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Database: UniProt
Entry: A0A401SJA4_CHIPU
LinkDB: A0A401SJA4_CHIPU
Original site: A0A401SJA4_CHIPU 
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
//
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