ID A3LWV1_PICST Unreviewed; 1176 AA.
AC A3LWV1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 98.
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=PICST_47968 {ECO:0000313|EMBL:ABN67343.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN67343.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN67343.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CP000500; ABN67343.2; -; Genomic_DNA.
DR RefSeq; XP_001385372.2; XM_001385335.1.
DR AlphaFoldDB; A3LWV1; -.
DR STRING; 322104.A3LWV1; -.
DR GeneID; 4840136; -.
DR KEGG; pic:PICST_47968; -.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_2_1_1; -.
DR InParanoid; A3LWV1; -.
DR OMA; QCYEKDY; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
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..1176
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002655121"
FT DOMAIN 726..1044
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1047..1176
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 424..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 133668 MW; C13F24FD5E9E3354 CRC64;
MRKLLFLLSL CMMAYVVLVA ASPRLEKVTT RYLPDSLLQN DAAPQTTEPP SKRTTDSSIL
PLDVRSLKDF KLTDLLLISD VDGNLHAVER KEGALIWTLP SDEPLVKIQS NSSTEDSQSN
ILWFVEPYQD GSLYYFTPKF GLNKLPTSIR QLVMESPFSL SGDDKIYTGS RKTALYTVNI
FTGEIVSSFG NEEKCPVANT HYKIDNLYSR SDTINIGRTT YELTIHSKLN TNVVWNVSYS
QWGPNNIDND LIMQNSESID KLYFTPFYNK SILAINKDIS APKWLTNLPS FAVSVFDVFS
NLKNSDCVLL PHPSKIFNQP QLDDDNDNNS DLVFIDRTSN RKEWFAMSFN NYPSLIKTAP
ISNYQLYLLK LQADFQDLNV NVDYLKNFQL STSPPEEVKT LISGIHRAFQ LSADTLYQPS
SRFEKSDDIK RIGQNEQTER TEQDERTEQD DQNDNSLKTD LEEIKPNIAE GVNFAHETSR
SEVLYLPPSN NEVESYRPYK DPETSHEIIN NLEPNSTTAI IRRILEDLVV LLVLFVLVMT
FGKSNKFVQG FFNNGSLVGP VSIEKDAVFD NDVVLDSNFS VSNDKEKVSI TEKDKSSQVV
ELANQDNKDA KDSNEVFKKV KIVVPNESLE KANDDPSKLE ENVDDDEEGN GDEITTKKKR
KRGSRGGKRG GRRVNKSKEN AGDDQEINDE SPEEEFISIA TKSLVKTITT PVKIPSKKLQ
IENNLVISDK ILGYGSHGTI VYQGTFENRP VAVKRMLLDF YDVANHEVRL LQESDDHPNV
IRYFCSQSSE SEKFLYIALE LCLCSLEDII EKPKKSPQLS IPKVNDVLYQ LASGLHYLHS
LKIVHRDLKP QNILVADIKK TSSSKATTKP SEEENNVRLL ISDFGLCKKL DSDQSSFRAT
TQHAASGTSG WRAPELLLHH DLLEISPDTI SSVGSGSRHS FTESWSTVTN SSSVQASGGK
RLTKAIDIFS LGCVYYYILS GGMHPFGDRY LREGNIIKGE YDISLLKQCC PNDKYEATDL
IASMIHANPS KRRSTSKILI HPLFWSSKKR LEFLLKVSDR FEVERRDPPS DLLLKLEDRA
NAVHGGNWHK QFDDEFMDNL GKYRKYHKEK LMDLLRAIRN KYHHFNDMPE TLQAQMSPLP
GGFYKYFNNK FPNLLMQIYF LIEENLAEEH AFKDFY
//
