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Database: UniProt/TrEMBL
Entry: C3ZAH8_BRAFL
LinkDB: C3ZAH8_BRAFL
Original site: C3ZAH8_BRAFL 
ID   C3ZAH8_BRAFL            Unreviewed;      2208 AA.
AC   C3ZAH8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BRAFLDRAFT_119973 {ECO:0000313|EMBL:EEN50381.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN50381.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN50381.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN50381.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; GG666602; EEN50381.1; -; Genomic_DNA.
DR   RefSeq; XP_002594370.1; XM_002594324.1.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; C3ZAH8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00364; LRR_BAC; 5.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          1378..1565
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          1924..2182
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          878..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1951
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2208 AA;  248069 MW;  C71181C1E7E5F714 CRC64;
     MEPLAPAETK KDRTLDLMLV LKEHFDPKQI CSVLNELMGL VEDGPSLECM EDYHVHQLIL
     DLMTQFKTNP DVQEVGCNAI WKLFHHSSRQ RKRIDKAEAY KLVMEAMERH KQVEAVQAAG
     LRCAAYLAIS RTTRASMLEN EIMDQVIIAM TAFKENPSVQ ANACQALTHL LFDDERHLTE
     LVSSKGYKLI VEAAAQHADC AAVMEQVLWA LRVLVTPEVN RRMLETERLY RYATSAMGRF
     AHEGEVQAAA CGVIEMLSTD GDALNASDDE DTFESRLVTG QNISWLEDIF SALTNHASDP
     AVQEAGCRSL CKLLEHHPDL IKHIGEEDNQ MPIHSAVLAA IMMHGEDQYV FKVACEAIYH
     LTAEWVLFCC CVIAEPLQTL MMNKGAYLSI LNYMGHHATI PGAQQFACRA LRGLTLLNDD
     HKQKLAEVSA LSLVASALKR FRDDVGVQEE AIGVIATMSD VVRHQCIIEK VHTIVLDSMN
     KFLLSRDVQD LGLEALGVLS LAAGVPAMLN EAGALHTTIH AMEKNPEDDS IQYKGLIMLQ
     VLVDEERFNS PQVCEEVGKL VVEAMSRFKD IIRIQEEGCV AIQLLAEMST DMSQVLVNND
     AQECLFHILE CYSYNQGLLD VASECLYVLS CELDLKPQML LSACSKGSIR GVECLIQLGA
     DVNTGEGHNT PLCLACERGD EHLVHFLLKQ LSLKKEHHSI IGLLLKHMGH DREAGVVSWS
     GLSLGGLRAE WLQPMLVDRN ITKNMDGSGV AMAAMVKHVR NRREMRPLPL TRNHFGGSDP
     SLAKMSFPLD DSTDRRFPLY RSVARPDDTN QASITSDTSF DGYEVQDIRR KSFAYARSPS
     EDSLLDDRID ASRSDKWWNR MLYPIFSVFS ELTGLGDSSR RLSGESDLEL TPAKPRKKLR
     RKYSKTGSEM PFNRWDPRNM TEKKFGQALA TIPQGKDRPL VTASSLGFSP FAQSRTGSSV
     DSSPTQLTPV GTPYTSTPIR SPSPNVLRRE RTWVSISEAE ETDSTVEEPL SPQRDSMDQS
     KSPSLAVPSQ PHADLPHKDS MDQVSPGQVK KLSLMKIEED NKQSFRKRAF TSADKPVRSL
     STNTVRLLDI SANGIVSLDG LTKSDTNILN SLVAVEKLDL SQNSLKDFPW RLCQALPKLQ
     SLDLHSNSFT TFPAHVLACQ HLDSLDLSHN KIADLTKKPS KTSFSLKEFN ISHNSLTALP
     SWIGICMPML QVLNVEGNRI ANIDDEDSFQ LRRLKFVNIS KNQLKELPLK FFLGCPKLET
     LVASCNELDN LPYDAAMKLQ NLSTVKLAHN KLAEPEPTYI PRFLLLLDRL RSLDLSNNEL
     QGLPPPSHWN THALRELMLG GNHIRKLPLD GLRLDLDPAI VKGRTKDVIG FLSQRLKQAV
     PHYRMKLMLV GFGGRGKSTL LRQLQKIKGD PRFNTATIGV LVKDWKIPVK KGRSKTHTYT
     LSTWDFAGQE EFYSTHQCFL SSRSLYLVVY DLSRGPKEVE SLRPWLLNIQ ARAPNCPVIV
     VGTHKDRIKR EEADTIILEM RHRVQTLCTT PGFPEIKGYS EVSCIKESPA MEDLRKQIIT
     VIDNFKVKGQ PVMGQMIPHS YMLLEDLVTE EAQSLKAGLP VIRHSRLLEL VKEANLQLDE
     EELSQAVRFL HESGVLLHYD DPALQLKDLY FIDPEWLCQM MAQVVTVREG NPFVNNKGIL
     KKSDVRNLFK GGAFPPELIP QYLRLLEKFE IALPQTEEEL LIPCRLPFVQ PPIDKTAWFT
     GHVYRQYVMP YIPIGYWSRL ITRLMVFSMY LKTGPLPPLQ QEYWREGIYV FWSTQEYFLV
     KRIKGEKNSM DITVPATRQG SRLLGHVVDL VDDLIEEWFP GLCEIDPVSG QTLVQRQVPC
     VLCETDPPHV FTLPEILVMS DRDDIIFCPN HDMPVPLHKL APDVMLSDLD SRYQLQEDKF
     KLEQIPENEL GDGSFGNVYR ASYKNMDVAV KVFSKVGEDH PHRMLRQEVT ILTRLQHISV
     ISLLAVGIRP RLLVLELAPM GSLTSHLCKK MSRGLQQRIA MQIAEGLMFL HTNMIIYRDL
     KPDNILIFSI AQNSPVNAKI SDYGISKFAT LLGLTAPEGT PGYRAPEVAR GDTAYNNKVD
     LFSFGILLFE LVTGRKPFED LHFRGELDEA IIKGRPLDPI TSCGSAPWPD VQDLITHCMQ
     PIPDDRPTAA EVFARLSSGE LLCLRRNVPL GKGLSPECIA IRVGGTMK
//
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