ID K1VVC2_TRIAC Unreviewed; 1018 AA.
AC K1VVC2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=holocytochrome-c synthase {ECO:0000256|ARBA:ARBA00012218};
DE EC=4.4.1.17 {ECO:0000256|ARBA:ARBA00012218};
GN ORFNames=A1Q2_04915 {ECO:0000313|EMBL:EKD00723.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD00723.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD00723.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00723.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC {ECO:0000256|ARBA:ARBA00007255}.
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:EKD00723.1}.
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DR EMBL; AMBO01000334; EKD00723.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VVC2; -.
DR STRING; 1220162.K1VVC2; -.
DR eggNOG; KOG3996; Eukaryota.
DR HOGENOM; CLU_296501_0_0_1; -.
DR InParanoid; K1VVC2; -.
DR OrthoDB; 36084at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004408; F:holocytochrome-c synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16495; RING_CH-C4HC3_MARCH; 1.
DR Gene3D; 1.20.58.120; BAG domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000511; Holocyt_c/c1_synthase.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12743; CYTOCHROME C1 HEME LYASE; 1.
DR PANTHER; PTHR12743:SF0; HOLOCYTOCHROME C-TYPE SYNTHASE; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF01265; Cyto_heme_lyase; 1.
DR Pfam; PF12906; RINGv; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00744; RINGv; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF63491; BAG domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS00822; CYTO_HEME_LYASE_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 242..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..229
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 171..223
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 827..888
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 958..1010
FT /note="BAG"
FT /evidence="ECO:0000259|PROSITE:PS51035"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 110570 MW; BFC3BDCCE2086F2F CRC64;
MSATYPERLE REGSHVDESR IDSELEHQLR RRNVAHAERE AADQLGEPEP GNVAASGPAA
GEYPSTGAST AHSFDTQPKN SMQEQLTPTP TVPLPDEGGQ DAALQSSTPA DGASAAALEI
NPAAQSAETG SKDTPPANAA DSTAANATAP GTAPGTTGAG VIDEEGKERS CRICFGGVDE
EGEMGRLMSP CLCSGSMRYV HVQCLAMWRA KNSKTFLECP QCKYTYVLRR GKWGDFILSS
RALSLATAAT FISMSLITGH FLLHFLLNLY QKGSHSSSAM GSTWESEDGT MVVYMGGATF
ILDLIDDSIN AFIAITAQAF DMFEGSRWVS PLMLDFILRF LLGVALLGAL SALSLLGSLR
LLAPLQLIYT ISLSGVISLD PVLSALGGSR SIIVGFVLLG VANSIVQVYD ALHACAMFGL
RFVESEIVEP TREQVTQATT PSVMKFNVGA DSTQATPAAP KTCPEGMHAK PAAAMPADHP
PVPAGMGADA CPVNDDARKV WTDVAEQASK AAPARPQRAQ LSTEREISSI PRSSHSQYTH
NSEQAALPTP EEEQTDKWVY PSEQQFFNAM LRKNHKPRQA DMRTIVPIHN AVNEKAWEDI
LMWEAGKGGD RCGGVRLTSF VGRPKERSPK AWIKTMFGYT PPFDRHDWIV DRCGTQIRYV
IDFYTGKPDP NNPQKMAFYI DARPALDDWE SIKTRLSGPA SSRPTQLSPP ARSGGQAAKA
KRWMMTVCHG SFGASESPRV HRDNYSPLYF PTQPPNLSFS AFDSIVPPLS GRAAMSQFKN
PFKRAQQEND SGQITVHVKW GRDRPHAAPT SRGLLLVADN RFNIPIPNPS LTPLSQLIGT
LSHQTGVPAS QLKLIYKGAV LKDPSLTISS YGITDGADLA LVGKEGKGPE PPAPKPQQVV
KKKNVQPETD QEDVLTDWIR GLVNGVVEPL EPAIATFVSY TNPKATNRPK QVPPFETLQR
EHARLSELLL RGLLDLDGVN IPSEWKNARQ ERKDGVKRLQ GELNKVDDSW GERKRLVA
//
