ID A0A3Q2ZP27_KRYMA Unreviewed; 1003 AA.
AC A0A3Q2ZP27;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alpha kinase 1 {ECO:0000313|Ensembl:ENSKMAP00000005543.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000005543.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000005543.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q2ZP27; -.
DR Ensembl; ENSKMAT00000005641.1; ENSKMAP00000005543.1; ENSKMAG00000004167.1.
DR GeneTree; ENSGT00940000159753; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16969; Alpha_kinase_ALPK1; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR043529; ALPK1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR46747; ALPHA-PROTEIN KINASE 1; 1.
DR PANTHER; PTHR46747:SF1; ALPHA-PROTEIN KINASE 1; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 775..994
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 503..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 110475 MW; 681131C3D4677214 CRC64;
MVQFFLNSDV ALFRDFHSCG ANSKEGGSPS DPGSMEECLR AAAAAAAAVA APHQAPQLTE
EVRLNYCSCR DSLCAELASL LQEAVEMKWP FVPEKWQYKK SVSPDDKTNL SDLISKHLHQ
LLVLLEASIV AQEAPTALAV VFLVDRFIYW TDESSRLLKI AKLLHRRHPD TPIAPQLVIR
QARVYFNSGK LQKAEYILSS LINNSGTTGS RWSYQSDGDR ALVQAVSVQV RGMILQKLGL
WLQAAELIWA SLVGFYSLPQ PDKKGIGTSL SHMDSDRLLS AAHAAKMSVT YSQYTPLYVL
TNVTTQGTCL LSYSFSLECP PPQRASFLQQ AREAFAVGLL TKADSDLVTS QQELHTFLKA
AYSITVAHKW LGAPQGVVTK AAQACQKALA NFYDYSRAAT QDKEELCAEI MRLVGQVKVL
LGVDPFPNSD KGSFIPDSYR NVKDSSVNFT LEAFSKIMQR FQKYHASLCE NTTRRCRGAE
DEADGARLCL TALGTTADTL GTECRADVDQ PQRKGSVPSS GHPPSDSDTC PTVESSDQLG
SSWQRLSPSS SGSPRPPGHG ANMSNQRCIT TESDDGRSAD ENQKERPHGR DSSISSHAGP
KSAASSSFSS KDPGDLEKFE VMQAELETVD TERDWMAIGV AQKQEAGAGG DLRSLSQLTL
KTSSSSLGDS FSSQSSWEKI PSGKNSPACG KPQPSHLSKP ETGQRSMSSD SNESFFILET
EDSEPSLLDL DATKKNQWKV GAPSEPRPLE NSDNKTFLKP ANSCPLSPPD ALHLKFSKAT
GLWTAKETCV YIGESMGMKG NQREAIWVQF LHQEERLSSY VGKDYLQPRG VQFHLKDVER
QMTAQYYVTE FNKRLYDKEV MAQIFFIPSE ALLVLNGDEI VGCLTVEPYM LGDFVKLTNN
TRKKNKMFRA TEYGLAFGHF TYLFSGGQEV VVDLQGWVTA SGKGLTYLTD PQIHSTRTPK
GPGNFADRGL RLFLEEQHGP ECNEICQLLK LHPVRTEIKK KKC
//