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Database: UniProt
Entry: A0A2I3HBZ4_NOMLE
LinkDB: A0A2I3HBZ4_NOMLE
Original site: A0A2I3HBZ4_NOMLE 
ID   A0A2I3HBZ4_NOMLE        Unreviewed;       703 AA.
AC   A0A2I3HBZ4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=ROCK2 {ECO:0000313|Ensembl:ENSNLEP00000041017.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000041017.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000041017.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000041017.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   EMBL; ADFV01073212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01073213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01073214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01073215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01073216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01073217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3HBZ4; -.
DR   SMR; A0A2I3HBZ4; -.
DR   Ensembl; ENSNLET00000046728.1; ENSNLEP00000041017.1; ENSNLEG00000014043.2.
DR   GeneTree; ENSGT01030000234517; -.
DR   OMA; NSQWIVQ; -.
DR   Proteomes; UP000001073; Chromosome 19.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   CDD; cd20875; C1_ROCK2; 1.
DR   CDD; cd01242; PH_ROCK; 1.
DR   CDD; cd22250; ROCK_SBD; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR015008; ROCK_Rho-bd_dom.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF103652; G protein-binding domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51859; RHO_BD; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01206, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          294..362
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          465..664
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          575..630
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          660..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          9..324
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          371..416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        678..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  82149 MW;  23BDD34321929F96 CRC64;
     MEIDMTYQLK VIQQSLEQEE AEHKATKARL ADKNKIYESI EEAKSEAMKE MEKKLLEERT
     LKQKVENLLL EAEKRCSLLD CDLKQSQQKI NELLKQKDVL NEDVRNLTLK IEQETQKRCL
     TQNDLKMQTQ QVNTLKMSEK QLKQENNHLM EMKMNLEKQN AELRKERQDA DGQMKELQDQ
     LEAEQYFSTL YKTQVRELKE ECEEKTKLGK ELQQKKQELQ DERDSLAAQL EITLTKADSE
     QLARSIAEEQ YSDLEKEKIM KELEIKEMMA RHKQELTEKD ATIASLEETN RTLTSDVANL
     ANEKEELNNK LKDVQEQLSR LKDEEISAAA IKAQFEKQLL TERTLKTQAV NKLAEIMNRK
     EPVKRGNDTD VRRKEKENRK LHMELKSERE KLTQQMIKYQ KELNEMQAQI AEESQIRIEL
     QMTLDSKDSD IEQLRSQLQA LHIGLDSSSI GSGPGDAEAD DGFPESRLEG WLSLPVRNNT
     KKFGWVKKYV IVSSKKILFY DSEQDKEQSN PYMVLDIDKL FHVRPVTQTD VYRADAKEIP
     RIFQILYANE GESKKEQEFP VEPVGEKSNY ICHKGHEFIP TLYHFPTNCE ACMKPLWHMF
     KPPPALECRR CHIKCHKDHM DKKEEIIAPC KVYYDISTAK NLLLLANSTE EQQKWVSRLV
     KKIPKKPPAP DPFARSSPRT SMKIQQNQSI RRPSRQLAPN KPS
//
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