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Database: UniProt
Entry: A0A1Q9NKA2_9ARCH
LinkDB: A0A1Q9NKA2_9ARCH
Original site: A0A1Q9NKA2_9ARCH 
ID   A0A1Q9NKA2_9ARCH        Unreviewed;       248 AA.
AC   A0A1Q9NKA2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Heme exporter protein C {ECO:0000313|EMBL:OLS22462.1};
GN   Name=ccmC {ECO:0000313|EMBL:OLS22462.1};
GN   ORFNames=HeimC3_30950 {ECO:0000313|EMBL:OLS22462.1};
OS   Candidatus Heimdallarchaeota archaeon LC_3.
OC   Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX   NCBI_TaxID=1841598 {ECO:0000313|EMBL:OLS22462.1, ECO:0000313|Proteomes:UP000186063};
RN   [1] {ECO:0000313|EMBL:OLS22462.1, ECO:0000313|Proteomes:UP000186063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC_3 {ECO:0000313|EMBL:OLS22462.1};
RX   PubMed=28077874; DOI=10.1038/nature21031;
RA   Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA   Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA   Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA   Baker B.J., Spang A., Ettema T.J.G.;
RT   "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL   Nature 541:353-358(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CcmC/CycZ/HelC family.
CC       {ECO:0000256|ARBA:ARBA00005840}.
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:OLS22462.1}.
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DR   EMBL; MDVS01000051; OLS22462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9NKA2; -.
DR   Proteomes; UP000186063; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0015232; F:heme transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR   InterPro; IPR002541; Cyt_c_assembly.
DR   InterPro; IPR003557; Cyt_c_biogenesis_CcmC.
DR   InterPro; IPR045062; Cyt_c_biogenesis_CcsA/CcmC.
DR   PANTHER; PTHR30071:SF17; CYTOCHROME C ASSEMBLY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30071; HEME EXPORTER PROTEIN C; 1.
DR   Pfam; PF01578; Cytochrom_C_asm; 1.
DR   PRINTS; PR01386; CCMCBIOGNSIS.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..188
FT                   /note="Cytochrome c assembly protein"
FT                   /evidence="ECO:0000259|Pfam:PF01578"
SQ   SEQUENCE   248 AA;  27953 MW;  D402160C54CE7EC6 CRC64;
     MKDEKKIYNL GLLKSPERRF FLLIGLGSII LILAFFNMYF LTEAFPSGPD CLSVPGQECF
     NVSGHPVFYM ISEAFIAFSL FAIASIGSIL FLVKKDLKYD SIVVASAKTG ILATSLTLLV
     GMIWSKVEWG YYWQWEQRQT MTLVMFIFYV GMILFRSTID DANDKAKLTA VFGLIAFPTV
     PMTNFIVGGL HPQPQESLSA GGNAFMGAIF MYIGTFLIYL AFLYMSVLLE EVNNKIEEYK
     YLVLAEQE
//
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