ID A0A163EDC8_DIDRA Unreviewed; 670 AA.
AC A0A163EDC8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=EKO05_0000114 {ECO:0000313|EMBL:UPX09425.1}, EKO05_000109
GN {ECO:0000313|EMBL:KAF9712379.1}, ST47_g5213
GN {ECO:0000313|EMBL:KZM23645.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM23645.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM23645.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM23645.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9712379.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712379.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9712379.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712379.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9712379.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9712379.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX09425.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX09425.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) 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};
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DR EMBL; RYYQ01000002; KAF9712379.1; -; Genomic_DNA.
DR EMBL; JYNV01000189; KZM23645.1; -; Genomic_DNA.
DR EMBL; CP095288; UPX09425.1; -; Genomic_DNA.
DR STRING; 5454.A0A163EDC8; -.
DR OrthoDB; 5491350at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 1.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:UPX09425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:UPX09425.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZM23645.1}.
FT DOMAIN 487..617
FT /note="Serine/threonine-protein kinase haspin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01331"
FT REGION 32..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 75276 MW; 36EA086B68D932B5 CRC64;
MPPRIVYGKK ATARPVSASY IKFLSPGEDQ LFSSTNKEEV QTQTNKGSSQ SARTTEERIQ
DELVALEAQL GGLAIDNDII KQDGLPVEKK LTSRSRKVLE DRDANTVPKK TSEHIEKPDK
AELKGTTQPT ELATPPQTPV ARPRKKRSKP TTTKKRAQPP TPESTPEHDD VHVRYISPLF
SFSDGKRITT FEQWSSELEP HFKITKIAEA SFSEVYRLSA ISATAGLGEE SVLKVVALKT
PPEAPLPCQT LERAIRDRKG QMAKELEERE EKDAYKSHVA DVLSEVKLLQ NLNQIPGFTN
FRALTVLQGR PSSSFNNAWK VWNKARPRGK KSYFPDPSKK TSYEDTQLWA VIEMQDAGMD
CEKLMESEGL GTIWEVWDVF WGVCMSVAKA EEACQFEHRD LHMGNICVRS SRPESDVAMP
TAKDPLRRRF RFTGLETTVI DYTLSRADIV THQQTPTSSP STLDAASQPR PHFTGNEVAY
LDLNKDPALF EGDAAEEYQY EIYRYMRGAA LYDNPLQSEP CPEPKVPTTP RPAPKKNIHI
RFGEIPETPQ KPSLETATDT NVWRRFHPKT NLVWTHFLLH KLLNHLKGYE PEHQSTTDIM
ANVDLGDDAS IPGAALRVKK KAIKLHRVLQ RVSELLCPVA LGQAGSLKSV KELVILAVEE
RWLRVGDVSG
//