ID A0A401SJA4_CHIPU Unreviewed; 1796 AA.
AC A0A401SJA4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha-type protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0008950 {ECO:0000313|EMBL:GCC30499.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC30499.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC30499.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC30499.1}.
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DR EMBL; BEZZ01000306; GCC30499.1; -; Genomic_DNA.
DR STRING; 137246.A0A401SJA4; -.
DR OMA; EMEYKTN; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091:SF2; ALPHA-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1382..1466
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1513..1745
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1796 AA; 200119 MW; F29A0E91A27E7FE5 CRC64;
MQEFEARNEA KQAPESDGPI SRECSRDCLS NPAQCASSSE RQGGFTRGRQ MDRLTETGLP
NTGRRLEQGE GARSVLPAGE RHRTASGGEP AMDEASPGGA EDEYYLEFLV CSDVLRDEDK
ARWEHRLCCP APLLLPGTPG EAGTAALPQG AGRPTAAPSR LPGSAPWQPS PPPPAMDTSP
GGLRQPESPL SPKHQQHPVR PPPSLRKNST SPAEQGAGGG PAGVQLGSED NTDHWTVRAE
MQPLLSKDGE ISFIKNATSS ASYKHDPSAC HGKKTDLLFL NKCDLVRSHE DNCDHKSECG
RLSPYCKTLS NAQIVDNTAS KSSAFKEMYH IQDNNQLQEK ILCFITKDDE LMRISKEYEG
SNNGYKAKTD CTRPLIDSSI GDYCIENKNS EHCENSSIYD KELGTLEQPS ELYTHNANLP
SSIVCNDSKS DMFKIEDTCG CIDPYLDIPP CLTVPVQIQD ISRLLNTSSN ISLVDGYGSE
NKFNSPSNVS TNNGNDGPAQ ATGQLQINKN YDSKSHEMDT TRYECPHLHS KVVCPKAMLQ
NLNLHKELAD EFEQTAFENR KSHESAVKSL SLPLNSTEGQ GQIQCSLNAS ENKLHEENRS
THQSMQLFET ADIEAHNNKA GSSFQETSRS VICQLEEQLP IEQPALFEDN LEIRSNKLVF
FNNKRDGTDW PLQEMEYKTN STATEPSVIT HQDANTFTLI DNEKLKNDEA SPFESLCWNS
SREITEGINN EYNSDVTNVE IEGLCKTEKN VNDEHLRNVF HDENMNQQFC NSTEIAMSPV
SNRSTEYEHF IFQSRIVQHS NSETVLDLED HLIALQSNNE PEVVKLDGLQ SSMSHMTEQY
LSPLIEQNQP RLIKIEANTA GNLMEYMEYP ISKEQKSSTV CIPISDQSSS LQEISRPIQN
SAEYVAEIDM HNRYGEVQDL ENSQIVVTDH LKAPLIDGSI LNTTQKSQPI LQNANHLEYL
SIVAAEEIKA TDKICDIDIN AAADFKYSDN SSSYFDEDVM LQGEFGHVEK NSGNHNITPA
RCGRERDHGH VNDKKRSAPE NLESATLSVS SVMNVPPVTE QIKDLKVRST TIGLNEDTQK
VKSLHDCKAN LSDVSKCCVV NMKEIGGIQL KEHLTKYKEK ESAIVAGEYN KTIEHNNFSQ
LTAVHNVESS IITQPMVGKI MNSSSDAQED CRDYTKRPRG NNLNKVKSAA IVPNHSLNYI
KTDTNTESRR KTCQMFTLPS NITQRFSPDT KIEKSPLTSK NDRSQGEPPT THTVSIISEG
QKKPLTEKSI AFTPSLNRQQ TTAVKIKQPL PAARNEELIS GTCDKTRFLK TSSEDTRATT
ETGSLAPSLN DQRKEKPVKR IRLSTDNMGK HPLENSKQAY SSTGKENLGK KIAVFKRVNE
KPKEEQSLKF EHKELKSIKC PLKDDHKDST IIWTKNSIVL TEAERSAGDD SPVSLAIVQT
TMKDRGLYQC SLKNKYGSVS CEFDFTTEVL NELLSYQVVE GHGYIESNKH NDLHAFPDSG
TGEKIELLQP IIKKELPNEC NFDVKMCGSI ATEKSHFGEG LHRKAFRTKV IYGLLPLFNS
GHRCVLKIHN AISHGTKANS ELIKQNYQLA VQECHVQNAA RQYGNMFSAE GTLLEGFGEA
PEVIPIYLIH RPTNNIPYAT VEEELIGEFV KYSVKDGREL NCGRKESEVG LKCCTFQHWV
YQWTEGNLLV TDMQGVGMKL TDIGIATSRK GYKGFKGNCS ISFIDQFKAL HQCNVFCKMM
GLKSLNQHKP KTISPVKTQV SKPISWSTKK MPQSPQSTNR IFVKSTFGDK TSQRHL
//