ID A0A0V0TRN5_9BILA Unreviewed; 1460 AA.
AC A0A0V0TRN5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
GN Name=MFSD1 {ECO:0000313|EMBL:KRX41287.1};
GN ORFNames=T05_8918 {ECO:0000313|EMBL:KRX41287.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX41287.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX41287.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX41287.1};
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=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00036767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000256|ARBA:ARBA00036767};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004308}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00037860}.
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:KRX41287.1}.
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DR EMBL; JYDJ01000175; KRX41287.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:InterPro.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 3.90.1030.20; DNA polymerase delta, p66 (Cdc27) subunit, wHTH domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR019038; POLD3.
DR InterPro; IPR041913; POLD3_sf.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF09507; CDC27; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX41287.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1352..1373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1394..1416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1428..1454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 573..846
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1355..1460
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1034..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 164868 MW; B481C6370E6B6BEC CRC64;
MSGCMDNESA QQCCHVKNQK EQFCIKCSLA DAFNLADNEI SLIGNSNVSK GLSKNSLIPS
SETVSSASDC SATVNPTVDV QNKDDNSSVI DVPVESPIRC ESESISVDLN NASSTPKQSL
LLRLFESNLF NMHIAIQYLF KSKEPGVLTY LGNRLFSYPD ADVDFYLPQL INLYLNVREV
ADVLHPYILH RYSLGFVNCV VDLHILFIFC IFFGCRKSVE FSLHVSWLLE AYGVDSYRGC
KRKSHGLKLK NLILSEQIKT KRCTVNVSWK SNQIASNPVE KKGHHRSRSD ATVQYSNPGG
SLKREVSISS FRSLYLSPGD LTTGRAFDSG CCCFDSDSCL VTSLQKSFLR CVCEASRLTP
ELEFVRSLMA IGNRLRSIPD RNTRCTRLIA ELAMLNLNLP ARVWLPLYSS EFCHLIVRIP
PNAGVILNSK DKAPYLLYVE TVDIDAELLF PASSKLYPDG KLGRELSKSA ENLHSADWNN
CEIQPKPVYS SFSSISANGD DDDLHKQFVF EKLTICDTLS QMSVDSNASG DSREPSALVS
ASDIRRRLTE SLSAPTKQLK HSTEDPSASI LSEPWDEKLK RVRESSPYGS LSGWRLLPVI
VKTGDDLRQE LLAYQILRQL QDIWKLEHVP LRLKPYRILV VSRDSGMIEP IVNAVSLHQI
KKHQIADAKA NHTLLDYFKK KFGDFNSEEF LTAQNNFIRS CAAYCLVCYL IQVKDRHNSN
ILLDTEGHII HIDFGFILSS SPKNLGFESS PFKLTDEIIE VMGGCESEMF HYFKILMLQG
LIAARKHHDR ILSLVETMLS GSQLPCFRGG ATVMRDLRAR FHTNYTDEKL HALVDDMVET
SRRSITTRLY DNFQYFTNGI LRNIQLDEVD CPAGDFSFRF KRRKTNELTV SDIKKKDELQ
RSINVGRSGV CGKASGMVTF LWLSGQLNVH VNKAKELLKQ YYIDHLSEKN ITAVFYLSGY
KYLGVHRILR IFHAREEHLD LLKSHLDEIL SCHIYSVQCC PLKDICGLFA SDMQSIMPSN
DLLPISPLHI GYSESRTEQS KTNEQQPTAE KCKAPKVVES TAEAGQFESQ REQTEQKKRK
ADDALLEASG EKEKLQKISS KKGKDRTKGR AVDKVEQEGV VHGNGSENGG SLPSVHKTVK
RRKRNKKVEE EKLVHIGRGR SSTPSDDEND QQNVKVDLIN DDEEEIKLHK KNQNTADNGD
LNSSGESETN NPGPARIKRM KTTYKTYIDD KGYLVSKRIR EMETVDADKC DVIDKHTDVA
DNKKLTSTVK GPKKQTSLAN NISMKYTEKM DLKVLSESRV NESQQQLTAE ENNEQQQHVI
SECDLQNTCD TVDRDERQVS PFLAAKFPHD RWYFRFYILV LVCFLNLGNY LIYDAPAALS
SDLRKDMNIT ISSYNLLYDV YSWPSIVLAF VSGVLIDRFL GLQYGGILFA LIILVSQIVV
SVGAFENLLW IMVFGRFIFA
//
