ID A0A2K6FQ55_PROCO Unreviewed; 2639 AA.
AC A0A2K6FQ55;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein kinase ATR {ECO:0000256|ARBA:ARBA00024420};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=ATR {ECO:0000313|Ensembl:ENSPCOP00000016121.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000016121.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000016121.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769}.
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DR Ensembl; ENSPCOT00000026743.1; ENSPCOP00000016121.1; ENSPCOG00000019808.1.
DR GeneTree; ENSGT00940000155714; -.
DR Proteomes; UP000233160; Unplaced.
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 GO; GO:0080135; P:regulation of cellular response to stress; IEA:UniProt.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00892; PIKKc_ATR; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR021133; HEAT_type_2.
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:SF128; SERINE_THREONINE-PROTEIN KINASE ATR; 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 SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 803..837
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1638..2183
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2291..2599
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2607..2639
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 427..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2639 AA; 300898 MW; EECFBBF56F9E303B CRC64;
PRVLGLQVLA TVPGLKTFYL YFSAAPEEYN TVVQKPRQIL CQFIDRILTD VNVVALELVK
KTDSQPTSVM LLDFIQHIMK SSPLMFVNVN GNHGQNEAKG SCIEFSNWII TRLLRIAATP
SCHLLHKKIC EVICSLLFLF KSKSLTIFGV LTKELLHLFE DLICLHRRNA VGHVEWPVVV
SRFLSQLDEH MGYLQPAPLQ FMNMQSLEFI EVTLLTVLIR IIATVFFRRQ ELLLWQIGCV
LLEYGSPKIK SLAISLLTEL FELGGLPAQP ASTFFSSFLE LLKHLVEMDT DQLKLYEEPL
SKLIKTLFPF EAEAYRNIEP VYLNMLLEKL SVMFEDGVLM RLKSDLLKAA LCHILQYFLK
FVPAGYESAL QVRKVYVRNI CRALVDVLGI QVNAEYLLGP LYAALKMESM EIIEEIECQT
QQENLNSNCD GISPKRRRLS SSLNSSKRAP KQNEEIKHVD MSKKSILWSA LKQKAESLQI
SLEYSGLKNP VIETLEGIAV VLQLTALCTV HCSPQNDCQH KSEKKPSVVI TWMSLDFYPK
VLKSCRSLLE SVKKPGLEAI IDNVVKIYDA LIYMQVKSSF EDHILEDLCG MLSIPWIYSH
SDDNCLKLTT FATNLITLSQ RISDSYSPQA QSQCVFLLTL LPRRMFLEWR TAVYNWALQS
SHEVIRASCV NGFFILLQQQ NSCNRVPKIL IDKVKDDSDI VKKEFASILG QLVCSLHGMF
YLTSSLMEPF SVHGRVDLFC KNLKATSQHE CSSCRLKASI CKPFLFLLKK KTPSPVKLAF
IDNLPHLCKH LDFREDETDV KAVLGTLLNL MEDPDKDVRV AFSGNIKHLL ESLDSEDGFI
KELFVLRMKE AYTHAQISRN TELKDTLILT TGDIGRAARG DLVPFALLHL LHCLLSKSAS
VSGAAYTEIR ALVAAKSVKL QNFFSQYKKP ICQFLVESLH SSQMTALPST PCQNAEMRKQ
DVAHQREMAL NTLSEIANVF DFPDLNRFLT RTLQVLLPDL AAKASPAASA LIRTLGKQLN
VNRREILINN FKYIFSHLVC SCSKDELERA LHYLKNETEI ELGSLLRQDF QGLHNELLLR
IGEHYQQVFN GLSILASFAS SDDPYQGPRD ITSPELMADY LQPKLLGILA FFNMQLLSSS
VGIEDKKMAL NSLMSLMKLM GPKHVSSVRV KMMTTLRTGL RFKDDFPELC CRAWDCFVRC
LDHAYLGSLL SHVIVALLPL IQIQPKETAA IFHYLIIENR DAVQDFLHEI YFLPDHPELK
KIKAVLQEYR KETSESTDLQ TTLQLSMKAI QHENVDVRIH ALTSLKETLY KNQEKLIKYA
TDSETVEPVI SQLVTVLLKG CQDANSQARL LCGECLGELG AIDPGRLDFS TTETQGKDFT
FVTGVEDSSF AYGLLMELTR AYLAYADNSR AQDSAAYAIQ ELLSIYDCRE METDGPGHQL
WKRFPEHVRE ILEPHLNTRY KSSQKSTDWS GVKKPIYLSE LGNNFAEWSA SWAGYLITKV
RHDLASKIFT CCSIMMKHDF KVTIYLLPHI LVYVLLGCNQ EDQQEVYAEI MAVLKHDDQH
TISTQDSASD LCQLSTQTVF SMLDHLTQWA RHKFQALKAE KFPQSKSNRD KVDSMVSTAN
YEDYQSVTRF LDLIPQDTLA VASFRSRAYT RAVMHFESFI TEKKQNIQEH LGFLQKLYAA
MHEPDGVAGV SAIRKAEPSL KEQILEHESI GLLRDATACY DRAIQLEPDQ IIHYHGVVKS
MLGLGQLSTV ITQVNGVHAN RSEWTDELNT YRVEAAWKLS QWDLVENYLA TDGKSTTWSV
RLGQLLLSAK KRDITAFYDT LKLVRAEQIV PLSAASFERG SYQRGYEYIV RLHMLCELEH
SIKPLFHQSP GDSSQEDSLN WVARLEMTQS SYRAKEPILA LRRALLSLNK RPDYNEMVGE
CWLQSARVAR KAGHHQTAYN ALLNAGESRL AELYVERAKW LWSKGDVHQA LIVLQKGVEL
CFPENKTPTE SKNMLIHGRA MLLVGRFMEE TANFESNAVM KKYKDVTMFL PEWEDGHFYL
AKYYDKLMPM VTDNKMEKQG DLIRYIVLHF GRSLQYGNQF IYQSMPRMLS LWLDFGAKAY
EWEKAGRSDR VQMRNDLAKI NKVIAEHTNH LAPYQFLTAF SQLISRICHS HDEVFVVLME
IIAKVFLAYP QQAMWMMTAV SKSSYPMRVN RCKEILNKAI HMKKSLEKFV GDATRLTDKL
LELCNKPVDG SSSKLSMSTH FKMLKKLVEE STFSEILIPL QSVMIPTLPS IPGTHAHHDP
FPGHWAYIAG FDDMVEILAS LQKPKKISLK GSDGKFYIMM CKPKDDLRKD CRLMEFNSLI
NKCLRKDAES RRRELHIRTY AVIPLNDECG IIEWVNNTAG LRPILTKLYK EKGVYMTGKE
LRQCMLPKAA ALSEKLKVFR EFLLPRHPPV FHEWFLRTFP DPTSWYSSRS AYCRSTAVMS
MVGYILGLGD RHGENILFDS LTGECVHVDF NCLFNKGETF EVPEIVPFRL THNMVNGMGP
MGTEGLFRRA CEVTMRLMRD QREPLMSVLK TFLHDPLVEW SKPVKGHSKA PLNETGEVVN
EKAKTHVLDI EQRLQGVIKT RNRVTGLPLS IEGHVHYLIQ EATDENLLCQ MYLGWTPYM
//
