ID A0A0N5BKY1_STREA Unreviewed; 288 AA.
AC A0A0N5BKY1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cytochrome c domain-containing protein {ECO:0000313|WBParaSite:SPAL_0000658400.1};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000658400.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000658400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602326-1};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602326-1};
CC -!- SIMILARITY: Belongs to the cytochrome c family.
CC {ECO:0000256|ARBA:ARBA00006488}.
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DR AlphaFoldDB; A0A0N5BKY1; -.
DR STRING; 174720.A0A0N5BKY1; -.
DR WBParaSite; SPAL_0000658400.1; SPAL_0000658400.1; SPAL_0000658400.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR PANTHER; PTHR10266; CYTOCHROME C1; 1.
DR PANTHER; PTHR10266:SF3; CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF81496; Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602326-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602326-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602326-1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 241..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..231
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 105..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 78
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 79
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
FT BINDING 197
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602326-1"
SQ SEQUENCE 288 AA; 31844 MW; 41551EE08AC28646 CRC64;
MQRAISSGMF KNVALGLGAV GAAGVGGLVY ALENSIQAGE NVVHPYKLPW PHAGLFDTFD
YASVRRGYEV YKQVCAACHS MKYLHYRQFV DTFMTEEEAK AEAAEATIHD KDDRGQPITR
PGVLNDTLPD PYPNKKAAAA ANNGAAPPDL SLMSLARHGG DDYIFALLTS YFDAPAGVKV
DEGKAYNPYF PGGVISMPQQ LYDEGIEYKD GTFASQSQQA KDVSAFLHWA AEPYHDNRKM
WALKIATLIP FLAIVLVYSK RHMWSFVKTQ KFAWRTIKGR EPPKPKSS
//
