ID C9STH4_VERA1 Unreviewed; 649 AA.
AC C9STH4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Mitochondrial chaperone BCS1 {ECO:0000313|EMBL:EEY22089.1};
GN ORFNames=VDBG_08199 {ECO:0000313|EMBL:EEY22089.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985224; EEY22089.1; -; Genomic_DNA.
DR RefSeq; XP_003001940.1; XM_003001894.1.
DR AlphaFoldDB; C9STH4; -.
DR STRING; 526221.C9STH4; -.
DR GeneID; 9536923; -.
DR KEGG; val:VDBG_08199; -.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_4_1_1; -.
DR OMA; YLMFWMA; -.
DR OrthoDB; 819832at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF87; ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14760)-RELATED; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 2.
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.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 61..263
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 298..458
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 563..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 72432 MW; 5B287B093D2818F8 CRC64;
MDTLSHSSCT TAATEASSFD APQAQPSQAI LDFFFPGFSI LTSACQKYFS IDLNVYIPLI
ILCGGATFAW QYLSDYVWGL IESHLMSSVD VRTDDEIYNI LMAWVATQRF AKRSRRFIAN
TNLNSRAWFL MRWSYDEDEE DEDEDDSTAT AASEVGHKKK GLAYTPSFGN HIFWYKGRLL
RFKRSQNQQQ GSYLTVSERE EISISCFGRS PWILKQLLLE ARLEYLKKDT KKTMIYRGGI
RAGSTDPTWQ RCMARTSRPF STVILNEKTK KELIDDVSDY LSPATRNWYS NRGIPWRRGY
LYEGPPGCGK SSLALALAGY FKLRIYIVSL SSIVANEETL ATLFSDLPRR CVVLLEDIDT
AGLTHTREVS DVLSGEADKS DASANAMVPG QLTTGILSAA ATSSSSRLSL SGLLNILDGV
ASQEGRVLIM TTNHVEKLDK ALIRPGRVDM IVKFSQADAE IIGAIFRAIY APLEGDDGAD
RDAPGLDADA EKAAAEAAAA RVAKTVAHVE ALSHEFVACI PAHEFSPAEI QGFLMRHKRS
PDAAIEHAAQ WVIDTRKQKK EKEIKAAEER RAQEEKEKEK EKEKEKEKEK EKEKEKEKEK
EKEKEKEKEK EKETTSDGKE AAPGQTKTAR DEHLQGPGSD SGYATSVES
//
