ID A0A1Q9E4R2_SYMMI Unreviewed; 1483 AA.
AC A0A1Q9E4R2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Choline transporter-like protein 4 {ECO:0000313|EMBL:OLQ02424.1};
GN Name=slc44a4 {ECO:0000313|EMBL:OLQ02424.1};
GN ORFNames=AK812_SmicGene14745 {ECO:0000313|EMBL:OLQ02424.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ02424.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ02424.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ02424.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000256|ARBA:ARBA00007168}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {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:OLQ02424.1}.
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DR EMBL; LSRX01000264; OLQ02424.1; -; Genomic_DNA.
DR OrthoDB; 8499at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR007603; Choline_transptr-like.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12385; CHOLINE TRANSPORTER-LIKE (SLC FAMILY 44); 1.
DR PANTHER; PTHR12385:SF14; CHOLINE TRANSPORTER-LIKE 2; 1.
DR Pfam; PF04515; Choline_transpo; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 2.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000186817};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1008..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1056
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1282..1302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1381..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1414..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 540..913
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 359..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 853
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 640..646
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 665
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 692
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 803
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1483 AA; 162313 MW; 5604E934F9AD537B CRC64;
MRRLGCPGDP SSASYDMLCV ASCALQAVER EQVAQAPRLQ LSTGRILGEY VGGTEHFSSI
PFAAPPLGER RSWNAAATGL RMIAEGDPCS GWIRGRRIGS LRIYGGGLLG GSKDDPGSSG
QCYAEQGIIY LSINYRVGAL GFLCPKGGDA NCGLWDQVAA LQWVQKEIRV MGGDASCTDV
CCVPVLVVFV LWPIVVVIGL KDADGAYSLT HGRDHYGQHC GREPLEAKPF AAFPDLENDF
KKDKLLQSRY GVCVEECPKQ FQTITDYEGD LKEGGQALRK EKDSLVWYIS LPTTPIAGRC
IPYDPPPEFT GSVEFCADPP CLAKDGMPQS YREVCGLHKD KTDRFWLLSK EVDDILEDGW
KREGADDQEE LGGTERGREG QGSVFAVPGK SGKGQDLDVS VNFETETRVL ELLQALASPP
SSVSIRLPLS AGEVEAHLRQ CLAAVGRQAG CDFALEDVTI IGRSAVSATG GYLKSEDETR
PLADSLSASV SADVIIDAAC AMAVLRGMGV MAATPKPLEG HLVRLWVVPE GVKPPNRGAI
LQECLGLPPW ALQESPEKWP AVLVAGGRLM MSRLSIFTPG TKGTAVSVLW RRGVAHALAP
MNAVLSDPQL DGKVLLQQLP SCLCVRVLDP CPGNRVLDMC AAPGGKTTHL AATLQGQGQG
LTAIDRSRAK VRRVEALCAA HGFGKVRCLA ADSRHLCNEA ASGRKPRSKI TEPSAAVEQA
PPELDLEEPW PPEAEEAFQR AFAEHHADRF RSTKRIWKVD ARLRRLEGGN PRPEMEVSDP
EGLRAEADGP PFPEGSFDKI LLDPSCSAMG QRPLLRWGIS AEEVRSHSDY QKQFLRTAVR
LLAVGGEMVY STCTLTPEEN EENVHWALQT LPVELLDARE KVFHPAEQGS TLLAGLPNCG
LTETERLQVL RFDPRAWDAG RKQHMYMGRS RFLHFEVPES GGEDDQQRVV AARVRLAAQD
KTETCKVKVY RDTRVQTAPV DSSLTYSLLT KYTGQIFVWC KRIYENRWLV LGLGIGGSLV
LSMAIIMGFA CCVGLVVHVL IALLFAVLIC ADYVLFRQAG LVTGRTGKMI LDALQKVTEW
DMPAELGSLI QDSTQDEQMR EVYKWSAVGL LLCILLLACA ALAARKNLQI LVALLKEASN
TMREMPSLLL APFMLALSMI FMSVVMLWVS LAFATASASD IPRTTEAWHL YIYPALKAAG
LAQANEMTQM RQTALVFNLF VFLFIYHFHV SLCIAITAMC VSHWYFYRND PERNAGTGVN
SEGWFFGRPI LLAFLRLCRH HLGSLVFGSC IMAIATMLRL IFEYIAAKTK DQESNPVVRA
AVCACRCCLW CLERCLQFIT EYAYVYVAVT GKTFCSSAHA SFVFFAKYPV QTAMDKMASA
ALGYLLCVTV PLGLAVVAFP WLSEGSWPPC AIVIIALAYV TTRLAAGIYD VCITTLFVCV
MRDCEHYDGR YMSKTLRSAC GFGELARQSL AARQSAVDGI ELQ
//