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Database: UniProt
Entry: Q5ENR0_HETTR
LinkDB: Q5ENR0_HETTR
Original site: Q5ENR0_HETTR 
ID   Q5ENR0_HETTR            Unreviewed;       163 AA.
AC   Q5ENR0;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Cytochrome c-553 {ECO:0000256|ARBA:ARBA00033211};
DE   AltName: Full=Cytochrome c553 {ECO:0000256|ARBA:ARBA00031247};
DE   AltName: Full=Soluble cytochrome f {ECO:0000256|ARBA:ARBA00030448};
OS   Heterocapsa triquetra (Dinoflagellate) (Glenodinium triquetrum).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Peridiniales; Heterocapsaceae;
OC   Heterocapsa.
OX   NCBI_TaxID=66468 {ECO:0000313|EMBL:AAW79333.1};
RN   [1] {ECO:0000313|EMBL:AAW79333.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15843030; DOI=10.1016/j.jmb.2005.03.030;
RA   Patron N.J., Waller R.F., Archibald J.M., Keeling P.J.;
RT   "Complex protein targeting to dinoflagellate plastids.";
RL   J. Mol. Biol. 348:1015-1024(2005).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC       {ECO:0000256|ARBA:ARBA00002347}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000256|ARBA:ARBA00004456}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000256|ARBA:ARBA00009650}.
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DR   EMBL; AY826872; AAW79333.1; -; mRNA.
DR   AlphaFoldDB; Q5ENR0; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR023655; Cyt_C6.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   PANTHER; PTHR34688:SF4; CYTOCHROME C-553; 1.
DR   PANTHER; PTHR34688; CYTOCHROME C6, CHLOROPLASTIC; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   2: Evidence at transcript level;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Signal {ECO:0000256|SAM:SignalP};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..163
FT                   /note="Cytochrome c-553"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004255718"
FT   DOMAIN          80..160
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   163 AA;  16605 MW;  D2EA15B65E9F2A6E CRC64;
     MQRSVCIVAA ALALYGASCF VMPSMMGAAP EVGRQAVREQ ALAAAPEAAS ASAGSWSPLA
     LGAALGLLVA VATGRPALAA DLENGESVFG ANCAACHAGG NNSVVPEKKI KKEALVTYGK
     YDVAAIIKQV TYGNGSMPAF GERLGPDDIE DVANYVFGQA DKW
//
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