ID A0A1Q9C496_SYMMI Unreviewed; 1373 AA.
AC A0A1Q9C496;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LINE-1 retrotransposable element ORF2 protein {ECO:0000313|EMBL:OLP77726.1};
GN ORFNames=AK812_SmicGene42184 {ECO:0000313|EMBL:OLP77726.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP77726.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP77726.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP77726.1,
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 ATPase C chain family.
CC {ECO:0000256|ARBA:ARBA00006704}.
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:OLP77726.1}.
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DR EMBL; LSRX01001721; OLP77726.1; -; Genomic_DNA.
DR OrthoDB; 3310054at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR CDD; cd18182; ATP-synt_Fo_c_ATP5G3; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 1.20.20.10; F1F0 ATP synthase subunit C; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR InterPro; IPR019530; Intra-flagellar_transport_57.
DR InterPro; IPR000477; RT_dom.
DR PANTHER; PTHR19446:SF415; REVERSE TRANSCRIPTASE-RELATED PROTEIN; 1.
DR PANTHER; PTHR19446; REVERSE TRANSCRIPTASES; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR Pfam; PF10498; IFT57; 1.
DR Pfam; PF00078; RVT_1; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW CF(0) {ECO:0000256|ARBA:ARBA00022547};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 154..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 734..1012
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 322..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 154481 MW; 0FA431987D7656C2 CRC64;
MYMSVLNVLR STDFSDVRLK RASMEAECSK LTASADVGTE MQGCSMAAPP PPPPQEVYNT
EALQLNDEVV DMLMLLDYEN RLFEKLGQLE LAMALLRSAS LRASLGAFRA ASVLPRALPN
LSAPVSASKL PEPLSAASIG LGAPLAKRHA GVSVLGCAIA MVAVGGCAQG IGQLFAALVV
GMARNPSMKE DLFTYTLIGM GFLEFLAIVV ILIAGLRCRA ALQHISFSRF CTKELKPLPR
TFFAYPAQNP AHQFKYFTQL VVWAMSILNM KADWDEFDDP NTVITNMLVI LKDMGLQAPW
LMAAALRPAA FASLTQDEQE TIRQKQKQAQ LKKKAAKKQR GASQLPASEP SEPVEEDITE
PARRLPDRTH LSLEEYFGAC PAGLFKQAGL RATEENLELL LGMDFNQVVG RFGDGSPEER
FIADGGILQE IWVPPLVRRL RIRCYNVGGV TPEIYDHLHH WLLHKSREDV IILQEIHHGM
GRSDSRWAIP GWTIVASADP QQRFSGVCII VADRVIESAR LTYNVCIPGR LLHVRCSNRD
VTLDVIAGYQ WVWQTAKSDQ IAQSRSYFWQ TLSSLVRIRD AVCALRRAEE FKKASRALRK
ASRQARRDWF EARITEAEHA AARHDIGEVY RIINLLAPKQ RREAVRIKSA EGSLLDPKAE
FEEIFEYYQS VFNRDVPFEL VTQPVVQFEH SEILDSVRKL KGGRAVPPKS VPSELWSLCA
EEYAAFLTPR LNLAESQESQ YPPEATDCTL ALLPKPHKTS RRPSDLRPLG LQDASSKVLA
NAIKHQLQQH TLEYLHSRPQ YAYTPDRAID EAVGRVARHC RLIRQRVHAS VASVHARRAG
VKQSQCIGGA MLGIDLSRAF DCIPRAVLQR SLQHAGAPPP LVQAVLQLHE SCRYSVRHKG
YQGSFRMLVG VRQGCVLSPY LYALFTCLVF DEIAQRTSLD WATAFLTLFA DDSHLAWEIS
TVADLQFFLH CLQTTFQAVP PDDGCVDISI AHPRVFSLKL ELPPLKRLRI LLFNLQCLKI
GVWLHSLLLL SWLSLKAIMA DAQMEESLSA QARQELEMVF SGRPSEDKSE KEKEKEDAQE
PEDGRRPKWR RDESKGKGPS SNSWENWSQG KRHWSEQQKS KESSKAEDPQ TQELLRCLVK
MSVRHEQELM RIRPDVGFIA FCDTSDLGCM GMLREVALSW SDLFSQGKVN TALKTMLVMS
MMKDMKERAE NVLREEDQLQ RCFTVGWLKE GATGLDPVWV YHTWNAKEKK QEVASTPPLK
HSDVLKLLDV LLEHLPRDGV VTRFNTTKRL DLMKEFKTEV VPMMLQLSLR GASAQLCYDA
MKALSGNAAM KLQGVRWRPE RAQKPPLAKA LEEAYLATSF CDWAPRDQSW ARR
//
