ID A0A1Q9EMJ7_SYMMI Unreviewed; 1492 AA.
AC A0A1Q9EMJ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative permease {ECO:0000313|EMBL:OLQ08659.1};
GN ORFNames=AK812_SmicGene7781 {ECO:0000313|EMBL:OLQ08659.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ08659.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ08659.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ08659.1,
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 nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000256|ARBA:ARBA00005697}.
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:OLQ08659.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000112; OLQ08659.1; -; Genomic_DNA.
DR OrthoDB; 35157at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1904823; P:purine nucleobase transmembrane transport; IEA:UniProt.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR049225; DUF6822.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR006043; NCS2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43337; XANTHINE/URACIL PERMEASE C887.17-RELATED; 1.
DR PANTHER; PTHR43337:SF1; XANTHINE_URACIL PERMEASE C887.17-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF20708; DUF6822; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1072..1097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1117..1136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1156..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1200..1218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1225..1243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1317..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1353..1374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1412..1438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 603..735
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 212..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 214..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1492 AA; 165130 MW; E9E81CBBEAE6EAB6 CRC64;
MELEAASYQA QLQALLIAVQ EDNQAEEGRE EAPEQWLQGW IQEIGAFIPG YRAGQTAQLV
DSITDADIDE MVRDEEEARS ERLAMQLQAE EEEGSRQKAE AAQEALFMQE VRHLEEEAAQ
YKQWERSEEA RALKCARVER TEDHRCVLTV EIASGSGDCP RVLRTMDVDM PLNGTRISVF
LRADMERAPS EVSTVPAQPV IEDPAAIETQ LEHSAAGEQA QSDQPADQPA DTQPLPMSAV
TTATSQEAQC NTVPGLLQLM DFDEYEVLFD RWTRGELNQR EILLYYGADV LELMLAQEAV
STEDIRGHED ARQSREDDDE AHLGMRKNDD GDWVRIGYAQ FEVTYGLWKE GALAEETICQ
RYGVAWLRLF RLWKAWGLQA IWHLLPRILD VLPDTAASRR GVDFHLLKPE PLPRDLRIPW
FVVRDFHREW MAGTLTDTMV VARFGAVWLV WFRRLRDEGL ERLKPELLDY VFWDEAEVRH
ARELAAIQET RALATMHMQT NGEGPAGLPW NEFLAQDPGR TWPVLHNVMA MVLGGKHRWN
EMLFHDVHHA FPNAVGTLSQ RGRFHGWEKV HDAAAEVLHR GLWKPNGDEE TQMQKTQKKR
MKLESLEEDW QHQCGVASAR SGRSFHVTTV VGGGGANAKQ QRWRLQQGSE VVVATPGRLK
FFMEEDYVVQ KDTWQHVKAL VIDEVDTLVG EDSPNPMFDL KAELPADIQW VFVTATVSEA
AKREIRMLKG QLQGEANDLG VRRDGQIVWT RGRPGVNLQM TNCENTGENR SKLTGNASNR
RLSRREDADA SDDDHGVCGD GGLAGTVMVM MMMMMMMVIR RLRLPPPLLL PPPLLPLLLP
EEEDDRGQGD DIAGSEHVLV DCTPKSLYNL PNSARLDAVM KAKIGALAWH LEKGVLCEES
DNRVMIFCNT ISNCSRVYEA LDERNPDDER SGGKQWKLLV LHGLRDKKEY QRNMDLFSTE
KVPAADFFKR RILICTDRLS RGMDFGSNPV KWASERTLVK QGARRASMLE ILGLKGNFSH
LNLKDPFNVK KLGSSYTTEI RAGLTTFLAM AYILPVNSGM LSLAVPDMKE QLVCATALAA
FIGCWLMGIL SNFPFMLAPG MGTNAYFTFS IVLGRGLPWQ AAFAAVFVAG CLFTLLSVTG
MRTLLIRLFP EGIKEIIGAG VGLFLTFIAF QSAEGMGFSV ADPATLVKLG SLSSDSYDSA
KMWLSLAVLV ITASLLAAKV PGAPLIGIVL GTVICWIEGW AHGTEGSIFG YPFGTGGDSS
AKDFRIYVPT GIVPRQQTEQ RGSYTDLLDS SGTFFAVAKV AGLTDSRGNL PLARQNMAYL
ADALAMMVGS VLGVSTVSTF AESTAGVADG AKTGLASLVT GSCFLLAIPF SPIVSAVPPL
ASGPILCLLG AMMCSSVKGV DWDDFQESLP AFVAMITMPF TFSIGYGIIA GLGLWISIQL
LLAPLRLYRG ESPMVRVHKL WGSAFVEGDE EEKGSGKGTP STVTPSQSFG EV
//
