ID A0A091DRK9_FUKDA Unreviewed; 593 AA.
AC A0A091DRK9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=RAC-gamma serine/threonine-protein kinase {ECO:0000313|EMBL:KFO25451.1};
GN ORFNames=H920_13212 {ECO:0000313|EMBL:KFO25451.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25451.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25451.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25451.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN123358; KFO25451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DRK9; -.
DR STRING; 885580.ENSFDAP00000011080; -.
DR eggNOG; KOG0690; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF199; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO25451.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 170..427
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 523..593
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 564..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 593 AA; 67621 MW; 43595CAC7EFC1FFA CRC64;
MPSFLSANSE KPPPILPPRQ TENVTDWNPA GGQSLFQCIP VQDQSQEQHI GVLTTLKHCH
QVDIVLDFLL EEKLSSVAAE CQLMKTERPK PNTFIIRCLQ WTTVIERTFH VDTPEEREEW
TEAIQAVADR LQRQEEERMN CSPTSQIDNI GEEEMDASTT HHKRKTMNDF DYLKLLGKGT
FGKVILVREK ASGKYYAMKI LKKEVIIAKD EVAHTLTESR VLKNTRHPFL TSLKYSFQTK
DRLCFVMEYV NGGELFFHLS RERVFSEDRT RFYGAEIVSA LDYLHSGKIV YRDLKLENLM
LDKDGHIKIT DFGLCKEGIT DAATMKTFCG TPEYLAPEVL EDNDYGRAVD WWGLGVVMYE
MMCGRLPFYN QDHEKLFELI LMEDIKFPRT LSSDAKSLLS GLLIKDPNKR LGGGPDDAKE
IMRHSFFSGV NWQDVYDKKI QQEDGGSHQR PPAPSTELGG LRDMYRDSHA CTGQRIYSSF
AHVLAIANLR QQSVSAALLM LGGADERAAG GKERRVFREE SGSSIRTAIL ALVPPFKPQV
TSETDTRYFD EEFTAQTITI TPPEKYDEDG MDCMDNERRP HFPQFSYSAS GRE
//
