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Database: UniProt
Entry: A0A1Q9C7P0_SYMMI
LinkDB: A0A1Q9C7P0_SYMMI
Original site: A0A1Q9C7P0_SYMMI 
ID   A0A1Q9C7P0_SYMMI        Unreviewed;      1739 AA.
AC   A0A1Q9C7P0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Putative methyltransferase, chloroplastic {ECO:0000313|EMBL:OLP78939.1};
GN   ORFNames=AK812_SmicGene40831 {ECO:0000313|EMBL:OLP78939.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP78939.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP78939.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP78939.1,
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   -!- 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:OLP78939.1}.
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DR   EMBL; LSRX01001542; OLP78939.1; -; Genomic_DNA.
DR   OrthoDB; 313813at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   Gene3D; 1.20.120.400; Nickel-containing superoxide dismutase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR036502; NiSOD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR014123; Superoxide_dismutase_Ni-type.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF09055; Sod_Ni; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF109770; Nickel-containing superoxide dismutase, NiSOD; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000313|EMBL:OLP78939.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Transferase {ECO:0000313|EMBL:OLP78939.1}.
FT   DOMAIN          590..671
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          348..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1317..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1693..1739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          432..466
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        355..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1346..1365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1366..1400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1405..1421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1695..1714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1739 AA;  190760 MW;  FE514CD984A54E5E CRC64;
     MLPAARIDMV SRYLLQKQAP PQAVEEEEEP SLLKRLPFVE QTDAIAGALG LPQSQEVEKL
     GRELLKEPQR LLGGPLQPAG TSTFQSPLVS FAYERGWRRS FASSGFPGPD EEFRLAQDFL
     REGTGLLGDT LLDASCGSGL FSRRFAASGD YSTVVALDFS ESMLRQVDDF ARQEIGPDYA
     QGGEGKTALQ LVRADIARLP FESGSLGGVH AGAAIHCWPN PELAVAEVSR VLRPGGVFVL
     TTFMPRGPLR TMGTNRNPYK FWTEEELRSL TSRCGLSDFK AIIKDPAFIM VRVKKPTAST
     PTALPLARPC EFVSQERLWK PLEAMSLSSN PCQRCRPDVQ VWSSRKRKLD ETTVRSPNDS
     IPTTAGTPVD SSSERSDFCF SFLHVSTSSQ GRRRQGEEAR GGRRSGASMA LQDSELEDAI
     HGLDLYACRQ YLKQLQVEKS LRREKLERLE EKLKATNQEL SSRQVEADKR KLEFFAEQEI
     NRRRADRRSK PDAGVLSLHG DPHDDLAQAH EQRRTSARNF IERELQTEMS KQQRIERTKF
     GFKEYEGARL MVFKPEEDIE EERSLRDSVL VTYAVPHAEK RKNLTYRIAR DTSIKSLKDD
     ACATGKTITL DVEASDTIDN VKAKIQDKEG IPPDQQRLIF AGKQLEDGRT LSDYNIQKES
     TLHLVLRLRG GHCQVPCGIF DDPKLVADVN EAVATIKKAM VQIGELSASM TPLNINQMTR
     WVNTKEEHAG KIITLMSEYC LCQRIKPVSD PKTPFSSEAD FIAALQAHHQ VMLAAVKCKQ
     NVDPALADSL AGAVAEMSKM YWGLSEVEFV LKTVSNAKPC DTMKVVDAFR KDEEAHFVLV
     QKAPKNISLL DKEYMDIIPK TGRRGQQLRQ QLQEKSATTS ALSGADGSLA EQMVLLPGLY
     QFMTQRDKDV KQHLQRTKLR SLCVYLVLAI LSASNVYLLR PPGEGFYCTK GILELLAGDV
     HSKPMADIRD AQDVWQWLDT TLVAEVLTDN STLRQSNYLV GYLQVLQQQV AAPSAMHCRG
     IEEPDDNSLS CADPGFCILS IRNFVDCRSP WPTYVVSWRR WLGGLAGFGG GDDGGGSVGS
     GGVFVGAHGG CAGWYAANLR ETMQRRLPAT XETMRRRLPA TAATASQVPQ GATSTSTPTP
     RTPSRTRTPA SSSTTLGAPP SAWMDGVHWQ SPTAQQPHDD GVSGSVFLDA PPPDRSQPTG
     AAFLQTAVST PASTTPGDGT PWGLTPEMVR QGIARMEAES AAISAAQTPG VTIQIDAEGR
     RHRAPPPGAE QRPTRPSSPP SRSTANLATF TPGSVAGTSV NTDEVLNEAA IRLAMSNRNN
     AGPDLDAQSP VPAPRRSIFP PLRETGNAEE ARRGRAERRG GERPATADDP PPPAPVQDYP
     PLTASPVTWT PAPPVTGPLP AERRTPAQAT SSTTTPPRTT TPRRRSADRG DRGTPERVAS
     LSPGPTRRSG TVGIRSKLSE AEVAEIRRNL SPDYSRYKDR MHRRGAAAED DVPQSIRHLA
     RPTVEDVIQT EAAADAGDPS AVPKIPPAEA PTFCGYWLCR RLPEGYLGAR IPWEATTPEP
     AAEMDGNRRY PPPTTRRLNC HGTGAVDDDR RLDLWLGVTN SPSVRDSFPV LLAHGVPEEV
     LLAILAPVPP QPPAQLVAQL RSDVPERRPS TRASMAAALE AMEPSRRAET MAAIDTNLLA
     QSTRRSMESR VRMLTTEGPD AHHSRREREF PAFPSRRAEA AAPRRSPPHR RVQVGGVMP
//
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