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Database: UniProt
Entry: A0A176VY29_MARPO
LinkDB: A0A176VY29_MARPO
Original site: A0A176VY29_MARPO 
ID   A0A176VY29_MARPO        Unreviewed;       171 AA.
AC   A0A176VY29;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Cytochrome c-type biogenesis protein {ECO:0000256|RuleBase:RU364112};
GN   ORFNames=AXG93_4368s1740 {ECO:0000313|EMBL:OAE25714.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25714.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25714.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25714.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU364112}.
CC   -!- SIMILARITY: Belongs to the CcmH/CycL/Ccl2/NrfF family.
CC       {ECO:0000256|ARBA:ARBA00010342, ECO:0000256|RuleBase:RU364112}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAE25714.1}.
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DR   EMBL; LVLJ01002295; OAE25714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VY29; -.
DR   OrthoDB; 444427at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16378; CcmH_N; 1.
DR   Gene3D; 1.10.8.640; Cytochrome C biogenesis protein; 1.
DR   InterPro; IPR005616; CcmH/CycL/Ccl2/NrfF.
DR   InterPro; IPR038297; CcmH/CycL/NrfF/Ccl2_sf.
DR   PANTHER; PTHR47601; -; 1.
DR   PANTHER; PTHR47601:SF1; CYTOCHROME C-TYPE BIOGENESIS CCMH-LIKE MITOCHONDRIAL PROTEIN; 1.
DR   Pfam; PF03918; CcmH; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364112};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364112};
KW   Membrane {ECO:0000256|RuleBase:RU364112};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364112};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364112};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Transmembrane {ECO:0000256|RuleBase:RU364112};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364112}.
FT   TRANSMEM        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364112"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   171 AA;  18914 MW;  1487540E3FBC480C CRC64;
     MAEEGPESDG SNRTKFEQRV RSAQIEARAR NISHNVRCLE CGHQAIEESQ AEIAIKLRKV
     IRDELSKGKS DKEIYHKLTT EYGETILYNP QFDAQSAVLW LLPVVTVGVV AGFTLYRGRR
     QSADVGELTR SLFHGIPLSA AEHNTLSAIV KPPHAAHSAS GLAWVRGLLS R
//
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