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Database: UniProt
Entry: A0A3Q2ZP27_KRYMA
LinkDB: A0A3Q2ZP27_KRYMA
Original site: A0A3Q2ZP27_KRYMA 
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
//
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