ID A0A0A2LEY9_PENIT Unreviewed; 1138 AA.
AC A0A0A2LEY9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PITC_010310 {ECO:0000313|EMBL:KGO77761.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77761.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77761.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77761.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77761.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQGA01000104; KGO77761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LEY9; -.
DR STRING; 40296.A0A0A2LEY9; -.
DR HOGENOM; CLU_004875_2_0_1; -.
DR OMA; QCYEKDY; -.
DR OrthoDB; 1630at2759; -.
DR PhylomeDB; A0A0A2LEY9; -.
DR Proteomes; UP000030104; 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 CDD; cd13982; STKc_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:UP000030104};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1138
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001990958"
FT DOMAIN 706..999
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1002..1136
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 547..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..649
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 126670 MW; 51A72247EEEED0C1 CRC64;
MRWRLPGVRS TLPASVTLLL LPALVAPLQQ ADTHNHISRV SVPLAQESSK QHASHLVAPP
IVKPNDASAL ATLALAGSGR AVRAPPVQAS STAAGLASQL HARSLEDWEV EDFVLLATVD
GTIHARDRKT GAARWALEVP SSPVVESIYH RANRSSFDDT EPEDDFLWIV EPSQDGSLYI
YSPAPDAGLQ KLGLTVKQLV DETPYSGTEP AVTYTARKET TLYTIDARTG SILRVFSSRG
PITAAPECRK VNGEDLDSDE CESTSGTLVL GRVEYAVAIQ NTETGDPICT LKYSEWAPNN
RDMDLQSQYY RTMDESHIYS MHDGVVLGFD HSRMDRPRYT QRFSSPVARV FDVIRPANKD
APDASTPLVL LSQPLQPPDP DYGSLDDERD MRVFIDCTEA GGWYAFSEET YPLATGRAPM
AQCYDKDFFR RGQALMSLSA RQQRNALAGV HSLTGPRIIR PQIPRIAGSS TSELSNDTPR
DILRSPSELA LPPALRNSAI IRKSWDNALD IVVTLILLFI CTFIYFNSHH IRDLAKQKLD
IKNIINSSDK PSLSAPSTPV VGGAPEIKRS STPTQQVPSV TVSLDLDDAT PEGASTPRAS
QDYTSDSTPR VQIREPSRGP DDEDADEAGK PKKKPRARGS RGGKSHRRRK KPGSEGDSPE
GADQVVERAN SLAPQPRNEH DVQMVRTVSN EIMEMDGVVR IGRLQVFTNV VLGHGSHGTV
VYRGSFDGRD VAVKRMLMEF YDIASHEVGL LQESDDHHNV IRYFCREQAT GFLYIGLELC
PASLQDVIER PASYPELVQT GLDLPDVLRQ ITQGVRYLHS LKIVHRDLKP QNILVAMPRG
RTVSRSLRLL ISDFGLCKKL EDNQSSFRAT TAHAAGTSGW RAPELLVDDD GPMSLASQHT
ESSEPAVVDP QTNRRATRAI DIFSLGCVFY YVLTRGSHPF DKNGKFMREA NIVKGQFDLE
ELNRLGDYAF EADDLIRSML SLDPRQRPDA SAVLMHPFFW PPSDRLTFLC DVSDHFEFEP
RDPPSDSLLC LESVAERVMG PEMDFLRSLP RDFKDNLGKQ RKYTGARMLD LLRALRNKRN
HYNDMPDHLK ENIGGLPEGY LNFWTYRFPS LLMSCHAVVV ELGLTRNDRF RRYFVPPE
//
