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Database: UniProt
Entry: G8BN48_TETPH
LinkDB: G8BN48_TETPH
Original site: G8BN48_TETPH 
ID   G8BN48_TETPH            Unreviewed;      2450 AA.
AC   G8BN48;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Serine/threonine-protein kinase MEC1 {ECO:0000256|ARBA:ARBA00021345};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   AltName: Full=ATR homolog {ECO:0000256|ARBA:ARBA00033001};
DE   AltName: Full=DNA-damage checkpoint kinase MEC1 {ECO:0000256|ARBA:ARBA00030459};
DE   AltName: Full=Mitosis entry checkpoint protein 1 {ECO:0000256|ARBA:ARBA00029679};
GN   Name=TPHA0A02430 {ECO:0000313|EMBL:CCE61326.1};
GN   OrderedLocusNames=TPHA_0A02430 {ECO:0000313|EMBL:CCE61326.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61326.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE61326.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR   EMBL; HE612856; CCE61326.1; -; Genomic_DNA.
DR   RefSeq; XP_003683760.1; XM_003683712.1.
DR   STRING; 1071381.G8BN48; -.
DR   GeneID; 11532380; -.
DR   KEGG; tpf:TPHA_0A02430; -.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_000178_4_0_1; -.
DR   OMA; IEYCKKW; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000005666; Chromosome 1.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00892; PIKKc_ATR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic 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; 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; PS00915; PI3_4_KINASE_1; 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:UP000005666};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1481..2027
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2131..2434
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2418..2450
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2450 AA;  284417 MW;  B41A692742B977B9 CRC64;
     METHIKYLDE LIHAIKESRL DTTDDNDFRN NSHLNKCQKF NIPEDNLREQ KSLKIMVTLI
     SNLKENTISS YNNNNNNNNN NNNNNKNSLF VENSDLIFNK SIKAIDLLIK SKPYLLWTSF
     SIANSQYSKL ESNDYGIISL FEQFTQIAIL NINLSNNNKE DNKMCKSRLW LLRKKLTEWC
     GLTSCLHSTT LKVSLSTFIL NRLNSIEKQL TEIVMTTNIN TDELYKMLKE LYVLLYFLSG
     QNDKFSNSLT FFDSVSVVNN WDFYFQRSIR IVLFIFGSIR LDLDRPLYLA VLRLELLYFS
     LITDYALSGT IKCGSQLKIG STSKLIFVLT TMYQFMKMLQ GMVIEEDDTI AKGLLRVYLI
     CISGINANDK NLQQEYSAKF SNQFVNIFKE YLPLDKWLNL NKLDENSMKE VQFNSLSQKS
     MLIILFDIKR RCSKENELEF DENNRIWTIK NDLVDKYILH HVISPFSNDQ IQLENLRKRL
     IKSFDERVNK KVTELKLLLN KVCPGLLGKY ETDITDLLEE ILARVKISVT TNQQHELVMW
     AKVLGLLTCY QVSREKDKSL DIHNWEQCDI CDDNTAHNNF KTIRPDRADA FKFSETYKIM
     LKYYLSNVNS INFSVATKAS ILVCMRRIFM HYQPPKLKME SNEIVAEGPC NIFEIISKTF
     TGEDRYLRIL SGKLIPLLNI SASHNSEDQH TALLVQFLQS QKNAYLTEVL ISTWIELTLT
     TSDEIFDTLL LKLIDIFNSA DYTIHNMMKF QIKSMAKTLN KTPYQLLSPI LPILLRQIGK
     NLVERKLTFQ RLIELLGYSP KTILEIYQRY IVPYALTQYK SDAFTEIAKL MSDNDPERMN
     IVKANLLEKN SRQIFAVALV KYGLFSLETL EALFLNRLPT FDKGYISAYL PDYRTLAEFL
     KLYKNNEFDE VTGNENEKTI ICALRYLVTD FEKDKRHGSK YKNIKDWDTQ REEKFQKKLQ
     DNILGIFQVF SCDIHDVEGR TSHYEKVHVV NGISFLIKHA NKKSIISALA QISICLQTAI
     EIDEVRFSAL RCWKLLVVSL SDEELSTVID SLISYILENW STFNYKIRST IYEILDILIK
     DKSNLVMNIK PFIMIALVNK TELGILVRNN TFARMVSKIR SITDWIPIFA DNLKSNNKYV
     IHQTLNNIEL FLKRKQTERS YTFFTNVKQQ SNVTLLLAGL IDASYKFRSI DKSLSEQCTR
     CIGLIGTLDM NIYDMRKSMS SENKVYDLND EVQTIKFLVW MLDNILVPAF WQSENPSKQL
     FVALVMQESL KFCGLSSASW DINKPELYPN EIKLWSKFNT ISKTTLYPLL SSLYLAQSWK
     EYVPLKYPSY NVKEGFKIWI KSLTLDLLKI GTGEDHPLHV FSSLIREDDG TLSNFLLPYI
     TMDIIMKADP TSIYEEIMHN LIIEFQFIFN YDLVGLNHHQ IESLKMCFES IFNVIEYCKK
     WMTQFKQNYN DSYGTFIIKE ERFLRMLNRT ENFLEAISAN LLAKRSLETN SFERSALYLE
     QCMRDSKKST TVTDPNLLLS LQTTYEEIGD IDSIDGLLKT FSTDNLSSKI QELQYSDSWK
     MAQYCFESLG NHTEEKHATS KMLKLDFDHQ NYSKVLMNIS PKLPATSMTI DKEMVEWYKM
     GIESANLVGD ITILKSWLGN IETLISVSDP ELLLGYNVGK ALSYVNTNQP EKIKNYINKC
     FKLIGMHFTA PCREISFIKM QDLLMKLHGL YDINILSNSR DRFLFDCNTS LLDFRMKRVG
     ADFVPNHYLL SIRKSFDSLR DVEYTSNDLA KSYFKISQLS RKNSRLDLSC KSLMSCLKFG
     QHGEELEFAE ILWTKGENDR AIKLLKEIHE RYQNDLTIEP RDKAIILLKY TEWLDQSNYS
     SSEQIIKQYG DVLDLDPQWE KPYYSMGLYY SRLLERKKAE GYETNGRLEY KSISYFLLAF
     EKNSIKVRET LPKVVTFWLD TATGAMNEPE GHRKEVLVKT TEDICRSIEN SLQSCPKYIW
     YSVLTQLLSR LLHSHSLSSQ LIMNILLNLA LEYPSHMMWY VSVLLNSTSK ERVKRGKYII
     EKYGTHCKNV QHIIQSADLV SAFTTVCLKE LKNTSTRSGR SLEKDFNFNM NMAPSSMVVP
     VRINLEMLSP LISESMKTYQ PFGSLVTIAR FGSSYKVFSS LKKPKKLNII GSDGKIYGIM
     CKKEDVRQDN QYMQFATTMD FMLGKEIGAT KRNLGITTYS VLSLREDCGL IEIVPKVVTL
     RSVFVTKYES MKLKYSLKGL YDQWQNVPPD QKLGFHKTQL EKFPPVLHQW FLETFPDPIS
     WYNSRNEYSR SYAVMSMVGY ILGLGDRHCE NILLDVETGK VLHVDFDCLF EKGRRLPVPE
     IVPFRLTQNL YDALGIMGTE GTFKKSSEIT VSIMRQNEVS LVNVIETIMY DRNMDYSIQK
     ALKVLRNKIR GIDSRDGLVL SVPGQVETLI QEAASIENLS QMYIGWLPFW
//
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