ID K9J225_DESRO Unreviewed; 593 AA.
AC K9J225;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA48384.1};
RN [1] {ECO:0000313|EMBL:JAA48384.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA48384.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GABZ01005141; JAA48384.1; -; mRNA.
DR AlphaFoldDB; K9J225; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF17; SERINE_THREONINE-PROTEIN KINASE PAK 4; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:JAA48384.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transferase {ECO:0000313|EMBL:JAA48384.1}.
FT DOMAIN 11..24
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 323..574
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 95..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 593 AA; 64532 MW; 5E4DF11C7DC292F1 CRC64;
MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT
SIQHEAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPPT RARQENGMPS
EQAATARGGP EKAGGQGWVA GLSEGGGSSG DRRRVGPEKK PKTSREGSGG PQESSRDKRP
LSGPDVSTPQ PAGVASGAKV AAGRPFNTYP RADTDHLSRG TQGEPHNMAP NGPSVGGLAV
PQSSSSRPPT RARGTPSPGV LGPHASEPQL APPARTLAAP AGPPAPGPPG PRSPQREPQR
VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGVVCIA TVRSSGRLVA VKKMDLRKQQ
RRELLFNEVV IMRDYQHENV VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA
SVCLAVLQAL SVLHAQGVIH RDIKSDSILL THDGRVKLSD FGFCAQVSKE VPRRKSLVGT
PYWMAPELIS RLPYGPEVDI WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL
HKVSPSLKGF LDRLLVRDPA QRATAAELLK HPFLAKAGPP SSIVPLMRQN RTR
//
