ID F8Q4L2_SERL3 Unreviewed; 650 AA.
AC F8Q4L2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SERLA73DRAFT_111855 {ECO:0000313|EMBL:EGN97067.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(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}.
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; GL945483; EGN97067.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q4L2; -.
DR STRING; 936435.F8Q4L2; -.
DR HOGENOM; CLU_010189_3_1_1; -.
DR InParanoid; F8Q4L2; -.
DR OMA; YLMFWMA; -.
DR OrthoDB; 404208at2759; -.
DR Proteomes; UP000008063; 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; 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.
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:UP000008063}.
FT DOMAIN 25..218
FT /note="BCS1 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01024"
FT DOMAIN 249..394
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 72154 MW; 2D8944B54799E3BD CRC64;
MEALKSMLSP LGMNTNAIQD TLKLVVIGGT VETARRASVS AWNGFVDSFF LTAHFSQEDY
PYDWLMHWLS KQPAWGRSRE FEITTRTVGR SGITQTTTGD LEEEDDVEED DDSDALVHGR
RKRKVAFMPS LDTTHTIYYR GHWLRITRTK RYPDYGHGAA LKISVVARNN DILKKLVLEA
KREYEKDAEH RVHIFMADTT YGCWRWNGAR QKRPMSSIVL QPGVKDMLLA DCKDFLCSED
WYAERGIPFR RGYLLHGVPG SGKTSLIHSL AGELGLDIYV VSLSSKGMSD NTLTTLMGHV
PSRCILLLED LDAAFTRSVS RDSSSTGAPT AASSTTNPAE TNDGSTLSLS GLLNSLDGVA
AAEGRLLFAT TNHIERLDPA LSRPGRMDVW VNFTHATKWQ AEGIFKCFFP SKPSAPATPL
PSVSVQKEGK DVDASQKNLP LPKRKTPTHA IPLLTEEEIS ALAKRFAEAI PENELSVASL
QGYLLKNKTR PRECVEEVDE WIIQERETRE KLKKEKAERE AKEKKEAEER ERKEQEEKEA
KERADRKEAR AKAKKALRTE TALKLDVSSN SSSGANTPVL PEGVQASLSE SSSNSESDSS
GGIEADTEES VTSEEENDKS ADENVVREGA AKEAVKEKWV SVKGQTAQDS
//
