ID A0A1Q9CC80_SYMMI Unreviewed; 1852 AA.
AC A0A1Q9CC80;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Rhamnosyl O-methyltransferase {ECO:0000256|ARBA:ARBA00016626};
GN ORFNames=AK812_SmicGene39038 {ECO:0000313|EMBL:OLP80539.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP80539.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP80539.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP80539.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the O-methylation of the hydroxyl group located on
CC C-2 of the first rhamnosyl residue linked to the phenolic group of
CC glycosylated phenolphthiocerol dimycocerosates (PGL) and p-
CC hydroxybenzoic acid derivatives (p-HBAD).
CC {ECO:0000256|ARBA:ARBA00003116}.
CC -!- SIMILARITY: Belongs to the rhamnosyl O-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007565}.
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:OLP80539.1}.
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DR EMBL; LSRX01001371; OLP80539.1; -; Genomic_DNA.
DR OrthoDB; 213738at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR007072; RNMT_CmcI.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR40048; RHAMNOSYL O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR40048:SF1; RHAMNOSYL O-METHYLTRANSFERASE; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF04989; RMNT_CmcI; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:OLP80539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:OLP80539.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1320..1344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1365..1398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1507..1542
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 637..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1852 AA; 204644 MW; 740D46655A300272 CRC64;
MVGTLQIAPG AHSLFAGVFI QKMPTDLWCY QQVIHDLRPM YIIDLGSSQG GSAVWFASML
KLFDIPGKVI SVDLALEQAY WLTKQRAEAA VQRLKLEAFV DWNYVTGGSK NKEIRAKVKR
LCKQGPCMVV SDSDHDYEHT YHEMEWYAKH VSVGQYLIVE DTNIYGWTGW VNINDPNEAE
LRKGPMEAAN DFELAQRADF VRTDWCAKHY GGLSQTQNGW FFRKAKRSRG FAEHVGQLPE
AGGGKDTYQM RKPFVEGSKE ALLLGDSWAA YAGTSLKAGL ALVVNRGLAG TTAADWASNL
DCFRISEGHV FSHARTGQDP NASVRHRAAV AQNVTFVNVS RLLQIVDGSC AARSYGLQRP
GIAWGFLLAP CLEEKVSESP FAHQLRKIGS RVNSLECLNK QHRALSSTSM TPFALIAAFC
LWHGAESRNA PVNMALAGDA VWFRMEDDQI CAGLGTSERD SDASQCLSTR DFTQEELLNL
LEPLLARIPA NASGRTSWRA IIGSLAVTLS TWTLMLSCLR ICCRQKAGKR ARISCTLLHR
WVRDCGDVPI KMPFLLRRGR LRATTAFSTP RQYEVDSEEA ESTLGSVKRV RKVFFTFPLM
GVKVVLDKMI VSPLTVAQAA LLRRRAAQTL RLQDQLLAEG GNTPGAGRKR ERASTSSLPQ
RIKRKSTARE KPKEPASRSS AATRPRLVPD DFPEPSLPLF PPEEEPAVDE WCQVQRHSEH
PKRALPAERS RPAETSKLAH AGKTGESAPS KSQLPTRKVS VHCTVDEHDD GEGGELLDDA
LQESSSSKPT AIAAEVATQP TSVKPPSPRP SLPVSVERPR QTPTVLRISP APSPLPVAAG
PGPGASRRSL EDPRSAASGS SPCVGAPPDA PLPPTQRPNA TEPRAEPRGD SEDAEMPVIL
TPLAPPPLHP PKLSGTAEPS AKLQGEAQDE DSEPRRPPPP DMPPPPCPAG QEILRWLQQP
PRGETAVPVV ADMGCFSGGT GGTPGWDGGM IQSCDTEEAI YDYQPPWKSE CSGRFTAEDD
VGKRLEAMVE ELAGPSSFEL LEDAFSKVDA ARVGSMPQGN GLPHSPGCWV RRVCRELPGM
ATRDLFSWLD ASLQREREEL AIRHHEILQE LHQLVQRNEL LKSEATNRWT PDVTDKMPAD
SAEGVKLTEM DLAQVQRTKS DEPSSIGRKM AEFHVVRVQG QTKVLRDPVS VEDTDVKRRD
HASRFERMGS ASSGVLKAET PKGIFKFVFD PMFETVICVL IVINSIVMSF EAQHAGLTLG
YDLGIRTYNA PGTELWPGAA DVFVASEWFF GPIFAAELIL KVIGMKCQFL RDFWNYFDTI
MVVAWFVDTV FSGLLPVDPM LLRLARLARL LRLMRLVRKL KGFDALYILT TALRGSVTVL
LWSFLMLFLL QLMFALFLQR VVSDSIESNI ANQVLMAESN ELFLYFGTCS RCLLTMFEIT
LGNWPPVARL LQDHVSEAFT AFSIIHKITI GYALIAVING VFLKETFQAA DNDDKIMMRN
TEKKRHQHIK KMKSLFEAAD ETGDGVLDQE EFMQVMTDPE IVNWLAAMDL HISDPNMVFD
MVQEDGGITA EQLVKGVSRL KGSARSTDLH LLTLDVKKLF FLVQDLHSGA RRGFSGAGFA
QPVPTAHPAK CQLRFMNPGY QRPEAWSQGN ADPRIHDGDL RPRAQGVRET STLEWAAFQL
TPQRICTVAS LSELSLRRQF DEGFFLGGEV ITVSCSPVAM FIAVDGTAAR PMVGASPKDA
GFIPKAMLQE VVALIFEYLP APAIKRIRRE LMVKPIYFLR QAAAQDHFTQ LRAFSHLAEF
ENICGGFEQG GLRAGPTPCR PGLHTRAAVA RQRADDRLRR EPPATAHQQM HV
//
