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Database: UniProt
Entry: A0A1Q9E4R2_SYMMI
LinkDB: A0A1Q9E4R2_SYMMI
Original site: A0A1Q9E4R2_SYMMI 
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
//
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