ID A0A1Q5U7U5_9EURO Unreviewed; 1496 AA.
AC A0A1Q5U7U5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ATP-dependent helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSUB_5549 {ECO:0000313|EMBL:OKP08562.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP08562.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP08562.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP08562.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OKP08562.1}.
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DR EMBL; MNBE01000567; OKP08562.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5U7U5; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000186955; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 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 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00487; DEXDc; 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 4: Predicted;
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:UP000186955};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 348..546
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1151..1189
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1255..1407
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 757..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1496 AA; 170337 MW; 657E22A7A5D27897 CRC64;
MGVVAEYTDI PGVIPETLIS AFAQNDTLDV DGRPSKRRKV TKSGPYNLSD ELGVSSTGIP
LGYIPLTRLS LRLDYPEAYR FNDKTPNKLS YLSRRIPVLV EIQNTSSRSD ATVTLDRPDV
EYVSHKLVIT TTDAEKKDII SCVVNDLRLV GFLEQLRHVT QLTAADRCYN RLPTACYQAT
VQLLTETKSL IVEIVGLWRD SLETPSLNHL PDPALELFGK YVLQEDHVTA LEYAPHGRRE
KLLGHHRQWL PREFYESVHV PQDTESASAN IKCDDLECEL FPFQRRAVRW LLWREGTQIK
EDGTIATIDR PLPNGLPASF KEIQDADGNV CYFSHLFMTI TTKISQWGDA ANLLRGGILA
EEMGLGKTVE MITLMCLNRR PAQETLKPDP DGLRVSGATL IITPPAILEQ WKQEIEQHAP
KLKVHHYTGI RRGQEKSDDL MIEEIADFDV VLTTYNVISR EIHYAGATPS RSLRHEKRFE
TRKTPLVRIS WWRVCLDEAQ MIESGVSNAA KVARLIPRQN AWAVTGTPLR KNIDDLFGLL
LFLQYRPFCD SSSLWKRLYS RFGPVLVSII NSIALRHTKD KIRDELRLPP QKRIVITTPF
TPIEEQHYGQ LFEEMCEQCG LDAFGAPLED DWNPEDPGTV EKMRTWLTRL RQTCLHPEVS
GSNRRALGAS NGPLRTVDEV LEVMIETTDT SIRTEERTVL LSQLRRGQLL ENAKRKKESL
TLWQAALDRA TELVNDSRAQ LQLQRLKNKG VALNGVTTIP QTPDYTTDDE NDEEEVDKNS
RIGQCRLKLR AALEVQHIAV FFTANAYYQI KSDPTLTQPD SEHFKALEKK EEEGYEAAKL
IRKEMLIDIS RKVERYMRAI KEKARKKEFV HIPTMKPYLY SRGLESYRIL NKFEDLCNAL
NKHAEQYNQW REVMIGLVSQ SLIDQEEDAE LEGNEYERST KHQDEMYVYM EALRTMYADR
HDALTGQKNI LISHEAKAGI AQAKKGEGPS PELFLSIMNT RSELMPDPNL GSLRGIVSEL
RSLVGSLDWQ ASGGSSRASA ELEMVTLVLK NAGRMIAEQL KISSNLEREV EMFRDTMNNR
LEYYRHLQQI SDTVAPYDEE NAGKPMDEKL FASKLKQEEK IEAKISSLKS KRRYLIHLRD
DPGEEDTSRI CIICQSSFEN GVLTVCGHKY CADCLRLWWR QHRTCPMCKK PLKFNDFHQI
TYKPQELVAQ EEETPFKFDH ERQSNNAIYS DISSGVLKQI ETIELDGSFG TKVDTLARHI
IWLREHDPGS KAIVFSQYRN FLVVLKRAFD RFGIVNSSVD APDGIEKFKK DPGIECFLLH
GKAQSSGLTL INATHVFLCE PLINTAIELQ AIARVHRIGQ SRPTTVWMYL VSGTVEESIY
ELSVNRRLAH IMEKEKKEKN SRFINPSDGD ESLIEDITET AIESANSMEL EDATLNSLMT
SGAAGGEMVK KDDLWQCLFG ATAGKDDHGL SSDAEREVGR FLRGEAAEQR REEAMI
//
