ID A0A2V1AVZ3_9ASCO Unreviewed; 1258 AA.
AC A0A2V1AVZ3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-NOV-2023, entry version 20.
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=CXQ85_004629 {ECO:0000313|EMBL:PVH21964.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH21964.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH21964.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH21964.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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};
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC {ECO:0000256|ARBA:ARBA00009124}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010006}.
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:PVH21964.1}.
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DR EMBL; PKFO01000006; PVH21964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AVZ3; -.
DR STRING; 45357.A0A2V1AVZ3; -.
DR EnsemblFungi; CXQ85_004629-t46_1; CXQ85_004629-t46_1-p1; CXQ85_004629.
DR VEuPathDB; FungiDB:CXQ85_004629; -.
DR OrthoDB; 208777at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06090; KOW_RPL27; 1.
DR CDD; cd05581; STKc_PDK1; 1.
DR Gene3D; 2.30.30.770; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001141; Ribosomal_eL27.
DR InterPro; IPR041991; Ribosomal_eL27_KOW.
DR InterPro; IPR038655; Ribosomal_eL27_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
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:UP000244309};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 219..485
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1258 AA; 138664 MW; BB41EB5839AA201F CRC64;
MSNRYTSSTQ NSGSGTGSGA GLSGTQSPDF GEIYSSYAQH SNPQQDQSSA SHNQSQDSLD
SNSNHVGDNT PPVRKTSYKI NPTRAQAVFQ ALNESSAQAS PRTPAREGSP GSSDSFDFTQ
PNQSALHSSS LNVLLDTPSS ESQYRQLVST PPVIETNYRH HGRHTESQEN VDDESSNVDV
SLRSESVDNW AEKGGAERTV SSTSSGYDYK VIGRTVKDFE FGKDIGEGSY STVVLATDKL
TDKKYAVKIL DKRHIIKEKK VKYVNIEKHA LNRLSGCPGV ISLFFTFQDK HSLYFVLDFA
ANGELLGLIK QYGTLNEECT RYFGAQMLDA IRYMHDNGVI HRDIKPENVL LDENYRIQIT
DFGTAKLLER KKNGETGEDE DYPLDVRAKS FVGTAEYVSP ELLENKYCGK PGDIWALGCI
LYQLIAGKPP FKATNEYLTF QKITKLQYAF SAGFPLVLRD LIKQVLVLQP SRRATINQIQ
KHHFFHEIDF NDTDSIWNTP VPELGPYKMT AKSMMKMPPA PKVSPKKIIR KPGKKKAAGQ
TAQAQEKPGQ KRVTSDSSSG GKKNYSAASV AAYVFHKQDE DDSQPNVSNP SASASARKPS
APEYIPGTNI LRPVINSRAN FSRSSVSHAS SSFSASSSQL ERKNSKQPEV PPISSVELAW
KDHLNSPEER ILHVGQAIVC KQPTEYFERK HKGLIHNAPL KYVNQLQAVA KVGGSDSMLS
RVAQGNKGGL RSAPESSPYA ANEKDAVIEF NLEEEVDPKI TSIPEDEDPP TSPVESKEKE
DQSNGTGKSA SKIGRKFLKK FLNHTEKNDD GSDASSSKSG GSGGNGRSRS SSFSLDRAKN
CTLVLTTHGR FLIFIKEGSN EPKLVTEVLL NYPFISFKEV VTNHSAKFGK IIPVTGIFAV
QAIESTFVFE VDKYEVDIWT VALARSKLGQ FDREREQSQV SSNPSPKLMD APSFKTPPLN
SEKSFELDSP SQPPAPAAAP PPPPKSNRKV SETGSQESPK TVQSPTSDQE PSSPKQTLDP
KGRSMFKSRT KQSRSMKRKP PPPLPKGNIN NTGFAKDPVS PDNDTLHAAL LAVNNNPSAK
SEESRRSSFS KTTPTSPTQN ITYRYQSPSN GKGRITAMNS KLLTRTRNNK HSAIVTRGRF
AGKKVVVVRP QDDGTKGHSF PHALVVGIER GPQRITKAHD AKKIAQRTKV KPFVKVINYN
HLMPTRYSLD VESFKNAVTS DALNEPSQRV EAKKVVRKAL EEKHQAGKNK WFFQKLNF
//
