ID   CCHL_NEUCR              Reviewed;         346 AA.
AC   P14187; Q7RVB6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Holocytochrome-c synthase {ECO:0000305|PubMed:2572587};
DE            EC=4.4.1.17 {ECO:0000269|PubMed:2572587};
DE   AltName: Full=Cytochrome c heme lyase {ECO:0000305|PubMed:2572587};
DE            Short=CCHL;
GN   Name=cyt-2; ORFNames=NCU05601;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=2572587; DOI=10.1016/s0021-9258(19)84657-4;
RA   Drygas M.E., Lambowitz A.M., Nargang F.E.;
RT   "Cloning and analysis of the Neurospora crassa gene for cytochrome c heme
RT   lyase.";
RL   J. Biol. Chem. 264:17897-17906(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Lyase that catalyzes the covalent linking of the heme group
CC       to the cytochrome C apoprotein to produce the mature functional
CC       cytochrome. {ECO:0000269|PubMed:2572587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[cytochrome c] = apo-[cytochrome c] + heme b;
CC         Xref=Rhea:RHEA:22648, Rhea:RHEA-COMP:10725, Rhea:RHEA-COMP:10726,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:60344, ChEBI:CHEBI:83739; EC=4.4.1.17;
CC         Evidence={ECO:0000269|PubMed:2572587};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC         Evidence={ECO:0000305|PubMed:2572587};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:2572587}.
CC   -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC       {ECO:0000305}.
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DR   EMBL; J05075; AAA33583.1; -; Genomic_DNA.
DR   EMBL; CM002241; EAA31327.1; -; Genomic_DNA.
DR   PIR; A34365; A34365.
DR   RefSeq; XP_960563.1; XM_955470.2.
DR   AlphaFoldDB; P14187; -.
DR   STRING; 5141.EFNCRP00000005557; -.
DR   EnsemblFungi; EAA31327; EAA31327; NCU05601.
DR   GeneID; 3876678; -.
DR   KEGG; ncr:NCU05601; -.
DR   VEuPathDB; FungiDB:NCU05601; -.
DR   HOGENOM; CLU_048602_0_0_1; -.
DR   InParanoid; P14187; -.
DR   OMA; EGAWDEI; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004408; F:holocytochrome-c synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018063; P:cytochrome c-heme linkage; IBA:GO_Central.
DR   InterPro; IPR000511; Holocyt_c/c1_synthase.
DR   PANTHER; PTHR12743; PTHR12743; 1.
DR   Pfam; PF01265; Cyto_heme_lyase; 1.
DR   PROSITE; PS00821; CYTO_HEME_LYASE_1; 1.
DR   PROSITE; PS00822; CYTO_HEME_LYASE_2; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Lyase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat.
FT   CHAIN           1..346
FT                   /note="Holocytochrome-c synthase"
FT                   /id="PRO_0000121715"
FT   REPEAT          34..39
FT                   /note="HRM 1"
FT   REPEAT          66..71
FT                   /note="HRM 2"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   346 AA;  38147 MW;  9A6167BF3A3C05D7 CRC64;
     MGWFWADGNA SAAAPVVPPS HKDLAASGAV PPPSCPMHNK TMDALSAHKP VTPAPEPTPA
     AAAPSKCPVN HGAKDTLAAA AAAVAPKQPQ PENHQPAAAS EPSFFSKLNP LNYMFSSISQ
     EPAPNQAIAL PTERDPSSIP KGTGDGNWEY PSPQQMYNAL LRKGYTDTDI TAVESMVAVH
     NFLNEGAWNE IVEWERRFGK GLMRGWEIMK RGEENAPMML RRLEAQENDP EPQPTLIRFQ
     GRPKDMTPKA ALLQVLGRIN SKYATEPPFD RHDWYVSRDE NGQKKEVRYV IDFYSAPPEP
     TGEPVFYLDV RPAVTVTGAC ERLLRWGGDV WWKASGGEVR ERERSK