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Database: UniProt
Entry: A0A1V6V996_9EURO
LinkDB: A0A1V6V996_9EURO
Original site: A0A1V6V996_9EURO 
ID   A0A1V6V996_9EURO        Unreviewed;      1908 AA.
AC   A0A1V6V996;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQE47257.1};
GN   ORFNames=PENCOP_c001G08369 {ECO:0000313|EMBL:OQE47257.1};
OS   Penicillium coprophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE47257.1, ECO:0000313|Proteomes:UP000191500};
RN   [1] {ECO:0000313|Proteomes:UP000191500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE47257.1}.
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DR   EMBL; MDDG01000001; OQE47257.1; -; Genomic_DNA.
DR   STRING; 36646.A0A1V6V996; -.
DR   OrthoDB; 180798at2759; -.
DR   Proteomes; UP000191500; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   CDD; cd17999; DEXHc_Mot1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044972; Mot1.
DR   InterPro; IPR044078; Mot1_ATP-bd.
DR   InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   Pfam; PF12054; DUF3535; 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; SSF48371; ARM repeat; 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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000191500};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1332..1505
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1679..1830
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          184..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1908 AA;  211794 MW;  8BAF525C864B3A33 CRC64;
     MASRLDRLVT LLETGSTQLI RNTAAQQLAD VQKQHPDELF NLLGRILPYL RSKSWDTRTA
     SAKAIGLIVS NAEVYDPNED DGLQIKSAAD EDDVEIKSEV KSEEPILADD FLRLDTLDIP
     SVLKYGKRLL GGAGKEYEYS LASMEPASRL QHQKKTLTSR LGLEGEYLEE DLIEDIEMAP
     KVVTPAPKHE PNIPPVSRHS SLHEAPSRQP SSPLESATKE DGGLSKRQLN QLKRKNKQNA
     KMGANKVRVV DLSSRRQSDI LTTSAATTPH PVKAENGDDQ NGEAKPDYFS LERTEEDDDS
     KLVTEFKGAA IPERSHIQPD IVEQGGGWPL EHMCEFLTMD IFDSNWEVRH GAAMALREVI
     RVQGVAAGRL DGKSRSENDA LNRRWLDDLS CRLLCVLMLD RFGDYISDNV VAPIRETVGQ
     TLGALLSHLH PNSVRAVYRC LYRIIMQTDL GLDRPVWEVC HGGMIGLRYL VAVRKDLLVK
     DSSMMDGVLE AVMKGLADYD DDVRAVSAAT LVPIAEEFVS SRTGTLGPLM NIVWDCLSNL
     QDDLSASTGS VMDLLAKLCT FSQVLDAMKA NAADDPEASF GKLVPRLYPF LRHTITSVRS
     AVLRALMTFL KLEGEGTTDW VDGKALRLIF QNLLVERNES VLKLSGQVWS ELLNVVELRG
     SLKSEEVLSD SIQPLVTLTL GAFGVPRYPI PMNASLFIKP SGLPFSTAVP APTPSKSSPP
     ASIPGGTENK LGRRRKSEKK EKEPPPPSAH NVDGHMLSGD IDLVGADTML RSKIYAAKAL
     GELVYLWDKN DLPSLWPAIL DGLDVSASTT QLASAMVIEE YARQSGPASK YCASLCDRLR
     PILEGERPPW YADIACYLHV ARSQCHSLLN TFRDHAHVAP SRLPTLAVVV QGDSEAGPNA
     FSLADAEKIV GPDFDRLKKN LTPAQRITAT QVLNDTRTTA QSAVEEARLI REQRDMRVLA
     ATAGALVALR DIPKKPGHII KGMMDSVKKE ENVELQQRSA TAVAGLIEHY TAATKRGPVD
     KIIGNLVKYC CVDTSETPEF LHNVQLEKSI LSLRKEEDRR DHPDAAKFEK EARDARIMRR
     GAKDALEQLA VKFGAELLEK VPNLAKLVER PLRDALAGDE LPEDITDPEN ELGQEIVDGL
     STLRALLPKF DPGLHEWVID LMPIIAKGLQ CRLSVIRYAA AKCFATICSV ITVKGMTMLV
     EKVLPIINNG LDVNHRQGAI ECIYHLIHVM EDGILPYVIF LVVPVLGRMS DSDNDVRLLA
     TTSFATLVKL VPLEAGIPDP PGFSAELLEG RDRERKFMSQ MLDVRKVEPF EIPVAIKAEL
     RPYQQDGVNW LAFLNRYNLH GILCDDMGLG KTLQTICIVA SDHHMRAEEF AKSQSTDSRK
     LPSLIVCPPS LSGHWQQEVK QYAPFLSCIA YVGPPAERSR LQPLLANTDV IVTSYDVCRN
     DNDILCPINF NYCVLDEGHL IKNPKAKITS SVKKLASNHR LILSGTPIQN NVLELWSLFD
     FLMPGFLGTE KVFLDRFAKP IAASRFSKSS SKEQEAGALA IEALHKQVLP FLLRRLKEEV
     LNDLPPKIIQ NYYCDPSELQ KKLFEDFSKK EQKELADKVG SADRGDKEHI FQALQYMRRL
     CNSPALVVKE GHKQYNEVQS FLTAKRSNIR DLAHAPKLNA LKDLLVDCGI GLDHTAEGEL
     DTGASYVSPH RALVFCQMKE MLDIVQNDVL KKLLPSVQYL RLDGGVEATK RQDIVNRFNT
     DPSYDVLLLT TSVGGLGLNL TGADTVIFVE HDWNPQKDIQ AMDRAHRIGQ KKVVNVYRLI
     TRGTLEEKIL NLQRFKIDVA STVVNQQNAG LGTMDTDQLL DLFNLGETAD TAEKPSDTAG
     NEVDMVDIDG EVKEKGKKGW LDDLGELWDD RQYQEEYNLD SFLETMKN
//
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