ID   A0A3Q4GH06_NEOBR        Unreviewed;      1361 AA.
AC   A0A3Q4GH06;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   31-JUL-2019, entry version 5.
DE   RecName: Full=Rho-associated protein kinase {ECO:0000256|PIRNR:PIRNR037568};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR037568};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008196, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008196, ECO:0000313|Proteomes:UP000261580}
RP   NUCLEOTIDE SEQUENCE.
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNBRP00000008196, ECO:0000313|Proteomes:UP000261580}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J.,
RA   Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J.,
RA   Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A.,
RA   Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O.,
RA   Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R.,
RA   Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T.,
RA   Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S.,
RA   Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D.,
RA   Rakotomanga M., Renn S.C.P., Ribeiro F.J., Ron M., Salzburger W.,
RA   Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R.,
RA   Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D.,
RA   Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A.,
RA   Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid
RT   fish.";
RL   Nature 513:375-381(2014).
RN   [3] {ECO:0000313|Ensembl:ENSNBRP00000008196}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2019) to UniProtKB.
CC   -!- FUNCTION: Protein kinase which is a key regulator of actin
CC       cytoskeleton and cell polarity. {ECO:0000256|PIRNR:PIRNR037568}.
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|PIRNR:PIRNR037568};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037568};
CC   -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-
CC       27632. {ECO:0000256|PIRNR:PIRNR037568}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037568}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|PIRNR:PIRNR037568,
CC       ECO:0000256|SAAS:SAAS00784564}.
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DR   Ensembl; ENSNBRT00000008431; ENSNBRP00000008196; ENSNBRG00000006322.
DR   GeneTree; ENSGT00950000182698; -.
DR   Proteomes; UP000261580; Whole Genome Shotgun Assembly.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; 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-KW.
DR   GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR015008; Rho-bd_dom.
DR   InterPro; IPR020684; ROCK1/ROCK2.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   PIRSF; PIRSF037568; Rho_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00593399}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000261580};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037568};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR037568};
KW   Kinase {ECO:0000256|PIRNR:PIRNR037568, ECO:0000256|SAAS:SAAS00593820};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR037568};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00253054};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037568,
KW   ECO:0000256|SAAS:SAAS00592725}; Zinc {ECO:0000256|SAAS:SAAS00253075};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00795753}.
FT   DOMAIN       76    338       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      341    409       AGC-kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51285}.
FT   DOMAIN     1125   1324       PH. {ECO:0000259|PROSITE:PS50003}.
FT   DOMAIN     1235   1290       Phorbol-ester/DAG-type.
FT                                {ECO:0000259|PROSITE:PS50081}.
FT   REGION      557    579       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1020   1039       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1318   1361       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      419    488       {ECO:0000256|SAM:Coils}.
FT   COILED      749    790       {ECO:0000256|SAM:Coils}.
FT   COILED      826    846       {ECO:0000256|SAM:Coils}.
FT   COILED      854    895       {ECO:0000256|SAM:Coils}.
FT   COILED      928    976       {ECO:0000256|SAM:Coils}.
FT   COILED     1078   1112       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    557    574       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1328   1361       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    198    198       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037568-1}.
FT   BINDING     105    105       ATP. {ECO:0000256|PIRSR:PIRSR037568-2}.
SQ   SEQUENCE   1361 AA;  158647 MW;  0DDF7609A6E81E38 CRC64;
     MSAGDTMEAR FEKIDAMLKD PKSEINTDCL LDGLDALVYD LDFPALRKNK SIDNFLNRYK
     ETISKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKATSK VYAMKLLSKF EMIKRSDSAF
     FWEERDIMAF ANSSWVVQLF FAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
     EVVLALDGIH SMGFIHRDVK PDNMLLDKAG HLKLADFGTC MKMNKDGMVR CDTAVGTPDY
     ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNALTFP
     DDSDISNDAK NLICAFLTDR EVRLGRNGVD EIKRHPFFKN DQWTWDNIRE TAAPVVPELS
     SDTDTSNFDD IEEDRGEEET FPIPKAFVGN QLPFVGFTYY SNQQSLTRWM SATLSDQLKW
     NVSVQLENLQ KRIYQLEEQL HSEMQLKDEL EQKCRTSNNK IEKIMKELDE EANLRKSAEA
     SLSLLEKDKL MQQHRFTEYQ RKADQESEKR RNLENEVSNL KEQLEDMKKI SQNSQASNDK
     ITQLQNQLEE ANDLLRAESD TAGRLRKSHT EMTKSMAHLE NLNRELQERS RAVEGEKAQL
     EKELLLLQST LDSERRNYSQ DSEEIRELQA RLSGLQEDNK NLKLSLSKME AERKQAQERS
     NNLEKEKNNL EIDLNYKLKT LQQRLEQEQT EHRVTRAQLT DKYESIEEAK SAAMSGMSQK
     MSEETGARMR AESRVVEVEK QCSMLEFDLK QSVQKMEQLM KQKERLEDEV KNLQIQVEQE
     SSKRIQIQND LKTRMQEMDR LRCSEKQLKQ EINTSLESKR SLEFQLAQLS KQYRGNEGQM
     RELQDQLEAE QYFSTLYKTQ VKELKEEIEE RNRQIQEANK KVQDLCNERD SLSAQLDLTV
     TKAESEQLAR ALQEEQYFEL SQENKKAVTR HKQEIGEKEA TIARLEESYK TLTKDVENLS
     REKTDLSEKL RIQDEEYVAQ KEEIEKSIKA NYEKILYTER TLKTQAVNKL AEIMNRKDMK
     LDQKKKGSTA DLRKKEKENR KLQLELNQEK EKFNHMAIKY QKELSEMQAQ LAEESTYRNE
     LQMQLDSKES DIEQLREKLN DLQQRMDNSS VTSLQTDETD SNIAESRLEG WLSIPNRANI
     KRYGWKKQYV VVSSKKILFY NDEQDKEQSN PSMVLDIDKL FHVRPVTQGD VYRAETDEIP
     RIFQILYANE GECRKEADLE TVPQGDKTNC LPHKGHEFIP TLYHFPSNCE ACAKPLWHVF
     KPPPALECRR CHVKCHKDHL DKKEDVIAPC KVNYDVTSAR DMLLLALTQD EQKKWIGHLG
     KKIPKTPPST FTRASPRSMS TRSGPNQSFR KNPKSNTGKL R
//