ID K0L006_WICCF Unreviewed; 1045 AA.
AC K0L006;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Guanine nucleotide-binding protein subunit beta 2 {ECO:0000313|EMBL:CCH46723.1};
GN ORFNames=BN7_6320 {ECO:0000313|EMBL:CCH46723.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH46723.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH46723.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009173, ECO:0000256|RuleBase:RU004464}.
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:CCH46723.1}.
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DR EMBL; CAIF01000264; CCH46723.1; -; Genomic_DNA.
DR AlphaFoldDB; K0L006; -.
DR STRING; 1206466.K0L006; -.
DR eggNOG; KOG0094; Eukaryota.
DR eggNOG; KOG1687; Eukaryota.
DR HOGENOM; CLU_291902_0_0_1; -.
DR InParanoid; K0L006; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR CDD; cd01861; Rab6; 1.
DR Gene3D; 3.40.50.12280; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR01957; nuoB_fam; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU004464};
KW Iron {ECO:0000256|RuleBase:RU004464};
KW Iron-sulfur {ECO:0000256|RuleBase:RU004464};
KW Metal-binding {ECO:0000256|RuleBase:RU004464};
KW NAD {ECO:0000256|RuleBase:RU004464};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT DOMAIN 218..325
FT /note="NADH:ubiquinone oxidoreductase-like 20kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF01058"
SQ SEQUENCE 1045 AA; 117427 MW; E136146735F55540 CRC64;
MYDTFDDNYA ATIGIDFLSK TMYLDDKTVR LQLWDTAGQE RFRSLIPSYI RDSHVAVIVY
DITSKKSFEL VDKWIEDVKA ERSENVVLCL VGNKNDLADK RQVSLEDGEA KAKELSCSIF
IETSTKLGYN VKNMFKKVAK SLPEFEESKN SQPEGEIPIR SVVTKNDVTP SKLATDFPLN
SNIPKPANSM DYVLTTLDNV ADWARKSSFW PVTFGLACCA VEMMHVSTPR YDQDRLGIIF
RASPRQSDIM IVAGTLTNKM APALRQVYDQ MAEPKWVISM GSCANGGGYY HYSYSVVRGC
DRIVPVDVYV PGCPPTAEAL MYGVFRLQKK MLAAKPTRMC IMSAPLIAIT YHSSEENDQY
LHQLSAERKL KHYYLNILRT QIKELKLSNG AINGDQASQE YGSDASDDDS DVLDEDELLF
KDSSSNPNEI RAYEYNKISL LKDYPGKYIK NHKIWTPFTS PKWIDSNLVE GRDQYNQELL
KSGEPIPASE FNSESFDVFD ESKFLNYLHL PKVMGKAPLP PLIYHTTCEI DGQIYILGGA
TTLFKDNNVL DDLSNYVVDG VNLPRPLNSK LLNNPSIIPN ERLYTVSSET SLISKPKASG
DIPPPLIAMS ASKISSRHIF YYGGFELINQ VAYDADSKKI YIKKHVRLNN SGYVLDVRCL
KFRKFELIAH PNMFTRYPLT VPRFGHSSCS VNLSKHLKIE TGTGGIAATV FIMGGFRQDP
NNPSKFKPIR DLWKVELSIT YRGKHDYIIF GDNVLATPIP GPLDDNLIPA ARGFHCAEIY
DANYVHGKRA PNQTKKLHNP NRIGIARPSS PASVLSESSI SSTQKNVNGN ETLDLKLVVH
GGTDGESIFG DTWIFDFDDE SWSHVSTYFH NYDDEAQPLK TKYQCQFKRT GHGAILIDKY
IYIIGGAMPS DFNDIELDSN ENTLPDISSL LSSIKNQNDV QNVKNDHYQR LFVLNLKTQT
WSLIKYFHGI LPLIGTSGSL TSFGNVGATV TQANSKVFVI GGQIVPHHKY NNNSKEYEMN
FLNGGISIFE FPLATSLQPD LKNYL
//
