ID H6QTF2_PUCGT Unreviewed; 3048 AA.
AC H6QTF2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Serine/threonine-protein kinase Tel1 {ECO:0000256|ARBA:ARBA00014619, ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|RuleBase:RU365027};
GN ORFNames=PGTG_22077 {ECO:0000313|EMBL:EHS64167.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EHS64167.1, ECO:0000313|Proteomes:UP000008783};
RN [1] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of
CC DNA damage, involved in the regulation of DNA damage response
CC mechanism. Required for the control of telomere length and genome
CC stability. {ECO:0000256|ARBA:ARBA00025079,
CC ECO:0000256|RuleBase:RU365027}.
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:RU365027};
CC -!- SUBUNIT: Associates with DNA double-strand breaks.
CC {ECO:0000256|ARBA:ARBA00011370}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
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DR EMBL; DS178312; EHS64167.1; -; Genomic_DNA.
DR RefSeq; XP_003889212.1; XM_003889163.1.
DR STRING; 418459.H6QTF2; -.
DR EnsemblFungi; EHS64167; EHS64167; PGTG_22077.
DR GeneID; 13541723; -.
DR KEGG; pgr:PGTG_22077; -.
DR VEuPathDB; FungiDB:PGTG_22077; -.
DR eggNOG; KOG0691; Eukaryota.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000178_11_0_1; -.
DR InParanoid; H6QTF2; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
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; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 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, ECO:0000256|RuleBase:RU365027};
KW Chromatin regulator {ECO:0000256|RuleBase:RU365027};
KW Chromosome {ECO:0000256|RuleBase:RU365027};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027}; Telomere {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1978..2568
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2695..3007
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3016..3048
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2975..3006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2404..2431
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3048 AA; 341207 MW; 8185EFD64BA42BCF CRC64;
MAPQNTRISP LDEALSLLGS STVTDRNQGV EQISNLLTNP SNWNSIKESR WAEIFHQLFS
AADTEKAAIL KPSNARKGSI ARASNLNRLR AALTLIRKCV VQFVSLFKHK VMKLVINRTI
ELIVVAKNRT LMDSIVLDCI RILRDFLLYR PHLEHLGHEL SAEILAICFA SILDRKLPET
FSIPDNESFG AEPPLEAEPL NPTDRSQAAS PRMIDSCQLL SIVIPASSSV CLECSKSLLF
DFRNVLEKFP RDTSAHFHLI TALHLLLREL ELNRGRDLSR SAILLGNCLI SLWPNKNIAL
KEQIVLCLTY LLPFVIREAE LDQMNSESQA SPQAEDLVRK ITHVISNDVE LYTKSSSISL
GTLRLVVPRK GFDSSFFCTK GFTRTSCDGV DVAIERVQAV TWAALRLGAS ALNHVTQSTH
QPSARGPETP SKRRKVESEL EIFLQDIQPG SLSAAVVHRI QLLTVTVDLH WENLDNSSRQ
KIIERVLGLL QSDDPVVVSW AFIFFGNTAH CIAPPGNSSS SYQETPPSDS WGPNIEHWKQ
IWSYAIHRTA NPTCSRSASY AAFCILVTHQ LPVHATHEAI HGFLRDLDVQ GPPFPYDSVC
MLISECLALA SEDIQLSAYA LEENVLRWLN KTWPEVDRST ATCNLIGGGS AQRNRRASTA
GFDSEAVFQL LVSIAKLPEI SLPTPMQVPP DCATTEVFAY LQATQSTRSS IFPGIQHHLS
RYDADHSSEP RNVRARLSVH DSSSRCNSKL EIMAILRRSM ERISQEFDQK NVEQTLSAVS
CSHLQMIIKM LIIVILFQAS CQASDSSFDS EIIKFIVSVF DVTIQLVGSS KWSPPERAQL
LACVEPIILP SVNRSATVSC DGLARPGVAS GIRLKERAKL QLGRFDSDAR ACPGSVPLQQ
YEIAASQVWS FSPPVRTQLD AFSKMCERLL QSVSSVAAST APGNAIETYL VQTQATGTTI
NFEEEEEEEL VVGDTLLAQV ESTICNSDGS MKRNFRTGLG SIGTERATLV VASVCVRTTV
TCTRTSTDHP QSARPLPLLS MIIDCVGLEV VYIGSPMLDC IFSGWITLTA DQADQVLQHL
GDTYLSTYTY SQNASVRKLS LQVVQTTLSH WKRAAEGIQE DVELTAHQLV EYMTSQMLQG
TLRSWEVQCE LSRLLDACTR SNLPQTSWAP LVIDEGQDVV SSRPADLMLW FLEDQDYRVR
YRAALYVSRS FELRDSENFH PVEYWRQVVE HLDLAAVQLE ISLTATLCMI NIFVVSEEIR
PRVYHKLLSL LSDPPALPDE VLHYKLGHGL LRRASGQLGF TSTMDLYLFY AAHIARVNLE
QEESPPICSH LCVGHRLKRH QRDELFYGHF LAVGPYLYIA DQKSFKKCAE CATLKEDDAL
RLCCSAIAAE LVARACTQMA SSDCALTGIN DLIEPMLKTM AKNLKLERGI MELESDRVVI
HLMRLVHVTP EGLDAISKIV IRDSTQRNVF GVLTSSLRKH SPCEPALPFY PILRIAQGIK
WIGDGHSLFT EPAFVYNVLC QTFASLTSCY FTNDRLRVLY SLSIFISLSH HTISCSLPIL
SLIIQALSPL ISHDDIFQPV SKFIQWTIMK ALQPSNTELK GHASMAQLII SVADSMKRVA
NSTLSDPPDI ICATEFNSWL LEHVAKTSQS GPLEYQTLCH SLLFNWPESH KIEIEDGAMR
SVLGSSTGPT FKMIHHLHSQ NFPGTAAETG NILYRLLASA QNLKTEIKVE DCQAYLKLLY
QNSGVLSSPR LGESTLAEPN AGFEERSLDS EDEIISRIYA IMVSYLQTYN FPLLWSLTDF
LQRTSSFASL PTLTKSGFSL APLLIEKFRL SCHKSESLEY SVKRVFKSRS PPDFPSLERL
AYSSCHWTRG FLHLLVASRA RARQFYVQLI PLLESNDELA AKFLPQVLHS CLLEEIGSTE
ANLRTKVSKH IRTILTSHST HQDVGIRVLE LVTHLRSHPR PGKDPLGNNK WLDVPWLQLA
KQATKWRMAA SAFLFVEIAR EEGLAIDVTK PLDGDLQSLL ERLYSISPEP DAFYSLIPSN
PTKFLLQRYQ HENQWESAFG FHGALVEDLS IKSRAFREEI PSLAGYLSGN GLNRLAHMVL
QTHNLGQDLS RTYTSEAEKL STLPLELAWR ASVWDLPAGN QVNVDSSTRI YSSLKSCYRD
RENSAQIDIT SSCLLGQFKE LINSTSARVQ PSSKDVGSAL ALSNVLDWLK NPRKDDFESL
VSLPSSFSYD VLERISAVRR SLLQVVTEQK QGEAVQDKIK RTAAREAELK LRIKTSQAAR
QSGNVQAAVN IIIPFSNLTD EEMGGTILHA KEEFAQVLWA KGEKALALNI MKEVQALQKN
LPESAVQLCQ IGEWISLARL NSPMEIVDQY FEKAIKSLDS MKHPEALGEI SYSYAKFADQ
QYHKMEDSEE MKKLRKSTKR LQAEIKGASK LAKVDGGAKR LVALKERLFE EDNNRLESLS
KLQTRYLSSS LTMYLSSLSH YDKADEVIFR FVSLWLEHHY DDALTKGISA HLNSVPTHKF
IPVANQLSAR LSKESSSEFQ KALGDLIVQL CQDHPFHVLF QILLLQRGIE SSCLDSLNSS
RSRRTSNVTA SNTLSPSDRS RAEAANDVLS KIVQTGPRKK VIKELLMVHK AYKEWALHPL
TIGNKGPKSG SRAQIPAHFS VNSLKDLSIP VSTSRISIDK TRRYLPDSIP CISSYETTFT
VASGKSTPKI TTCRGSDGIR YKQLFKGGDD ARQDAVMEQV FELVNSVLER DPECQKRRLN
FKIYMVIPLS PDSGLIEFVK NTSSLLEVLK PVHAKYNQPP DWEFEKLWKY LAIKASAEQR
IKRYQEAITH CRPAMRFWFW ENQKCPQKWY EMRLNFTRSA ATTSIVGHIL GLGDRHLSNI
LIDRVTGEVV QIDLGVAFDG GKLLPIPERV PFRLTRDMVD GFGVAQTEGV FRRCCEQTLR
VLRENKRLIM TILDVLKQDP LQSWIVSKQE EKVKQGAKQD LESSGEEDEE SWDQSMSDAP
EQASRALASV DDKLSSNLSV ETTVNQLILE ATSVENLGSI FCGWSAFY
//
