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Database: UniProt
Entry: A0A3P8VR54_CYNSE
LinkDB: A0A3P8VR54_CYNSE
Original site: A0A3P8VR54_CYNSE 
ID   A0A3P8VR54_CYNSE        Unreviewed;      1395 AA.
AC   A0A3P8VR54;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=CIT {ECO:0000313|Ensembl:ENSCSEP00000016789.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000016789.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000016789.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000016789.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   Ensembl; ENSCSET00000017002.1; ENSCSEP00000016789.1; ENSCSEG00000010676.1.
DR   GeneTree; ENSGT01030000234517; -.
DR   Proteomes; UP000265120; Chromosome W.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   CDD; cd20814; CRIK; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR22988:SF71; CITRON RHO-INTERACTING KINASE; 1.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          738..787
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          815..934
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          968..1258
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          38..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1312..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          210..237
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          274..560
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          653..687
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1323..1370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1375..1395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1395 AA;  159845 MW;  5EA8BFB285CAE36E CRC64;
     SKINELQEKL AKASKASSEA TDLLQIMRVA KERMERDLER LQNKEASTDS LRRRLRETED
     GRKTLENQVK RLEMVETKIK DEIQSKTQQI QQMADKILEL EENLRETQAT AQRFETHLKQ
     KEKLYEDKIK VLEAQMKADM ADKEMLESSQ SKYEEEVREK CSIISEQKVV RADQPGSDTI
     LAANSSIYTQ KNMKAQEEMI SELRQQKFYL ESQAGKLEAQ NAKLEEHLEK ISQQEQSNKS
     RVLEQEIRLR EMGLEHEEQK LEIKRQVTEL TITLQERESQ VSNLQAARHA LESRLQQAKT
     ELEETTTEAE EEITVLRAHR DEIQRKFDTL RDSCAVITDL EEQLTRLTEE NAELNRQNFY
     LSKQLDEASD EREDCLQLSQ DVDRLRREVA DREMHLNNQK QNLETLKTTC TMLEEQVLEL
     ETLNDELMEK ERQWDTWRTT LVGEKNQAER KTREIQRLLD TEKQKRIRAE QRSSESRQDV
     DQAVKEHKAE ILALQQALKD QKLRAETLTD TLNDLEKKHA MLEMNAHSLQ QKLESERDLK
     QRLLEEQEKL QQQMDAQKTH IFRLTQGLQD ALDQTDLLKT ERTNLEYQLE NIQAVYSHKK
     VKMEGTIGQQ TKLIDFLQAQ AHDGSKKKKG LFGRRCEDLL PVPLQYSDMK LALDKERAHC
     SELEDALQKM RAELRSLREE ALQYKDQGNS SNPPSSRQQM IMSAMVKSPE HQQAPPNLAP
     SQRDRERERE RVMHHSTAHR FTVGLNMRAA KCTVCLDTVH FGRQAATCLE CHALCHPKCS
     PCLPSTCGMS SDCSLHLSEG LCRDKGQQLK DCSGHMHVEG WMKQPRNGKR GQAWERKFVA
     LDGTKISVYE VEPREGILKP LEKFDLCLSD GEVMVHGAVG ASELPNTAKS DVPYVIKLET
     RCHAPCWPGQ SIYFMAQSFP EKQRWVSVIE SVVASGRASR EKAEADAVSV SEPKLLGNSL
     LKLEGDDRLD INCTLPLTDQ IVLVGSEEGL YALNVIKNSL THVPGLGSVF QIHIIKEQEK
     LLMIVGDERA LCLVEIKRVK QSLAQSHLPS QSELAPYIFE TVKGCHLFSA GRVDNGSCIC
     AAMPNKITIL RYNDNLNKYC IRKEIETLEP CSCIHLTSYS IIIGINKFYE IEMKQFVLDE
     FLDKNDMSLA SAVFAAASHS FPIAIMQVAS SLQKEEYLLC FHEFGVFVDM YGRRSRTEEI
     KWSRLPLSFA YREPYLFVTY FNSLDVVEVQ GHSTLGPTVL AQLDIPSPRY LGPAISSGAI
     YLASSYQNKM RVICCNGSLI RESLELQRSG SSWGSPTKRC PPTYTEHITK RLTLGPGSHD
     GLHREPSTPH RYREGRTEFR RDKSPARPLE REKSPGRVLD SRRERSPGRF GESTHAGSVR
     TQLAPVNKVW DQSSV
//
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