ID B8MV31_TALSN Unreviewed; 312 AA.
AC B8MV31;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Serine/threonine-protein kinase HT1, putative {ECO:0000313|EMBL:EED11918.1};
GN ORFNames=TSTA_110970 {ECO:0000313|EMBL:EED11918.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED11918.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
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 ---------------------------------------------------------------------------
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; EQ962661; EED11918.1; -; Genomic_DNA.
DR RefSeq; XP_002488674.1; XM_002488629.1.
DR AlphaFoldDB; B8MV31; -.
DR STRING; 441959.B8MV31; -.
DR GeneID; 8110126; -.
DR VEuPathDB; FungiDB:TSTA_110970; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_000288_31_7_1; -.
DR InParanoid; B8MV31; -.
DR OMA; VMYEVIT; -.
DR OrthoDB; 2221719at2759; -.
DR PhylomeDB; B8MV31; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR43671:SF112; NIMA-LIKE KINASE; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EED11918.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EED11918.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..312
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012022664"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 312 AA; 34785 MW; FE649026D452BF07 CRC64;
MLQLFIIIDL KMAASLFMDL DGMPILDSDV IGYGGSGVVV RRGNLAIKMP LRYPGSSEED
VQSNIKVLQH EQEVYRRFNS FTEDLIDRIV PCSRLCTNAI ELGFMENGDL RSYLQKHQPS
RTVQIAWFRQ MARALEQIHG KYVLLCDIAS RNILLDSDLS IKICDFSEAS ILPLGTTMET
VNDQGFSVQT DIGLLGAVIY EVIAGQQCKF NLFDGPAASQ ATFPHRTSLP STASLWLGHI
IEKCWTVGGF QNAHALSQAL ESADLEQENH STNKKCTTLL EYFRGETETS IIVLAITFSA
LIAVTTWVRR QT
//
