CCHL_CHICK
ID CCHL_CHICK Reviewed; 273 AA.
AC Q5F339;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
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; ORFNames=RCJMB04_37l21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; AJ851811; CAH65445.1; -; mRNA.
DR RefSeq; NP_001026446.1; NM_001031275.1.
DR AlphaFoldDB; Q5F339; -.
DR STRING; 9031.ENSGALP00000008922; -.
DR PaxDb; Q5F339; -.
DR GeneID; 424482; -.
DR KEGG; gga:424482; -.
DR CTD; 3052; -.
DR VEuPathDB; HostDB:geneid_424482; -.
DR eggNOG; KOG3996; Eukaryota.
DR InParanoid; Q5F339; -.
DR OrthoDB; 1282808at2759; -.
DR PhylomeDB; Q5F339; -.
DR PRO; PR:Q5F339; -.
DR Proteomes; UP000000539; Unplaced.
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 2: Evidence at transcript level;
KW Heme; Iron; Lyase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat.
FT CHAIN 1..273
FT /note="Holocytochrome c-type synthase"
FT /id="PRO_0000331126"
FT REPEAT 30..35
FT /note="HRM 1"
FT REPEAT 40..45
FT /note="HRM 2"
FT REGION 1..39
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"
SQ SEQUENCE 273 AA; 31438 MW; B38205DFF1E3E32D CRC64;
MGLSASSPAA TAQSAAEPSK QHQVASPPSE CPMHQEKMRG CPMHMKASDR RAENTDDVPA
HQERAYEYVA CPVKSGASQV NDDIDPSNMM PPPNQLPSPD QPFPLSTVRE ESSIPRAHSD
KKWVYPSEQM FWNAMLRKGW RWKDDDITSE DMTNIIKIHN QNNEQAWKEI LKWEALHAME
CPCGPSLMRF GGKAKEYSPR ARIRSWMGYE LPFDRHDWIV DRCGKEVRYV IDYYDGGAVD
KNYQFTILDV RPAFDSLSAV WDRMKVAWWR WTS
