ID C3YCA3_BRAFL Unreviewed; 2077 AA.
AC C3YCA3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_88035 {ECO:0000313|EMBL:EEN62135.1};
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:EEN62135.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN62135.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN62135.1};
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GG666500; EEN62135.1; -; Genomic_DNA.
DR RefSeq; XP_002606125.1; XM_002606079.1.
DR STRING; 7739.C3YCA3; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG4625; Eukaryota.
DR InParanoid; C3YCA3; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR006573; NHR_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR040847; SH3_15.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF07177; Neuralized; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF18346; SH3_15; 4.
DR SMART; SM00588; NEUZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51065; NHR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
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:ARBA00022527}.
FT DOMAIN 449..604
FT /note="NHR"
FT /evidence="ECO:0000259|PROSITE:PS51065"
FT DOMAIN 1770..2041
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 251..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..224
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 260..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1800
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2077 AA; 230132 MW; 1BC83E36FDAB54A4 CRC64;
MGKDKRGIYR WDCRNCGDCT EFQPSSRGLR CEYCDCAPTH HSKDKTVPVQ GYPTDYEERS
NEEYMYHQNS PTDRQSSGYD SPGTQYFSNP TQPPAHNIPF APRNEPCYYQ EQPREVYYSY
QPRDAVYTGQ HQQHGTADRP VLVRPCQQVN GNPQVYFPGG RDPPYHHQAE AHYTFHPPHT
RGSDELEIGP SRIDSYAAMM QERLRNLEEE HSNLKNELEN LFVSAVPGMD MQPDTQSPVA
TNQVAAYIRG KPPGWPQPFK NNSDHPSPMK ISQTTSQFGP SSDKNVVDQT VDTSRGRQDD
TSVETSVVNS SEQPSTAEAK AEVAYINATP TGLLTVEKDS PPNASAGARK PDQFKHGTPS
QKTIPTRVTS NNSSGSSKTS RIASVTEIGQ PGPNSERDIQ KSQANSNSAA RNGSPDNPAE
LAPSVSLPTP AVKQELQAKQ PILKLYQNHP TFNTKIHGEN ICIEQEGTTA HSTNSLCNGI
CFSRYPIKIG QQIHLMITET KKFTGSLRIG FTFTNPESID AESLPSHSYP DLAQKPGFWV
KPLHDRFAQQ GNVVTYKVDS SGDVFYSINA KDRGLFFSGV DVSGRIWAAV DVYGSTIAVK
YVDEEAACDK GNRTIQEGDM VRLEVDCVET LKWLQEGHGG LGDLAEFIKQ DGVVIRLDDE
EDVVVRFNSH KKLWCVNPAA LQKVGTTDPD ASIIMEGDLV TERAMAGNES INNTGRVKKI
TVSGDICVRN ITGKTAEFTT DFLRKVKRAP GEACEKGLHY WKRGVAKVCT DCGQCTDKGA
SCNLKASPLR SPGSPCGCGN RVEGCADCGL CRTCAGEPAE EKETEEGELG KLLRALYKRH
GVGEEEDTAH GMTKGDKVMV DIDADTFRML QEESRLHWNE DMRKVIGVEG TVVQSTKNSV
TVQYPDGVRW SLVPGCLKRT SPGQHEGRAW IKKGELVRVL NDERKVKRLQ EGHGGYKHDM
QASLGKTGCV LKVKKHQVKV EVNYKSWWFN AEALTPAMQG SIEEVATVCQ LKEGDHVQVD
LDVETFKTNQ AGHGGYVSKM AELVEQVGVV HQIDMDGDAI VYYPNGTSLG KLASEECGVV
DVSGVMEVGD WVKVESDKKK IKHVQERTVT WDEGYYDAAG KVGQVQTTYP FNDVVRVSIE
HKGYPLNISL VTKATAQDVH EAFGSGDVAS PGVGRGDLVK IGVSVDKLKR MQDGHGGFVD
QMEEATGTIG SVSYIDRDGD VYVRFNVRRL CFNPDVLSRV TPVENTFYVG DIVLVESDQD
RFKLLQTEEH GGLNSRMLMT CGKTGRLHSI VSQERIRVKV QGKVLETGSQ LPSVPQDNMT
GAGVAACLCG CGNGDAGCDD CGYCRRCAGE LQMRERDDDE QDDVMQKLLQ LGDDIGGLFT
GPLHEAFMEW LGKKGEKSDT PGHGRGDTPA PPREEMAPVL KKMSQAVELM RKSKSLDSLD
VVKNALQNDC FAPFQKYNSI ADKRLMADTL ANVDGAQIFM DYLRLLSSVS EGNEVTAHSQ
VQECTEVLQT LLISCTSNSF EFCRAVGRCG LLQMFVQDLV ALHKEAQKES TRPKIQFRLI
FLANCAQTPD IQEVFTHCDS AEALKPYLRN KDANIRFTTL FCLAFIVENQ NMHLIRVNVD
GAELIVTLLK DALDSPEHVT LIGDYTCTAL EVATMLSALV RNDENKQVFV TNGVVDLLIR
LIEIGTDREK EAAILCIQKL AYSDHISTII KKETRAEQVL RALKHDRGLS SLIRDVAAAA
LQILREGPPR VVEDQSGGPG IISTINYSDL TVNNVVGKGA FGQVCKGYHK KWMVDVAVKK
LNSSSREQSI RRSKALMEEA NFMYRARNAN RFVVGLYGVC IEDTFTAMVM EYMANGSVGD
LMSRVKHVPW ALKWRILQET ILGMNFLHSL DPQIIHRDLK VQNVLLDEDF HAKISDFGLA
EYKPLTSIGD EKGNLCGTIT HIAPEHFKNP HMKAGEKFDV YSFGICIWEV ITGKRPYREI
AIGGQEAIMK HVMKGKRPDR KQIPTEGPNE LSFFVHLMEN CWHQDAQERP TFRALGEQIQ
IVTQKTNVQV AEAIQVVLKE QERDTRLKLA ADWAADS
//
