ID A0A1Z5T4R1_HORWE Unreviewed; 1814 AA.
AC A0A1Z5T4R1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=BTJ68_10953 {ECO:0000313|EMBL:OTA30851.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA30851.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA30851.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA30851.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RSE1 family.
CC {ECO:0000256|ARBA:ARBA00038266}.
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:OTA30851.1}.
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DR EMBL; MUNK01000128; OTA30851.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5T4R1; -.
DR VEuPathDB; FungiDB:BTJ68_10953; -.
DR InParanoid; A0A1Z5T4R1; -.
DR OrthoDB; 101343at2759; -.
DR Proteomes; UP000194280; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR PANTHER; PTHR10644:SF1; SPLICING FACTOR 3B SUBUNIT 3; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00022728};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 1242..1642
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 854..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1225..1252
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1641..1658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1814 AA; 200382 MW; 572C3697FC6C65AC CRC64;
MANVQQTQSF YSLTLTPPSA PSCSVTCNAI PGLKTQDQQI FEARGQRIYL HRIVENEDRS
EVKLSTVLDQ DVFGIIRGVS AFRIPGTATD QLVVSSDSGR MSMLNYDVDK NAFRRVHLET
FGKSGVRRTV PGQYVASDPR GRCLMLASTE KNKVVYMVNR EPDSTIRISS PHEANQWASL
CFGICALDTG WEHPIFAALE VDYSEAEADS SGIEYERREK HLVYYTVDLG LNHVIKSWSD
TVDYSANKIF GVPGGQDGPS GVLVCCEGRI YYRHDKAEGL SIPIPRRSGP TEDPERKRII
VSGCLHLSKA RHEFFFLLQT EDGDVFKLTL DMAEDAQGRR TSQPVRINLK YYETFPVAKT
MLLIRKGYIY TASEHGDSKL YHVNDLAEDM DFEPHNNFSS DDVSPDPADA YTPTFFKPRG
LTFTSLATTQ PSLHPLMKTK VDNLTGEDAP QIYAIQGSGA NSRFKTLRHG LEVQEIVSSP
LGNIPFDNLW SLRHRASDDY HSYLLLSSAY GDKTIVLSIG DEVETMEDSP FLTNRATVTA
QTMGDATLVQ VHARGVLSIL ESGAVNEWPS PAHRTIVAGS ANSRQLLLGL SSSELAFFFM
GDDGVLNQLE EMPEMSGKIT ALAVGATPPG QLQAKFAVVG CDDCTIRVMS IELDSPLEPK
SVQALSAMPT SIEVVSMRDP SSGTLTNYVH IGLQSGLYLR ATIDEVTGEL GEVRTKFLGA
RPTRLFPVDV PGQAQHADDA ASSSAILAAS SPPWLGYNHP VSDLYTLAPL VTSQLEAARP
FASEHLKGLC AVQGGNLLIF GVEGVEGGLL SSKDIPLRYT PRAMSRNPWL PVWYVAQAEG
NTLSEGTKKG LLEGAGAKKE EDGQNGAEVK MEDSTEGEMS PAELDKHLGL SRAPGHWASC
VQVVDPTAEE PVCTLELGEN EAALCCAAVP FESKEWDIYL AVGTGQHLRP GEPVVGEKPK
GYVHIYRISE EGRKIELVHK TPFPTPIYAL HPFHGRLAIG VGNELFIYDL GLKSLLRKSR
GTVVPNLITS IDSRGNRLIC ADISESLTFI VFKPAHNRLI PFVDDTIPRW STALSVLDYE
TAAGADKFGN LFVLRVPEQA SKESDEEGVG GYISNERSYL NGTPYRLDLR AHVFTNDIPT
SIQRTPLVPG GQDVLFFSGL QGTMGILVPF VSREDVEFFA QLEMLLRAED PPLAGRDHLM
FKGYYVPLKG VVDGDLCERF LRLGMDSKVR VAAELEREVK EVERKVLEVR GRVACLWQSV
LAPFRLLDLS AQAVKRPKSM DPDKKIEEET VPNYDSSGYY PVQIRDVFQN SAENFKVLKI
CIHQDGNSLR EQDAYAQLFS GFRTSNEGLF YTRIPQKRFE VTGPSGYQHA CFVFVPAACT
LWEIMKHYDG PMNLNLIKYT VLSAIKALDF LHSDAHLIHT DVKLDNMFMS LTDDAEVEVL
ASYLVENPPE FKVDETGRKI YQGYNLRNLG QNSWGHAMLG DLGEAYVFDE GEDDGLLGPS
IVAPAVLRPP EVILGMKWGT PLDIWQIGCL FFLLLNTRLP FQNFAGAERW SGCYHLTQMT
ALMGPPPEDY LARSEEQYLE CDETCAWRCP GSKGVPDMSF EALLERFEGE DKTAALDFVR
CIFHWKPEER STAKELLQHP FLNFDKEDTE KEGTGESSAE EASAEEADAE TDAEDIKSEK
TSPTSQCNDS KTLKDCTDVS ESQKPSEEVV ASLDTLVGTH GVSDVGGESQ QDSSHVRKSP
ENKVPVREEQ GGVEGTSEAP KSEESEDSKE EPEQTAADAK KGCDGRVVDE PRLKPLEEFA
DLQIRPAESL QRKQ
//
