ID A0A091DNA2_FUKDA Unreviewed; 929 AA.
AC A0A091DNA2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=H920_14391 {ECO:0000313|EMBL:KFO24261.1};
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:KFO24261.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO24261.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO24261.1};
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.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KN123629; KFO24261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DNA2; -.
DR STRING; 885580.ENSFDAP00000022440; -.
DR eggNOG; KOG0589; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08221; STKc_Nek9; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042767; Nek9_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44535; PROTEIN CBG16200; 1.
DR PANTHER; PTHR44535:SF1; SERINE_THREONINE-PROTEIN KINASE NEK9; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 3.
DR Pfam; PF13540; RCC1_2; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO24261.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW 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:ARBA00022777, ECO:0000313|EMBL:KFO24261.1}.
FT DOMAIN 14..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 337..393
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 394..447
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 448..499
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 500..564
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 565..617
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 618..675
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REGION 13..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 101437 MW; 825D2B3FE3CC8139 CRC64;
MSVLGEYERH CDSINSDFGS ESGGGGESGP GPNTSAGPRD DSLVVWKEVD LTRLSEKERR
DALNEIVILA LLQHDNIIAY YNHFMDNTTL LIELEYCNGG NLYDKILRQK DKLFEEEMVV
WYLFQIVSAV SCIHKAGILH RDIKTLNIFL TKANLIKLGD YGLAKKLNSE YSMAETLVGT
PYYMSPELCQ GVKYNFKSDI WAVGCVIFEL LTLKRTFDAT NPLNLCVKIV QGIRAMEVDS
SQYSLELIQM VHECLDQNPE QRPTADELLD RPLLRKRRRS STVTEAPIAV VTSRTSEVYV
WGGGKSTPQK LDVIKSGCSA RQVCAGITHF AVVTVEKELY TWVNMQGGTK LHGQLGHGDK
ASYRQPKHVE KLQGKAIRQV SCGEDFTVCV TDEGQLYAFG SDYYGCIGID KIAGSEVLEP
MQLNFFLSNP VEQVSCGDNH VVVLTRNKEV YSWGCGEHGR LGLDSEEDYY TPQRVDVPKA
LIIVAVQCGS DGTFLLTQSG KVLACGLNEF NKLGLNQCMS GIINHEAYHE VPYTTSFTLA
KQLSFYKIRI IAPGKTHTAA IDERGRLLTF GCNKCGQLGV GNYKKRLGIN LLGGPLGGKQ
VIRVSCGDEF TIAATDDNHI FAWGNGGNGR LAMTPTERPH GSDICTSWPR PIFGSLHHVP
DLSCRGWHTI LIVEKVLNSK TIRSNSSGLS IGTVVQSSSP GGGCGGGGEE EDSQQESETP
DPSGGFRGTM EADRGMEGFI SPTEPMGNSC GASSSCPGWL RKELENAEFI PMPDSSSPLS
GAFSESEKDT LPYEELQGLK VASEVPVEPK PPAGGAWPPL LTPAVPGAGK GAPLTPPACA
CSTLQVEVER LQGLVLKCLA EQQKLQQENL QIFTQLQKLN KKLEGGQQVG MHSKGTQTAK
EEMEMDPKPD LDSDSSWCLL GTESCRSSL
//
