ID A0A3B4W9E9_SERLL Unreviewed; 1821 AA.
AC A0A3B4W9E9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alpha-protein kinase 3-like {ECO:0000313|Ensembl:ENSSLDP00000000549.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000000549.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000000549.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 1841481.ENSSLDP00000000549; -.
DR Ensembl; ENSSLDT00000000596.1; ENSSLDP00000000549.1; ENSSLDG00000000513.1.
DR GeneTree; ENSGT00940000158534; -.
DR Proteomes; UP000261360; Unplaced.
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 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 69..160
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1396..1484
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1512..1743
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1755..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1821 AA; 202057 MW; D863503D097F6E19 CRC64;
MTSRRPMTRS FSGNGRTSSF SEEEGSSSNG RNTYLSNVRP ENSSRYSHYR PTRSTLCSVM
AQLTEDIQPS FETTLKSKAV SENCNVKFTC VVSGYPAPEL KWYKDDMEMD RYCGLPKYEI
GRNGKTHTLH IYNCTLDDAA IYQASASNSK GIVSCSGVLE VGTMNEYKIH QRFFAKLKQK
AEKKKKDLEE QTKKEDKTNI QREKPQKSPE RPPRKRPILP PKEKPVFKEL EVGEQVGAAA
EPNGVSSEVM ETETISSTNS SPEKEVPPSG ETLAKKKIKI SNGVDVGVSN SNSSSSSSGR
SHMMGNGGEN CYDGGISLAQ FLAETLQSQS AEEKQNSSRV EKPKEMNVPV VNDSKETEGM
QKEREEQEKA TEEEYEREKR SDEDLVIEKE RLSEMWHTSD HSKHDSEVKH HSRAHKDHDH
HNIQASFSSM LHTVKDFFFG KSKKGFHDHI EDREREFDHD SIQPPQPETP PSFRLQQECN
PDVYKPLTED VVPMETDKPN ESSGSVYMQQ PSVSLETHEH KHEDSVLHTD LTPADKLPPK
STEESTRQSV KEADDAAEAM EVSVGTGSSS PGEEIPLSGL QVLTETEDKD SQVVSVISKV
PVNQQEPDCL VVSPRPDHQA ARDASLPRED ISVLPLTKTP SEEGEEQLSI DKMGQEGKPD
TVEGLSFNKL CEEEKAEVKS SKQPCSDINR SENTELTTPS LEERIEPCES KTPDQVLSPL
PAVVADTAEK DYVKEEAKCT SLVQEMNVGF PPSAAPDSLE NVDLKIQPEC PPSTAEESAD
VHTLNAIPSS SSGFTSGEEK SDLKDLVNSV LEEGVEVKLC NDLNTQEQAT LEGENTETSN
ECLQFDVETE KRVEESDESK IVSVTQNEGS SANVLEEHNE IAQPDGGETQ LGWPSENIPQ
IQISAIEDTP GIKPTVPDVN QNEHFVIPKI EIMEPELKEC TQPLTVVALK EPESEPALLQ
KHDATHVSEI IVQDQSMTDS PHSLPTEKGM QNDYNLSLAQ KVKEVAQLDD ETEMLEQEQP
RVKSSEQLPQ MDYASIPLIN VSCTDDKEND AFVNAHVSHT LQPFETPTVP LFVVPPISVT
CHESDPGVRL PTHSEWTETE TSATTQRGTK HNVDITMTAK PEKAESRKQN LEEVSDKSVK
ENTPSLVSEA PLPKVGDNVV SINKTAEDNI VPEKKNKTKP LKEAKIENSV SVEDPQKNRC
TVERLSCKPP AHPSLSPASL RKFMPKAAPD SDSEAVTAVP VITVGDRQSD KADEDLSGGS
TPTSSLSCES SPRLKRRDSL SLIRSATPEE LASGARRKIF IPKAKDDGEG AVLGVLDTQG
KKETPYMSPG QARRTALLQA STGQNTPPME RRSPLLSRRK ATLEVPKVVE ETPKEEPVTK
REEKPAEKKL DPLKAPQVIR KIRGEPFPDA SGHLKLWCQF FNVLSDSTIK WYRDEEEILE
VKRSGGDESQ VALAIVLASS QDCGVYGCTI KNEYGSDTTD FLLSVDILSE ILLRDDLEVG
EEIEMTPMLF NKGLADCGNW GEKFFGRIMT ETVNIGEGCA HKASKVKVIY GLDPVFDSGS
NCIIKVQNPI AYGTKQESNL TERNLEISKQ ECKVQNMIRE YCKIFAAEAR VIENFGHSLE
VIPQYLMYRP ANSVPYATVE ADLAGVFLKY CMMDPKGRLI TRTISEVEQK CSAFQHWIHQ
WTHGNLLVTR LEGVEAKLTN VRAVTKSKGY QGLTEYGSPE VFEQFLTQHQ CNYYCGLLGL
RPLKSMDSLL QPTKIKGSRS PLLNRKLGSN SPQLQRKGQS PQLSRKANSS PRVTRKVQEP
ENNKSDTKPK PAETVNALEM P
//
