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Database: UniProt
Entry: A0A178E849_9PLEO
LinkDB: A0A178E849_9PLEO
Original site: A0A178E849_9PLEO 
ID   A0A178E849_9PLEO        Unreviewed;      1162 AA.
AC   A0A178E849;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=IQ07DRAFT_563599 {ECO:0000313|EMBL:OAL51489.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51489.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL51489.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51489.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441642; OAL51489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E849; -.
DR   STRING; 765867.A0A178E849; -.
DR   InParanoid; A0A178E849; -.
DR   OrthoDB; 5477649at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd00180; PKc; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45641:SF1; NEPHROCYSTIN-3; 1.
DR   PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   DOMAIN          65..377
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          767..800
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1162 AA;  130263 MW;  378B425D600560BE CRC64;
     MAEFTHNTEF YAHGSQLGKR LLSSDVLFQS SSAIQSVAGA GPIAHCNFIY FCGLVQGLGL
     DFLPITWQPY VGLGGSGATS KIRQSLLGTD LSLAFKSISV SDTSRAYTPS EKQILFALFI
     SEIKHMANRA VLMSPHIQHV DGICWSLSSN TGAVDPVLVY ERASHGDLYH YMSSGEGEKA
     KNIYARIETC RDIAIGLHTL HSCDIVHGDV KPQNVLMLDI DHEFVAPKLC DFGYSTAYTD
     PNSTITVSRT IPWNAPEVGN NMGGYLPQEA VKTDVFSFGM LCLWTLFCKQ FEGTLGIASD
     FTDISGSQGQ SPTFKRITRL KLEDQLRPFC RDAIEFLALE PKQKESLNQL FDITLSPDPH
     RRASDVDQAR VLLDQCLADP SGWPFGETPQ GDAGIEQIDM EQHFDFQISA SIVQLLRADF
     RIRQYITKSL IEEAKGSNCV SCKSNAAFQL SVCFSIGFGI PANYDSSRNW LHRSGKSEVD
     LTNQLELIKE FSWVEHPYTY HTHFLNNLHN EGFIRNIDYL DTYMSCLTLL EVKHEYEREL
     EDLAVALGEA AVPYLTLHQV YAVILKAAGN YQDAIKIHRR DLEVLKGRDD FDEGRHDMPN
     IMSELADLYL LQGDFETSAH YCKSVKELRT SIFGPNHPLT LVSLHLEGKL LAETGNVEEA
     ERTLKIVLEY RKATLGLNHQ ATLNVMCDLA SVYSRQLRYE EAITIIEEEI HIRTSLLGPH
     HHSTLSTLCD LANVLIDTDK LNHAQKLLDQ ALFGLPKSLG EDHVATSAVL AGFGALYLKL
     QDYDKSLECY DTALLAIERT LGQNHPVAMN LIRSKAVLLA EMGSDIDEPK ALFQQSLRYQ
     ETSLGEGHPE TLVNLSEYCT FLLEHDCLEE AEKCYRILLQ RQETHLGMRH IAVAATLCEL
     GQTLERMENQ EAETTMRHAL DVATDFIEGK HVLGWKCMEQ LAEYLHKKDI NLEESKELYE
     RSIAEKEADG DFEPMERYAP LHSLVDLCLD LQNLTRAIEA QRKIITIADT FEGEYADERM
     KTRAQLAQIL DKAGELCEAE IAYRDALSHS PRSCNENVND ILECTAKLAW CLERQNKHDE
     ARTLIDQAME GSETLQVLEV PVRHTVLLGA AAVYSRQGDQ PLAISLSQKV VEECSTLYGV
     ESEETCAAVK THARYSNQPQ HS
//
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