ID A0A135LLB0_PENPA Unreviewed; 948 AA.
AC A0A135LLB0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Zinc finger, RING-type {ECO:0000313|EMBL:KXG49773.1};
GN ORFNames=PGRI_057410 {ECO:0000313|EMBL:KXG49773.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG49773.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG49773.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG49773.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:KXG49773.1}.
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DR EMBL; LHQR01000048; KXG49773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LLB0; -.
DR STRING; 5078.A0A135LLB0; -.
DR OMA; ETTVWRL; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000070168; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16509; RING-HC_HLTF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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 InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 379..552
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 706..744
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 777..944
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 105128 MW; 75B7C27ACB026AF7 CRC64;
MAGKRKSNVD PDEDVLYAQS GRAPKSTRTA PTLNTETTSS GQRFGETVDY ISLDQDTSSG
QRFGESAEFI PLNQLSQVAG ADEDDEAALD VIQGSQDVDG TSLTSSILYG VISTKIVGVR
FYRGRANPGE RVIIHRDANN QYDSNAIKVE NVMGAQIGHI PRQMAAKLAA YMDGRDLIIE
GTLTGAIGDF TCPMDLKLFG SRDPIKRSNL KQRMQKDKLP VRQLNELERE ERKAEKEAEK
QQKEAAKKAR AMALGKAAAQ WQANQNSEYA NLSTPTGLDG EQNESLEELL NQSSTFNPRD
IGQVVETFGQ KESDLINMPM VDTPAGLSTQ LLPYQRQGLV WMIKQESPSL PTRGTDDIVQ
LWKRKGNDFL NVATNYVTAT EPALASGGIL ADDMGLGKTI QIISLILANA KPLTADSSKT
TLIIAPVGVM SNWRNQIQDH AHKETAPSVL IYHGSGKKEA ANLAKYDVVI TSYGALALDF
NLNARQTPAK GIFSLHWRRV VLDEGHIIRN PSSKASLAAC GLRADSRWTL TGTPIINTLK
DLYAQIRFLK FSGGLEDLGM FNSVLIRPLT AGEPEARLLL EALMGTICLR RRKDMSFINL
KLPEMTSRII RIKFNAHEKE KYSAFQTEAQ GALLDFKDKD GKTKYSHLLE VLLRLRQVCN
HWALCKNRID KLMGMLEEHK VVPLTPENVR ALQEMLQLHI ESQEQCAICL DNLEQPVITA
CAHSYCRGCI EQVIERQHKC PLCRADINET NTLVSPAVEL GEDTDTVEAD PDSPSSKIET
LVKILTAQGQ APGTKTVVFS QWTSFLNLIE PHLKQRGVKF ARVDGKMQSV KRDISINTFS
NDPECTVLLA SLSVCSVGLN LVAANQVILC DSWWAPAIED QAVDRVYRLG QKRETTVWRL
VMEDSIEERV LAIQERKRSL MLAAFRETAK KKAEDRGTRV ADLEALLQ
//
