ID A8N7Y5_COPC7 Unreviewed; 747 AA.
AC A8N7Y5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Mitochondrial chaperone BCS1 {ECO:0000313|EMBL:EAU91005.2};
GN ORFNames=CC1G_02392 {ECO:0000313|EMBL:EAU91005.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU91005.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU91005.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
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:EAU91005.2}.
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DR EMBL; AACS02000003; EAU91005.2; -; Genomic_DNA.
DR RefSeq; XP_001830941.2; XM_001830889.2.
DR AlphaFoldDB; A8N7Y5; -.
DR STRING; 240176.A8N7Y5; -.
DR GeneID; 6007394; -.
DR KEGG; cci:CC1G_02392; -.
DR VEuPathDB; FungiDB:CC1G_02392; -.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_3_0_1; -.
DR InParanoid; A8N7Y5; -.
DR OMA; VWIEFRN; -.
DR OrthoDB; 404208at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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 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; BCS1 AAA-TYPE ATPASE; 1.
DR PANTHER; PTHR23070:SF232; MITOCHONDRIAL CHAPERONE BCS1; 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 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:UP000001861}.
FT DOMAIN 1..168
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 199..382
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 83744 MW; 29B8CF3FF8D87178 CRC64;
MLWLSRRPEW QRSREFETTI RSGSTSTSST FGSPADQEWD EAEREWEAYN AHFERGYSHH
GQDGEDDTDP IEKPKTRIVF QPTYDTTHTI FFRGHWLRVR RSRKHDTNSE MISISVIARS
NNILKQLVLQ AKKEYEAECV HRIQIYFADA HGSWRWTDSR AKRPLSSIVL NPGVKEMLVD
DAKDFLRSEK WYADRGIPFR RGYLLYGVPG SGKSSLIHAL AGYLQLDIYV VSLSASWISD
STLTSLMGRV PARCVVLLED LDAAFTRSVS RDDEEEILGS SNNNNNNGNN GGNNNNAEGP
QEQQSGFSSF YGSGRRRGGR SGRSGEYLSD VNTLSLSGLL NALDGVAASE GRLLFATTNH
LDKLDEALRR PGRMDVWIEF KNASKWQAEA LFRNFFPACD EDEVEDVDSD GALSAGELEA
RRRDAREAQK RREREVDEAL KNIKVESRMF TPNPPVPTTG VPSSPSTSSV WSIASSASNL
LSSASSLSLP FGSSSGSSTP SVSPASSTSA SRKTSSASSS IASAAAAVSS SRPHVKKFGE
GNTAYIAPPP TDDIASRRHS AAPLDKKTLA VLAKKFADGV PEEEFSVAGL QGYLLKHKSN
PHLAASNIES WVASERALRV KLAQEKAARE EREKQLREKR RQELLLKREE KKKQEEKEAE
MEKIKAKLAE KEKEEELEKM RQKLREKEEE ARKKEREERE GKSGDSAEEK KEEEKVEEKK
EEHKTEEEKK SDSDDDEDKE NWSDALP
//
