ID B6QUE4_TALMQ Unreviewed; 1181 AA.
AC B6QUE4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=PMAA_008830 {ECO:0000313|EMBL:EEA18595.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA18595.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995906; EEA18595.1; -; Genomic_DNA.
DR RefSeq; XP_002152980.1; XM_002152944.1.
DR AlphaFoldDB; B6QUE4; -.
DR STRING; 441960.B6QUE4; -.
DR VEuPathDB; FungiDB:PMAA_008830; -.
DR HOGENOM; CLU_004875_2_0_1; -.
DR OrthoDB; 1630at2759; -.
DR PhylomeDB; B6QUE4; -.
DR Proteomes; UP000001294; 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; 2.
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, ECO:0000313|EMBL:EEA18595.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1181
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845840"
FT DOMAIN 741..1042
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1045..1179
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 584..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1181 AA; 131643 MW; 32FB320ECE512228 CRC64;
MRWKLPTVLP ASAAILLLPS LLLTAPQQLS HAQQHDAVVS SSIYAAPRPT GQSIVDESPH
TYFRDTHTHM PPDVKKINPD DVSALATLAL AGSDSRAVRA PPAQLSSPTA LLASQLQARS
LQDWEVEDFV LLATVDGTIH ARDRKTGSPR WALEVPSSPM VESIYHNRST TGFDTGSSIR
DDDFLWIVEP SKDGSLYIFS PGRQGGLQKL GLTVKDLVNE TPYSGTDPAV TYTARKETTL
YTVDARTGNV LRVFSSRGPL SADHNCKIDR LATDDMLDDD NSDEDGGHCG GTSGTLTIGR
IEYAVAIQNT ETGEPICTLK YSEWAPNNRD VDLQSQYYQT MDQSHIYSMH DGVVLGFDHS
RMERPRYTQR FSSPVVRVFD VARPVNVKSP DSPLPLVLLS QPLEPPDPDY AASPDTEHRV
FIDCTEAGGW YAMSERTYPL VTGRAGMAQC YNKDFFRDGH SLLTLDLERQ RKALVGVHSV
NMPTSHGGRR SRMHSISGPS AIGGGPNGTP RDVVSSPAYL AASPALRQSV IIRTGWENRT
DIFVLAILAL FGYFLWVNSA LFQEHLKQKL DLKNILAAYD QHISEPPTSP TVSSFQRGTS
PIGIRSEFTT PRKASVQLED LQVDNESTPR NERASSLSGD PETTPRVRIR EPSRGPDDEG
DELNLQEPKK KKRQRGQRGG KAHKRKAKPG SDEEKALSQT VDQVKSLVPP SGLEADVQLS
RQVSNEVYEM DGAIRIGQLK VYTDTVLGHG SHGTIVYKGS FDGRDVAVKR MLVEFFDIAS
HEVGLLQESD DHSNVIRYYC REQAVGFLYI ALELCPASLQ EVVEKPQDYP QLVKGGLDVP
DILRQITLGV RYLHSLKIVH RDLKPQNILV AAPRGRSMSS QYPALRLLIS DFGLCKKLED
NQSSFRATTA HAAGTSGWRA PELLVDEDQQ SAIAINSGHS NHTESSEPAV VDPQTNRRAT
RAIDIFSLGC VFYYVLTRGG HPYDKDGKFM REANIVKGNY NLEELERLGD YAFEADDLIR
SMLSLNPRSR PDATTVLMHP FFWNAADRLN FLCDVSDHFE FEPRDPPSLA LQYLESVARN
VMGPDMDFLK LLPKEFKDSL GKQRKYTGSR MLDLLRALRN KRNHYNDMSE HLKAHIGGLP
EGYLRFWAVR FPSLLMNCHR VVVELDLCRL ERFKRYFTPP E
//
