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Database: UniProt
Entry: A0A1Q9EKW2_SYMMI
LinkDB: A0A1Q9EKW2_SYMMI
Original site: A0A1Q9EKW2_SYMMI 
ID   A0A1Q9EKW2_SYMMI        Unreviewed;      1336 AA.
AC   A0A1Q9EKW2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ferredoxin {ECO:0000313|EMBL:OLQ08076.1};
GN   Name=Ferredoxin {ECO:0000313|EMBL:OLQ08076.1};
GN   ORFNames=AK812_SmicGene8420 {ECO:0000313|EMBL:OLQ08076.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ08076.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLQ08076.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ08076.1,
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007874}.
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:OLQ08076.1}.
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DR   EMBL; LSRX01000124; OLQ08076.1; -; Genomic_DNA.
DR   OrthoDB; 312286at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR010241; Fd_pln.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   NCBIfam; TIGR02008; fdx_plant; 1.
DR   PANTHER; PTHR43112; FERREDOXIN; 1.
DR   PANTHER; PTHR43112:SF3; FERREDOXIN-2, CHLOROPLASTIC; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1336
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012932149"
FT   DOMAIN          73..191
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   1336 AA;  148249 MW;  113ACD6745BC58D5 CRC64;
     MASQSRTLPV LVAAACCVAV LRSFCAPSQP TFVAPQQSVH MGCQALSGGA LASGNVPAIV
     NTVPARPGVP AHFKVTLETP DGTQSFECPE DVYILDQAEE EGLELPYSCR AGSCSSCAGK
     VLEGEIDQSD QAFLDDDQMG EGFCXXXXXW EYRSSDVFDR MDVAVVGDAD AHTRCVTYAT
     SDVTIKTHCE VQGEHGRLTC RIQEEAIMSA FQVLMAMSNK DLALSSEAKE SLRRLVCTFL
     SLPHGADFTV RLHLLANAIL LALQPPDLRL QRKPVQAPRA AAFSRCGTLT RHVRNKGTAR
     DRGAAKDCGP LLIDLLKEQL FHDSAEPPNP EKKRRAIEER TGVKSLRVQL RLREKTGAPH
     TWPWPNGMEH AEPDWVTGLS VFCEAWFPSE AEQGQSIPGY WFGARKASYR PLFDKLNASC
     LEPARRLAAA GQFRRMWWPR WEPSASARMR LKAAIFLDQT SRNYQSTQRG DDALLKAARV
     KEQCDAVALQ MALSVVAAGG GTANGAFFLQ LGSVPELCFL SLVLRHTREP CFIQLAEGML
     VSIVEELQRS DHGLPSEGLQ GHLGLCSRFL EETRDALEAV GVEAYLQRAL QTDQPLLIGQ
     PEQTPRLEVL DQRCQAHAAG LRFLDPLLCD TARFEQHHLV EELRRSLQVL GFLHAESGIV
     LSLSGGVDSM VTCCLLWLLR RRLPPEQCFK FCALHLCHPN RDDARDEEGW VRWSCSKLGV
     ELLTYRLKIR RPHGTLRTGI SRERYEEKSK QIRFRMYSRC FEHLGVPFER GATLVAHHED
     DADENRLAEL GKGNIIHIDG MLPSSTTQGV TVIRPFLKVR KAELIGFADL AALCYMQDST
     PKWSRRGWIR YVLDEMNSEE QQSFTRLQML LSRAGEASAT LGEAIDESLA VWKESDITSG
     VISVPEVTLT TGDSKKGQEQ IVHGYSSHQV PVVVLRLPVL FTLAQEFHQK VKQLMDDFRD
     IASIWNKAIE KQTAMPNGHG DGARKTGAAH ESLDMEDEEA GACPLQAVRV CDGPFEMGPF
     VLGRAVCVAL NAVPEVHRLL GGQLVARKAL KHVWDCVVRA RREHHWGTLH KMCPFLYVRE
     ASSLVLCDAQ ECGPEFADAR WQRHFVAAVT EFLQTQEKAG SPLVILVWGS ELWSFPAGWR
     LTMFFCCTCA DEQTKLCFGD NADVVDSGQK GDKEKTVGHL SAFSARAPID ATQEDDRETA
     KQRLQRLIRD FAHDAVGPGL PVEVSIQESE EGTANFQGML RLDRRLSQVE IWPAAEEGTS
     SSITVPFNQV KSVSKLSDCP DIDISETKDG DAPSLTIEST RKPTVKLCFD STMSRDRAYT
     CLRIFHMSMD QPVAAG
//
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