ID A0A367XPV1_9ASCO Unreviewed; 1212 AA.
AC A0A367XPV1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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 Name=IRE1_0 {ECO:0000313|EMBL:RCK55654.1};
GN ORFNames=Cantr_05585 {ECO:0000313|EMBL:RCK55654.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK55654.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK55654.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK55654.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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:RCK55654.1}.
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DR EMBL; QLNQ01000029; RCK55654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XPV1; -.
DR STRING; 5486.A0A367XPV1; -.
DR Proteomes; UP000253472; 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; 3.
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, ECO:0000313|EMBL:RCK55654.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1212
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016704965"
FT DOMAIN 767..1079
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1082..1212
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 35..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 138760 MW; 4468EDB73C4E1B5E CRC64;
MHFIHFIPYI ISILILSVVA SPRLEKITTK YLSSDLGPHN HNTGQQHEQQ QSDDHHNQQQ
HQQQPYQYNY HQNERNNVNK QNHQPTPTNQ AYSSSLLPLH DRSLDDWDLN NLILLSDTNG
SLHGVNRENG NLIWTLPIEE PLVKIQTNIG TESTASATST SSTSSDSAAQ GNILWFVEPH
LDGTLYYFTP KYGLNKLPTS IKDLVMESPF TLSGDDKIYT GTRKTSLYSI NIHTGEIKSS
FGNTEECPIP KSTLPPGKQT SRNDDDNIMI GKTTYQLTIH SKTNSNIMWN VTYSQWVPNN
IDNDLILQNQ QSLDKVYFTP FHDRSLLAIN QDIGTPIWIS KLPALPVDIF DVFRNNENSN
EYLVLPHPLK VLNDLQMNDI NNQDMVFVNK TIDSNQWIAM SFRNYPTLIK SAPISKYQEY
LNKYYAGINK EAIDYILNFQ IVNNSEENIE NFVSGIHRVF ELQSVNSYQP FERFHSPLED
IKRIGDGKSN DEAIPETTDK VPNIMDGFRF PSRPSTLRSE VLLLEPARDD EIDAQHRTQK
VYEPIGSGVD TGSSVSSLAI IRRIFEDLAV LLVLFVLLLT FGRSNKFVKK FIGELPLEKQ
VADDEEQQQV QPSQSVIIEK PQELIEPNKV VEEVVEKTEE VSSTSEEKEP EQAEIKENVE
QADEVVTPEA TKKPKKVTIV EPEEDKESND DVSEEPTGKR KKRRGGRGGK RAAAYRKNKL
KVEEEEQQDD DNDDVDEEII TTKSLLPPAT IPVVKSKKKL QIQNNLIISD KILGYGSHGT
VVFEGTFENR PVAVKRMLLD FYDVANHEVR LLQESDDHPN VVRYFCSQSS ESEKFLYIAL
ELCLCTLEDI IEKPQKLPSL CVPKKNDILF QLASGLHYLH SLKIVHRDIK PQNILVATIK
KSKHDKTIIE DGCENNIRLL ISDFGLCKKL ENDQSSFRAT TQNAALGTSG WRAPELLLNH
DLLELISPDS ISSVHSNNQA PSSTSLMSTG TSTGKRLTKA IDIFSLGCVF YYILTGGYHP
FGDRYLREGN IIKGEFDVSI LMEKCPNDKY ESTDLITKLI AHDPSVRPNT AKILKHPLFW
DFGKRLEFLL KVSDRFEVER RDPPSELLLK LEEHALNVHK GNWHKQLNDD EFMENLGKYR
KYSPEKLMDL LRAIRNKYHH YNDMPESLQM KMNPLPFGFY KYFNDKFPKL LMEIYYVVEE
HLKDEHVFKE YY
//
