ID I3KDE7_ORENI Unreviewed; 992 AA.
AC I3KDE7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Alpha-kinase 3a {ECO:0008006|Google:ProtNLM};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000019142.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000019142.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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DR AlphaFoldDB; I3KDE7; -.
DR Ensembl; ENSONIT00000019159.2; ENSONIP00000019142.2; ENSONIG00000015209.2.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000158534; -.
DR HOGENOM; CLU_003270_1_0_1; -.
DR TreeFam; TF332629; -.
DR Proteomes; UP000005207; Linkage group LG7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd16973; Alpha_kinase_ALPK3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 59..150
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 572..660
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 686..913
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 111177 MW; F3DD661C943F7A81 CRC64;
MTSRRPMTRS FSSNGRTSSF SEDEAPSFNG RNTYLSNVRP ENRSTLCSVM AQLTEDIQPS
FETTLKSKAV SENCNVKFTC VVTGYPAPEL KWYKDDMEMD RYCGLPKYEI RRNGKTHTLH
IYNCTVDDAA IYQVSASNSK GIVSCSGVLE VGTMNEYKIH QRFFAKLKQK AEKKRKDAEE
QTKKENKENV QKAKPLISPE HPQRKRAVPP PEEREVVKEC EAMEELGATA EPNGISSENE
ETASLASRDR GLEDETGPSD ETLATKRIKM SNGELQKKRE EQEKAQKEEY EKEKRREEEQ
AIRREKERER QPQVSHTAAH GKHGPDVKHH SKGHKDHDHH HIQTSISSML HSVKDFFFGK
SKKSTHGHTD NEEADFEHSV EAPEPEMPPS FQPQEHSPDV SKPLTEEPPT SPASLRKLIS
KAAADSDNEA AAAEDLSGGS TPTSSLSCES SPRMKRRDSL TLIRSATPEE LASGARRKIF
IPKPKEDIDG TLALDTQGKR ESPYMSPSQA RRASLLQAQK TPPIERRSPL LNRRKSTLEV
PKVVGETPTE ETASTKREEK PAEKKIDPLK APQVIRKMRG EPFPDASGHL KLWCQFFNVL
GDSTIKWYRD EEEILEVKRS GGDESQVALA IVLASKQDCG VYGCTITNEY GTDSTDFLLS
IDSKKHNSVF ASVGEEIEMT PLLFSKGLVD SGTWGDKYFG RIMTERLHLG EGCAHKASQV
KVIYGLDPVF ESGSTCIIKV RSPIPYGTKQ ESNLAERNLE ITKHECKVQN MIREYCKIFS
AEARVIENFG VIPRYLMYRP ANSVPYATVE AELTGLFLKY CTMDAKGKLV MQKISEIEQK
CCSFQHWIHQ WTHGNLLVTQ LEGVETKITN VRVVTKSKGY QGLTECGSPE VFNQFLTVHQ
CNYYCGLLGL RPLKAMDSLQ QPAKAKGSKS PLLNRKAGST SPQPQRKGHS PQIARKANSS
PKVTRKGQET EDNKSSAKPK PAEITDATVE TR
//
