UniProt: A0A444Z7C6

Database: UniProt
Entry: A0A444Z7C6_ARAHY

LinkDB:  A0A444Z7C6_ARAHY 
Original site:  A0A444Z7C6_ARAHY

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (27)   
   InterPro (13)   
   Pfam (5)   
   PROSITE (5)   
   SMART (4)   
All databases (37)   

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ID   A0A444Z7C6_ARAHY        Unreviewed;      2530 AA.
AC   A0A444Z7C6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=Ahy_B05g078540 {ECO:0000313|EMBL:RYR10075.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR10075.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR10075.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR10075.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC         ECO:0000256|RuleBase:RU364109};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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:RYR10075.1}.
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DR   EMBL; SDMP01000015; RYR10075.1; -; Genomic_DNA.
DR   STRING; 3818.A0A444Z7C6; -.
DR   Proteomes; UP000289738; Chromosome b05.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd05169; PIKKc_TOR; 1.
DR   Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 6.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
DR   InterPro; IPR036738; FRB_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024585; mTOR_dom.
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; IPR026683; TOR_cat.
DR   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR   Pfam; PF11865; DUF3385; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF08771; FRB_dom; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01346; DUF3385; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM01345; Rapamycin_bind; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 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, ECO:0000256|RuleBase:RU364109};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2492..2513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1302..1892
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2070..2386
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2453..2485
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2530 AA;  284545 MW;  25C59E340EC8E453 CRC64;
     MAMATPSQSH RYIGPPPVPG TSFDSLNRIL ADLCTRGHPK EGATLAFKKH LEEEARDLSG
     EAFSRFMDQL YDRISSLLES SDVAENLGAL RAIDELIDVA LGENASKVSR FSSYMRTVFE
     AKRDPEILVH ASRVLGHLAR AGGAMTADEV ERQVKIALDW LRGNRVEYRR FAAVLILKEM
     AENASTVFNV HVPEFVDAIW VALRDPALPV RERAVEALRA CLRVIEKRET RWRVQWYYRM
     FEATQDGLGR NAPVHSIHGS LLAVGELLRN TGEFMMSRYR EVAEIVLRYL EHRDRLVRLS
     ITSLLPRIAH FLRDRFVTNY LTICMNHILS VLKVPQDRDS GFIALGEMAG ALDGELIHYL
     PTITTHLREA IAPRRSKPSL EALACVGSIA KAMGPTMEPH VRGLLDIMFS TGLSTVLVEA
     LEQICASIPS LLPTIQERLL DSISMVLSKS HYHPGRPAAS IGRGTVMNVP QQVSELSGPG
     LIQLALQTLA RFNFKGHDLL EFARESVVVY LDDEDGVTRK DAALCCCKLV ASSFSGVACA
     HFGSSRSNRS GGKRRRLVEE LVEKLLISAV ADADVTVRHS IFTSLHGDRG FDEYLAQADN
     LSAVFAALND EDFDVREYAI SLAGRLSEKN PAYVLPALRR HLIQLLTYLE QSSADSKCKE
     ESAKLLGCLI RNCERLILPY IAPVHKALVA RLVDASANSG IISGVLVTVG DLARVGGFAM
     RQYIPELMPL IVDALVDGAA VSKREVAVAT LGQVVQSTGY VITPYNEYPQ LLGLLLKLLN
     GELVWSTRRE VLKVLGIMGA LDPHVHKRNQ KALPGSHGEV TRPASDSSQQ IQCMDEFPVD
     LWPSFASSDD YYSTVAINSL MRILRDPSLA SYHLKVVGSL MFIFKSMGLG CVPYLPKVLP
     DLFHTVRTCE DSLKDFITWK LGTLVSIVRQ HIRKYLQDLL SLISELWSSF TLPAPARPAL
     GYPVLHLVEQ LCLALNDEFR TYLPVILPGC IQIYCTKGIY NICDCLGQKM VNHDDLILGN
     LGTLDEHMHL LLPALIRLFK VDASVDIRRA AIKTLTRLIP RVQVTGHISS LVHHLKLVLD
     GKNDELRKDA VDALCCLAHA LGEDFTIFIP SIHKLLLKYR LRHKEFEEIE GRLQKREPLI
     LGTTTSQRLS RRLPVEVVSD PLDDVEIDPY EDGSDAHKLK GHQVNDGRLR TAGEASQRST
     KEDWAEWMRH FSIQLLKESP SPALRTCARL AQLQPFVGRE LFAAGFVSCW AHLNETSQKQ
     LVRNLEMAFS SPNIPPEILA TLLNLAEFME HDEKPLPIDI RLLGALAEKC RAFAKALHYK
     EMEFEGARSK KMDANPVAVV EALIHINNQL HQHEAAVGIL TYAQQNLDFQ LKESWYEKLQ
     RWDDALKAYT AKATQATSPH VILDATLGRM RCLAALARWE ELNNLCKEYW TPAEPAARLE
     MASMAASAAW NMGEWDQMAE YVSRLDDGDE TKLRGLGNTA SNGDGSSSGT FFRAVLLVHR
     GKYDEAREYV ERARKCLATE LAALVLESYE RAYSNMVRVQ QLSELEEVID YRTLPIADRV
     AEERRALIRN MWTQRIQGAK SNVEVWQALL AIRALVLPPV EDVETWLKFA SLCRKSGRIS
     QARSTLVKLL QSTTPPPSFP QYDPEMSAEN VRYHGHPQVM LAYLKYQWSL GEDSKRREAF
     IRLQSLAMEL SSALSIQPVS SSGFTSGLSP TVPLLARVYL ILGSWQWSLS PGLDDDSITD
     ILGAFEKATH HANKWGKAWH KWALFNTAVM SHYTLRGFPD FAARYVVAAV TGYFHSIACA
     ANAKGVDDSL QDILRLLTLW FNHGATAEVQ MALTRGFSLV NINTWLVVLP QIIARIHSNN
     HAVRELIQSL LVRIGQNHPQ ALMYPLLVAC KSISNLRKAA AQEVVDKVRQ HSGVLVDQAQ
     LVSKELIRVA ILWHEMWHEA LEEASRLYFG EHNIEGMLKV LEPLHEMLEK GAMENNVTLK
     ERIFIEAYRQ ELLEAYECCV NYKRTGKDAE LTQAWDIYYH VFRKIDKQLQ SLTTLDLEAV
     SPELLECRNL ELAVPGTYRA DAPVVTIASF ARQLVVITSK QRPRKLTIHG SDGEDYTFLL
     KGHEDLRQDE RVMQLFGLVN TLLENSPKTA EKDLSIERYA VIPLSPNSGL IEWVPNCDTL
     HHLIREYRDT RKITLNQEHK YMLSFAPDYD HLPLIAKVEV FEYALNNTEG NDLARVLWLK
     SRTSEVWLER RTNYTRSLAV MSMVGYLLGL GDRHPSNLML HRFSGKILHI DFGDCFEASM
     NREKFPEKVP FRLTRMLVKA MEVSGIEGNF RSTCENVMQV LRTNKDSVMA MMEAFVHDPL
     INWRLFNFNE VPQMSMLTSN HVPPVVNAEE SAPTRELAHP QRGARERELL QAVNQLGDAN
     EVLNERAVVV MARMSNKLTG RDFSTSSAVL NSSLQHAMEH SSLISGDTRE VDHALSVKLQ
     VQKLIVQATS HENLCQNYVG YEKFKNECSS SIVVPFLVNL MGAVNIVYNL YIVKTPRGYC
     EIRFLPRIYV
//

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