CCHL_SCHPO
ID CCHL_SCHPO Reviewed; 377 AA.
AC O74794;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative holocytochrome-c synthase {ECO:0000250|UniProtKB:P06182};
DE EC=4.4.1.17 {ECO:0000250|UniProtKB:P06182};
DE AltName: Full=Cytochrome c heme lyase {ECO:0000250|UniProtKB:P06182};
DE Short=CCHL;
GN ORFNames=SPBC26H8.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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:P06182}.
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:P06182};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC Evidence={ECO:0000250|UniProtKB:P06182};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P06182}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P06182}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21104.1; -; Genomic_DNA.
DR PIR; T40024; T40024.
DR RefSeq; NP_596655.1; NM_001022577.2.
DR AlphaFoldDB; O74794; -.
DR STRING; 4896.SPBC26H8.12.1; -.
DR MaxQB; O74794; -.
DR PaxDb; O74794; -.
DR EnsemblFungi; SPBC26H8.12.1; SPBC26H8.12.1:pep; SPBC26H8.12.
DR GeneID; 2540445; -.
DR KEGG; spo:SPBC26H8.12; -.
DR PomBase; SPBC26H8.12; -.
DR VEuPathDB; FungiDB:SPBC26H8.12; -.
DR eggNOG; KOG3996; Eukaryota.
DR HOGENOM; CLU_048602_0_0_1; -.
DR InParanoid; O74794; -.
DR PhylomeDB; O74794; -.
DR PRO; PR:O74794; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004408; F:holocytochrome-c synthase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1903607; P:cytochrome c biosynthetic process; IC:PomBase.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IC:PomBase.
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 3: Inferred from homology;
KW Heme; Iron; Lyase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat.
FT CHAIN 1..377
FT /note="Putative holocytochrome-c synthase"
FT /id="PRO_0000121716"
FT REPEAT 114..119
FT /note="HRM 1"
FT REPEAT 124..129
FT /note="HRM 2"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 42880 MW; F8F44897D3BC1682 CRC64;
MTSSETTTDH PRTGKCPIDH SKFARSNEAN PDAYINGIKK DQQSSSWWNS LWSRNTDVAS
EPDVAMLHKK PSTVDTHDHP LANPPPGCPM HKASNENSTG FFSNLFGREK QNSEATPAVQ
PPATCPMSNS NQKPAGVSEV LTGVDSKQQS YVPEGCPVAT PKRGWFNWFG NNDDQKQEAY
EVDKSNMMYK NIPQTAVDDQ VVGLETTRTT SSIPKVDGKN WEYPSPQQMY NAMWRKGYRD
SGENVPIMVQ VHNFLNEGAW SEIKAWEREA GENTEPKLLR FEGNANKRTP RALWYMMLGR
INPNRWGSGE GPFDRHDWYV QRKDNSIVRY VIDYYEAPDS ADGKPVFSLD VRPAVDSFES
VALRWKHWRA MRQMQQQ
