ID   CCHL_BOVIN              Reviewed;         275 AA.
AC   A5PJG7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Holocytochrome c-type synthase {ECO:0000250|UniProtKB:P53701};
DE            EC=4.4.1.17 {ECO:0000250|UniProtKB:P53701};
DE   AltName: Full=Cytochrome c-type heme lyase {ECO:0000250|UniProtKB:P53701};
DE            Short=CCHL {ECO:0000250|UniProtKB:P53701};
GN   Name=HCCS {ECO:0000250|UniProtKB:P53701};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P53701}.
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:0000250|UniProtKB:P53701};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC         Evidence={ECO:0000250|UniProtKB:P53701};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P53701}. Membrane
CC       {ECO:0000250|UniProtKB:P53701}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P53701}.
CC   -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC142105; AAI42106.1; -; mRNA.
DR   RefSeq; NP_001092356.1; NM_001098886.1.
DR   AlphaFoldDB; A5PJG7; -.
DR   STRING; 9913.ENSBTAP00000016072; -.
DR   PaxDb; A5PJG7; -.
DR   PRIDE; A5PJG7; -.
DR   Ensembl; ENSBTAT00000016072; ENSBTAP00000016072; ENSBTAG00000012113.
DR   Ensembl; ENSBTAT00000073523; ENSBTAP00000072945; ENSBTAG00000012113.
DR   GeneID; 506250; -.
DR   KEGG; bta:506250; -.
DR   CTD; 3052; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012113; -.
DR   VGNC; VGNC:29770; HCCS.
DR   eggNOG; KOG3996; Eukaryota.
DR   GeneTree; ENSGT00390000004175; -.
DR   HOGENOM; CLU_048602_2_1_1; -.
DR   InParanoid; A5PJG7; -.
DR   OMA; EGAWDEI; -.
DR   OrthoDB; 1282808at2759; -.
DR   TreeFam; TF105185; -.
DR   Proteomes; UP000009136; Unplaced.
DR   Bgee; ENSBTAG00000012113; Expressed in tongue muscle and 104 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Heme; Iron; Lipoprotein; Lyase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P53701"
FT   CHAIN           2..275
FT                   /note="Holocytochrome c-type synthase"
FT                   /id="PRO_0000331125"
FT   REPEAT          31..36
FT                   /note="HRM 1"
FT   REPEAT          41..46
FT                   /note="HRM 2"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P53701"
SQ   SEQUENCE   275 AA;  31069 MW;  09364E710C8BF993 CRC64;
     MGLSASAPAA STVQTSTPAA SDHQTAAPTS GCPMHEGKVK GCPVSAEPSD STCGSKTNSV
     PAHQERAYEY VQCPITGAKA ANKENLDPSN LMPPPNQTPA PDQPFPLSTV REESSIPRAD
     SDKKWVYPSE QMFWNAMLRK GWKWKDEDIS QKDMYNIIRI HNQNNEQAWK EILKWEALHA
     AECPCGPSLI RFGGKAKEYS PRARIRSWMG YELPFDRHDW IINRCGTEVR YVIDYYDGGE
     VNQDYQFTIL DVRPALDSLS AVWDRMKVAW WRWTS