ID S8AYD9_PENO1 Unreviewed; 1136 AA.
AC S8AYD9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS26992.1};
GN ORFNames=PDE_01933 {ECO:0000313|EMBL:EPS26992.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26992.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26992.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB644409; EPS26992.1; -; Genomic_DNA.
DR AlphaFoldDB; S8AYD9; -.
DR STRING; 933388.S8AYD9; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; S8AYD9; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 598..765
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 952..1126
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 125567 MW; 5385F1E8438489DF CRC64;
MTDTVPDTPT RMKKPEPGTS DDEGDHETIA TLPAHTTTPS QRLTQATQLV DLPYSRQNNP
TVQVAASSPI ASASSPPPQR PRGGLLSSLM APSGTSFRPP VTTVRPTKRT PTFNMDDGPT
YRGGSSDDDE NRIDIKPVMF EKTSRSPEKI AESPIRNGAG SMDRFKEITS SAFYDPSSAG
IKRSADQMSP SGAPRGVATK KIRQTGPSRA QPVNAPISTL LDIADFRVKV KVERILKILP
TKSVQECVDA LMSANGNFDL ALDLLGDESS KANGIGARDS VIEIESSEDE LNAQPNRDVG
HIAKQKIKAR GTIQDKWAAT KGHITSQKED DGKPRGRLMR GPRSRDPTAP IDTITIDSDG
SPPKKKASRL QKGPRRAPSL TPEAVLSDSE DSDVVEEDVN AGDLEQKVLR FFNTCKPHDL
ADIAAVPEET AELITSQQPF GSLGEVREVT APVDENAKPK GKGKGRKAPK PIGDKIVDKC
LEMWTGYLAI DALVAECEAL GKPVAEEMKK WGVDVFGKRG DAELDLATLG GSHDSGIATP
SSTHPSPAAD DSEDEIRPVA KSRKTQSNDQ SGFISQPSIM AKNLVMKDYQ IVGLNWLALL
FEKKMSCILA DDMGLGKTCQ VISFLSHLYE KGVKGPHLVV VPSSTIENWL REFSTFSPEL
QVRPYYANQN ERAFIREQLE SDRDEINVVV TTYTIAKAKV DAKFLRDMDF CVCVFDEGHM
LKNSQSLLYE KLIRINAEFR LLLTGTPLQN NLQELASLLG FILPGVFKDH KDDLQAVFAN
KARTSDESHA ALLSAQRIER AKSMLKPFVL RRKKYQVIDL PAKHSFVEYC EMKTSQRDIY
DHEKEQVRQL LEDRAAGKKT GSKSANILMK LRQAAIHPLL ARRHYTDAIL KKMAKSCLKE
DKWAASDPAI IEEELQAYND FECHHMCLEN PSSLGRYKLK NEEWMDSGKV EKLRELLTRF
IANGDRTLIF SQFTMVMDIL ENVLETLKIE FVRLDGRTNV EDRQSILDAF HERVEIPVFL
LSTKAGGAGI NLACANKVVI FDSSFNPQED VQAENRAHRV GQTRDVEVFR FVTRDTIEEQ
IYALGQTKLA LDQAVAGDDD SAASKKSEEI GMKAVENMVL ADMEKQDGHN AQSKAD
//
