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Database: UniProt
Entry: A0A1J8PJM1_9AGAM
LinkDB: A0A1J8PJM1_9AGAM
Original site: A0A1J8PJM1_9AGAM 
ID   A0A1J8PJM1_9AGAM        Unreviewed;      2073 AA.
AC   A0A1J8PJM1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AZE42_01077 {ECO:0000313|EMBL:OJA07995.1};
OS   Rhizopogon vesiculosus.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA07995.1, ECO:0000313|Proteomes:UP000183567};
RN   [1] {ECO:0000313|EMBL:OJA07995.1, ECO:0000313|Proteomes:UP000183567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA07995.1,
RC   ECO:0000313|Proteomes:UP000183567};
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000256|ARBA:ARBA00010769}.
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:OJA07995.1}.
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DR   EMBL; LVVM01006478; OJA07995.1; -; Genomic_DNA.
DR   STRING; 180088.A0A1J8PJM1; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000183567; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR   CDD; cd00892; PIKKc_ATR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_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; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR012993; UME.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF124; SERINE_THREONINE-PROTEIN KINASE MEC1; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08064; UME; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM00802; UME; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1025..1580
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          1708..2018
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2041..2073
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          46..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2073 AA;  233374 MW;  4FC7C5BC4B015DDB CRC64;
     MELLRSETWG SSGSELRALA VLYIRGCVSR LDPVSSQAAQ SFLQGNASNC PDSEPLPITQ
     AAGTPTGSPM EEDTGSVDTS HWRAALQNIV STLITPDQLQ WKGFEHDDAT SFYIQRILDA
     IKSRWARGLH DPSSSARITL AENVISFASH LNQFSRHKSS PLGVATALLL PLHRILEGPL
     TEDTIPARRE VFKALRIIFR DHPTDFRSDE PPPVFELLQR GFMDKDRSVR VDAGRALAEL
     VDLHAHAIDR GCRPNEAIFM KIGILLDSNV KDVVKETLLI TVGAIGCGAQ FELLGLVVFC
     LITQLGQRNH ALKGLAYAQL LEIVKKQKKS PYALVSSYFS QVAPFVVCRK LTNPVLIFET
     CRFISVHPRD FISATRFKTL PYLFANCEGK VIEDISKELD EKISVLFTSY PLEILTHTFL
     LHGPGQTNGA LRFITQLLSE STGNNITVFS LVKSFVFQLV ATLLVVGTEN EERATLATDA
     LRKVERTLAD ETRERALADV DLPAFLKTVM LGVVSHLNGM LQDYHGKKSF SLKKQILRGL
     EALIIQIGPS VHGISLQVMA TLQTMLVPEL AEVTLTTWYT FLSTLEVDDV VPHIGATSAA
     IVCAWSVLAP SARELAKKCL RHVVFDIPSN VRSDAGDILN EVVDFSHIPE LSEIHTQLQP
     LRIRDPCMQL NKILDRCSSH NVTVAQMALA ELQNFMRNNH ASLIQNLAVG DAFDSSIGRI
     HSTLFQIVSR HAGVDCIRGL AFECMGILGA VDPDRCEIKS NETRMVMRSN FEDDQEAVLF
     AMHLIQDVLA GAYQSTSDIE YQTQLALTIQ ELLQYCKFTR DLVSSRSTIS VPMQVRNRWN
     SFPKHVLEII TPLLDSRFKL PHNTLPQLPS PIYPHQKTYR EWLQLWTSYL ITKASGDTAQ
     TIFGPFRWAV RNKDVGVSHH ILPHLVLNIL ASENEDDTSG ILQELLTVLH DQVALDSLST
     PDKKFLSAQV VFMLLDHLSG FVRVQRQETT KKPEAKKSRV TLDVKRRQEQ LARVDSVLSS
     IDHELMAKAA LQCRSYARSL MNFERQIVSM RERRPPPPGQ DFTPYYERLH EIYSHLDEPD
     GMEGISTLIL SPSLEHQIRQ HESTGRWTSA QSCWEVRLQQ HPDNLDFHLG LLRCLRNLGH
     YDTLRTHVQG VLVRNPGWES ALVDFQVESA WMIGAWDDVH RIAANEHHQG ASMVKARVLL
     AMRAGNLSLI EENLTRARLV LGAPTAASGI SGYRRAYDAL VDLHMIHELE LIHEAVCNLP
     PSSQGRKSAI VTLSQILSAR LDRTLPTFRV HESLLSMRRT AFSLSSVPRP SITSQIGQSW
     LASAKIARKA GQWQTAYSAM LQAQHSSAPF SFMESAKLVR ARGEPLRALQ ELENSMHILG
     LVDNSNTLDL TRDDEQSKRM KAKAQILLAR WMNESDRYEA SYVLKKFQTA TELAPEWESA
     FYHLGQFQDQ SFRNLPSDDK SNRCSGLKMN LSTIQCFAAA VAFGNKFVYQ TIPRMLTLWL
     DLGEYKKIAE NSNYERINAA IANSIDSVPV YKWFTAFPQI VSRVGHPNRL VYSVLSKLIL
     SVIRGYPNQA LWFFAPVVNS TKTNRQQRGR TILNQLKNDP AHAGSDLPGL ITNLHAMIDE
     LLQLCDYPVE EGRKTLSMKR DFPKLFQMRN HSILIPLQSS LTVNLPPVSS MNNRDKQHNV
     FDPSPPTFQG RIFLQLKVTI VTGLHADFYD EIEIIHSLAR PRKIYVQGSD GTIYMFLGKP
     KDDLRKDARL MDFNGIINKL LKTNSDSRRR QLHIRTYGVV TLNEECGFIQ WVPNTTAVRA
     ELLKYYNGKN AFPSWLSEVT KRIKESTDKE AAELFVTKIL PQFPPVFHEW FVDTFPEPSV
     WLASRLCYGR TMAVMSMVGF ILGLGDRHCE NILLDGITGD LVHVDFNCLF EKGKTLETPE
     RVPFRLTQNL VDGLGVTGVE GVFRIACEIT MQILRDNQDP LMSVLDAFIH DPLVEWEDEA
     RKQRRQVKDA TAAKHGSDLR QWAKTVLRPI ERKLKGLYSP ANLTERTYGG ITTRAGGQEE
     REISISNLVQ MLIQEAVDSA NLGKMYPGWA PWH
//
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