNSG DGQSDQNQRC
RSDDCCVGGL SSNQRQALAE MLDRDGLIRV RDGAQERMQK IMHRYEKRIA FLQTELFRAQ
TACAYGKCPT CDQRTATVVD FSSSTDPIMA VVMEGRDQTR TRNSESQSAL SENGAEPRSC
DSRTTTQSDA SSWEAVDCED GTPTLWVPDH AARRCMGCDS EFWMVNRKHH CRSCGKIFCG
SCSNYECPVP EEQFYEPVRV CNSCFSALKY QQKVEA
//
