ID B2A9Y1_PODAN Unreviewed; 509 AA.
AC B2A9Y1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Mitochondrial chaperone {ECO:0000313|EMBL:CDP22534.1};
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 1, supercontig 1 {ECO:0000313|EMBL:CAP59892.1};
GN ORFNames=PODANS_1_2170 {ECO:0000313|EMBL:CAP59892.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP59892.1};
RN [1] {ECO:0000313|EMBL:CAP59892.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP59892.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP59892.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP59892.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP22534.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007448}.
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DR EMBL; CU633438; CAP59892.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP22534.1; -; Genomic_DNA.
DR RefSeq; XP_001912411.1; XM_001912376.1.
DR AlphaFoldDB; B2A9Y1; -.
DR STRING; 515849.B2A9Y1; -.
DR GeneID; 6196815; -.
DR KEGG; pan:PODANSg09459; -.
DR VEuPathDB; FungiDB:PODANS_1_2170; -.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_6_2_1; -.
DR OrthoDB; 664379at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR PANTHER; PTHR23070:SF232; MITOCHONDRIAL CHAPERONE BCS1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08740; BCS1_N; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01024; BCS1_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 66..251
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 282..414
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 55533 MW; CC102112329EFE91 CRC64;
MPAPNSQMPP AAGLPFPPSP QSAQSPPPYS PSAPPSTSPS TAAAPSFLPL DQLFTNPVFA
GGLGLASLGA AAAFGRRALI QGTALLRRQL LVNIEISKRD PSYSWVLAWL AQPRDNSGFI
AQRLTRLRSL SVTTTTKSLS KVAGEEGNGR THADFRVQPG FGHHIVRHKP GVYIAVNREK
ASTATTATGE PHETLTLTLL WMHRHVLAEV FTQAHELAQS FQQGKTVVYT ARNMQWTVLG
KPRLKRPLGS VILDEGVKES LVADVKEFMA AQEWYTERGV PYRRGYLLYG PPGTGKTSFI
QALAGELDYS VAMINLSEMG MTDDLLAQLL TQLPEKSILL LEDVDAALVN RRQRDPDGYS
GRSVTASGLL NALDGLAAGE DRIAFLTTNH IDKLDPALIR PGRVDMMVRI GEASRYQAGQ
MWDRYYGDVD TDHKGRERFL ERLDGLGLFG GDQKDPAVPK RHTSTAAIQG LFQFHKGDME
GAIKMAEHLI PRTYEPEPPT VEGSIKSPA
//
