ID M5FXH9_DACPD Unreviewed; 551 AA.
AC M5FXH9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Transitional endoplasmic reticulum ATPase {ECO:0000313|EMBL:EJU00500.1};
GN ORFNames=DACRYDRAFT_80702 {ECO:0000313|EMBL:EJU00500.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU00500.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU00500.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU00500.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; JH795866; EJU00500.1; -; Genomic_DNA.
DR AlphaFoldDB; M5FXH9; -.
DR STRING; 1858805.M5FXH9; -.
DR HOGENOM; CLU_000688_8_3_1; -.
DR OMA; DRHIYVA; -.
DR OrthoDB; 24013at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19503; RecA-like_CDC48_NLV2_r1-like; 1.
DR CDD; cd19511; RecA-like_CDC48_r2-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT DOMAIN 44..185
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 318..456
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 551 AA; 59966 MW; D3D1E8FFFD434D46 CRC64;
MDHDEEMNAF ASVGGLDRQI AEIRNLIELP LQRPDLFRRF GIKPPRGVLL HGPPGTGKTR
LAHAIATSTR SSLILIHGPE LSSAYHGETE AALRQVFQKA RKQSPCVIVL DELDALCPKR
EEGSGEVEKR VVATLLTLMD GMADEDEKEG GRVIVVGTTN RVNTIDPALR RPGRFDREIE
IGIPDATARL AILHVLLARI PHSLDDDTLK PLADRTHGYV GADLAALVRD AGTLAIHRWL
DASKLTAAPK MTAELTNADL LNALPGTRPS AMREVFIETP SVRWSDIGGQ QSVKEKLKEC
VEWPLLYPKT FERLGVTPPK GVLLYGPPGC SKTLTAKALA TESGINFLAV KGPELLNKYV
GESERAIREI FRKARAAAPS IIFFDEIDAL GSMRTSGDNA GGAHEGMLTT LLNEMDGIQE
LVGVTIVAAT NRPDVIDSAL MRPGRLDRIL YVGPPDLEAR MEILKIRTAK MAVEPGIDFH
DLAVKTTGCS GAEIAALCQE AALAAMKENI DAAFVGIRHF RESIDTARRG ITPEVVERFK
IWSETSGVRH A
//
