ID A3LQM4_PICST Unreviewed; 445 AA.
AC A3LQM4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Ubiquinol-cytochrome c reductase core subunit 1 {ECO:0000313|EMBL:ABN65227.1};
DE EC=1.10.2.2 {ECO:0000313|EMBL:ABN65227.1};
GN Name=COR1 {ECO:0000313|EMBL:ABN65227.1};
GN ORFNames=PICST_81500 {ECO:0000313|EMBL:ABN65227.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65227.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65227.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000496; ABN65227.1; -; Genomic_DNA.
DR RefSeq; XP_001383256.1; XM_001383219.1.
DR AlphaFoldDB; A3LQM4; -.
DR STRING; 322104.A3LQM4; -.
DR GeneID; 4837554; -.
DR KEGG; pic:PICST_81500; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; A3LQM4; -.
DR OMA; PYNNGVS; -.
DR OrthoDB; 1358314at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF126; CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABN65227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT DOMAIN 38..173
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 182..359
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 445 AA; 47293 MW; E7BF2C75FDD4A573 CRC64;
MIRGSALRTS AKSLTARRLL STANGQTKYT TLSNGVTIAS ETNTNAATAT VGLYYGAGSR
SEHPYNNGVS ALTASILGSG LQDGVLLSSE STKETNGILA TTTNANIASA GKLIAQIASN
PVQILEKSDF AAAKNKLAAA ADAVEADPNA KVLEHLNASA FQGYSLGLPT LGTSESVQDL
ELQDAVRSLE KHLVASNTVI AAAGNFDHEA LVAAVEANLT LTQGLKPQEK PASFLGSEVR
MRDDTLPKAY VAIAAQGEAF NSPAYYVAKV AAAIFGDFDH HSAFAAYTSP KLASIVQEYH
IADKYTHFST SYSDTGLWGF ASEISNIEAI DDFTHFTLKE WNRLSVSISN AEVARGKAAV
KTALLRQLNS TPAVVSDIAT KVLLAGYRSS VKEALEKIDA IQTKDVKAWA QATLWDKDIV
ISGTGQIEDL LDYNRNRNEM AALRW
//
