ID A0A0M0J6K4_9EUKA Unreviewed; 2204 AA.
AC A0A0M0J6K4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Surface antigen-like protein {ECO:0000313|EMBL:KOO22241.1};
GN ORFNames=Ctob_006374 {ECO:0000313|EMBL:KOO22241.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO22241.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO22241.1}.
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DR EMBL; JWZX01003297; KOO22241.1; -; Genomic_DNA.
DR OrthoDB; 312371at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR45661:SF3; RICH REPEAT DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR45661; SURFACE ANTIGEN; 1.
DR Pfam; PF13415; Kelch_3; 2.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 134..310
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT DOMAIN 1018..1081
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1159..1486
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 313..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 2204 AA; 233500 MW; 036CE5D72CDA8206 CRC64;
MAARQLAEAA EHTHQAPLAD EVHSTAAFEA YYKAQGIVPP SEWDALLAAL HRPLPVTFRF
SAYPGSARTV SGYREQWRQL RESFPGCHTT PLPVAGAWQL PYDRATLSAR ESTVTREIHK
WLGGCGDGAA RRGYDRIVCD VPCTGDGAIR KAPELWRYWS PHLGRQLHSL QLQLALRAAH
LLAPGGVMAY STCSLNPLEN EAVVVALLQR SSGELELLPT AHLLPELQRR PGLTTWAVFD
DRMRRLHSFG QSQRKRVSKG LRRCFRATMW PPAGSAEGAD AILSVLPRCM RLVPHLHDSG
GFFVALIRRC TPAPRPPRAP SRALSPPSAG RQYRPVSPEA CRMLTSSLGL SAAEHHTFVR
VIGRRLHADD SHAVARIGGG GYDDDGDEDG ALDEKDDDDE HEQEHEHEGE ERMAAEPHAP
RTIVVLSETT AAVLADARPA FRPVCAGARV FVRFPGGKYQ LVQDGAALLL PALPPRCVAK
LPWAELVAVL QCHVRGEALG LPRGLQESVC LLGSDDGREG SDEALVACCV FAADAHDTFG
TLYALRYREG ASGNTLRWVP QPTSGKPPLS RARPSLVVLD TYVFMLMGIA GGKPLSTVAM
LNTHTYCWSM PILDGTSPPA RMGATATRVG TDLYIFGGSD GRTSLRDLHV LVYVTWFTPS
YAGKPPDCRV GHTSNFIGAR LYVLGGASQG VAHNDLYVLD PNLQTWTRPP MYGTPPDALV
GHSAVVLGSE LIVWGGGDGK AAHAAFSVID TLNMLWSRPT TSGSQPSARV GHTAVLHDSK
MFVFGGYGQR QYWNELVALD TGILVWIRPH TVGQPPAPCV LHSATLVGHV MVVYGGSFNE
VALNQLVAFD TVNMSWTNIG SFLWEGPRPL PLFGHGAVAI DHRLLIFGGT TGGVPDSLAS
YLFGRGFVTG YAAGARNDLV VMDLQARTFS MPKYAGRRPP PAYRHTVSTR KGKIFVFGGV
GGDGHMSLLD TGHAPGEVAS TGVLKKAPST LDAAAAGLFA AEMGAEFGRT DGRGLDATRA
SQLVSLLQEL DMNKYTRLFL RQEVDVDSLL TLSDADLKDM GVTALGARRK LTVAIHKHKL
QQMSEKGGGG STAIKAGGAA AALAAAAATA MKVKSTAAAG SSSAADATSS RRTEDVDGRT
QGAQTHGFVV AGQVYRGRYL LNGKTYIGGS ARVVLGEDVK TGQPIAVKVH SSRTYFAREM
KLLRAMQSEY IVRFLDAFDE EDAPSAVVLE GGSCSLAELL AEGQLQPVER KHVLERLCLA
VDFVHSRGFV LVDLKPANIV IFGSLLTFKL IDLECLRKNG DTVHFKLTPF YAAPELASAA
LETMRLGALP PLEYSRARGP VDATSDQWGP NLGKGALLSE SPTLARAVAQ ASSVVNTAGD
VGDFNKDELR QLEAPLKLPN GKPLRASVAM DIWAVGLIAF ELFTNEPFFA GCSDDVALQV
LASSTPLELP MARIADTQAQ HLLAKILVKR PKERATIEMI LRHAYLVGGL DTQQVGGSFA
MLHESQSAFK SELDRLQAGL GPMGGESHFG EPRFGSPAFG GGSSVLKKAH GGGSSGGGDR
KARFAGVRSA EGEEVAWSRL AAARSATLAN WVSDTGGAEG AFATLVPAAA LRTLSRVAEG
GAEDGRALEG CSPAQLAQLL HGAHFLDVDI ELRRLLSRSL CTGHLAGKSG PELGRLLDVV
SDFPTEAERQ AATEEPLYTQ DAQHNATAPG AADAPTPPAP MCWLSTQLVN EDALEDALAD
ADVPTLCALK GVSLAWRARA RRVLCARLCT RVGLPLTSNL VEVTELNLLD SRAAGRLIAD
AVDASCGLPN LAKVTGLGGF EVDVAALRRV ASSDGSEEYG DGTQPYPMAG VRACIRGEGE
VPMEVLLAAC VLRHGEAHVL VNAFRDDTSM TSIALPAGLT SIGESAFEDC SSLTSITLPA
SLMSIGVNAF WGCCSMTSIE LPASLTSLGK CAFCGCSSLT SIQLPAGLTS LGESAFEFCS
SLTSIELPAG LTSIGSCAFI SCSSLTSIEL PAGLTSLGEF SFEGCSRLTS IELPSSLMSI
GVNAFEWCSS MTSIELPASL TSLGERAFCG CSSLTSIQLP AGLTSLGESA FECCSSLTSI
ELPAGLTSIV SCAFISCSSL TSIELPAGLT SIGDYAFYGC SSLTSIELPA GLTSIGDHAF
HGCSSMTSIV LPAGLTSIGD DAFYGCSSMT SIELPACFDD SMTA
//
