ID A0A2V1AWW5_9ASCO Unreviewed; 1157 AA.
AC A0A2V1AWW5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_005296 {ECO:0000313|EMBL:PVH22269.1};
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:PVH22269.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH22269.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH22269.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:PVH22269.1}.
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DR EMBL; PKFO01000007; PVH22269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AWW5; -.
DR STRING; 45357.A0A2V1AWW5; -.
DR EnsemblFungi; CXQ85_005296-t46_1; CXQ85_005296-t46_1-p1; CXQ85_005296.
DR VEuPathDB; FungiDB:CXQ85_005296; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09769; Luminal_IRE1; 1.
DR CDD; cd10422; RNase_Ire1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 2.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000244309};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1157
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015961540"
FT DOMAIN 714..1021
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1024..1156
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 565..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 130681 MW; 00751FF50F1E587B CRC64;
MKLNPFFLLA FLFAYFTAVL PAVFGEAVSQ EAAGDDNGRP LLSEVKNKNI LPLDLRSLQD
WKLTDLLLVS DIDGNLHAVE RHTGAFLWTL PLDEPLVRVS RNKFPRKDPE NNTNLLWLVE
PYQDGSLYYF TPQYGLNKLP TSIKNLVMEA PFSLSGDNKI YTGVRKTSLY TINMKTGEVL
NQFGSADESC PAPNLYKSPN FRPDSDENTI MLGKTTYELS VHYKYDSSVV WNITYSSWGP
NNIDNDLIMQ NGQSIDDLYF TPFHDKSLLA INKGSGTPQW ICRLPSLAVN VFDVFNNEEN
LNQYVTLPHP LKVLNDLQQL DDAQKEAANN DLCFVNRTAN GKEWFAMSFR NYPTLLKSAP
IAQYQMALYQ FATGTLDRQT QDFLSRLNVS REDVEPFING VHKINLLSPD SMYQPHSQFR
KEEYLGIGDG SDGSTGVEKE SKQVPHMIDG ILFPQTNDDP GQGLATIDER RKELMANDRN
YPTGLPASRS DADVAIPQSD PRHTLSFFRR IAEDVVVLCI LLLVLFSAGK LNGFIQFNKG
KDIALAEKVN DLEINLQDPK ALKVVEEPEE KPLPQIPVES TDATQETQDL KKEPTTEESP
KKKVKIITDE DTHEVVPGEA ANDGSAIADG ESNTITKKKR KRGSRGGKRG GKGKKNAESK
DEEDPKDEAS ENTQVASDES SVEDAEPIPT KSLVKQFSKR NNTNKKLQID NNLIISDKIL
GYGSHGTVVY EGTFENRPVA VKRMLLDFYD IANHEVRLLQ ESDDHPNVVR YFCSQSSESE
KFLYIALELC VCSLEDLVEK PKLDKAALKL DHHLKNEVLL QLVSGLHYLH SLKIVHRDIK
PQNILVGDST RKKHSKTVAA FRLLISDFGL CKKLDADQSS FRATTQHAAS GTSGWRAPEL
LLHHDLMEIS PDTVSSLNST SKHSIKDGNG PANGSGKRLT KAIDIFSLGC VFYYILTGGG
HPFGDRYLRE GNIVRGEYDL SALKQHCPHD WVEATHLIAS MISFNPKTRP DTSLIMRHPY
FWTYNKKLEF LLKVSDRFEI ERRDPPSPLL LSLEEAGQTV HQGDWLARFD QEFIDNLGKY
RKYNTDKLMD LLRALRNKYH HFNDMPPELQ VQMSPLPTGF YSYFNNKFPK LLMETYRVVA
DEGIKDEHIF ESFYSAT
//