ID A0A0A2LBW0_PENIT Unreviewed; 1990 AA.
AC A0A0A2LBW0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE SubName: Full=Helicase, C-terminal {ECO:0000313|EMBL:KGO77444.1};
GN ORFNames=PITC_048170 {ECO:0000313|EMBL:KGO77444.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77444.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77444.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77444.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO77444.1}.
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DR EMBL; JQGA01000156; KGO77444.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2LBW0; -.
DR HOGENOM; CLU_000335_2_0_1; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR PhylomeDB; A0A0A2LBW0; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KGO77444.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 275..468
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 499..702
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1136..1311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1341..1535
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 149..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1990 AA; 223194 MW; 037F187F982CFFDE CRC64;
MDSIAATESQ WLSQLAAMRQ AIADLKLPKD LPHESISYGS DIDLDIDDDY SSPGTRDDVW
DIISSDDETS DDMDDLDGFD GLHLAPGSSY NRFWLEDKCQ DLAMRNSTMD AIELAQQVIA
TLAADSNDEE LQMSLAEVVG FDDLDLMGSW QGNSKHEQRX QTRAEREHAL QQRDLEHKSA
ALMPAQTRSE PSYPHVFKQH TSGNTLSASG KKYGLPLGSE QIEEPKYTEF AIPASKVGTL
GKGRKLVEIA EMDGLCRGTF KGYKALNRMQ SLLYDVAYKT NENMLICAPT GAGKTDAAML
TVLNAVGKNT SPNPLENPEA TEFTVQVDDF KIVYVAPMKA LAAEVTEKLG KRLAWLGIKV
RELTGDMQLT KREIVETQII VTTPEKWDVV TRKSTGDTEL VQKVRLLIID EVHMLHDERG
AVIESLVART QRQVESTQSL IRIVGLSATL PNYTDVADFL KVNKMAGMFF FDQSFRPVPL
EQHFIGVKGK PGSKQSRDNI DSVAYEKVRD MMERGHQVMV FVHSRKDTVM TARMLMQLAA
EEGREDLFSC HDHENYSNAL RDMKHARARE LRDLFASGFG THHAGMTRSD RNLMERMFSE
GLIKVLCCTA TLAWGVNLPA AAVVIKGTQL YNPQEGKFID LSILDVMQIF GRAGRPQFQD
TGIGFICTTH DKLSHYLSAV TAQQPIESRF SSRLVDNLNA EISLGTVTSV SEAVQWLGYS
YLYVRMKREP RNYGIEFAEL RDDPMLVQRR RQLILQAARV LQKSQMIIFN DKTEDLKAKD
VGRIASQYYV LQTSVEIFND MMRPRSGEAD VLKMISMSGE FDNIQSRDSE SKELQRLREE
VAQTEVAGGN DTPHAKTNLL LQAYISRAKI EDFALASDTG YVAQNAARIC RALFMIALNR
RWGYQCQVLL SLCKSIEKQI WPFDHPFRQF DLPQPILRNL DEKLPTSSIE SMKEMEPTEI
GQLVHNHRMG NTLSKLLDNF PTLSVETEIA PLNRDVLRIR LSIYPEFTWN DRHHGASESF
WVWVENSETS EIYHHEYFIL SRKKLYADHE LNFTIPLSDP LPSQIYIRLI SDRWLGAETV
SPVSFQHLIR PDTESVYTDL LNLQPLPISA LKNPILEEVY GQRFQFFNPM QTQIFHLLYH
TPANVLLGSP TGSGKTVAAE LAMWWAFREK PGSKVVYIAP MKALVRERVQ DWRKRLTRQM
GLKLVELTGD NTPDTRTIRD ADIIITTPEK WDGISRSWQT RDYVRKVSLV IIDEIHLLGG
DRGPILEIIV SRMNYIASQS KGSVRLMGMS TACANASDLA NWLGVKEGLY NFRHSVRPVP
LEIFIDGFPE QRGFCPLMQS MNRPTFLAIK NHSPEKPVIV FVASRRQTRL TAKDLINYCG
MEDNPRRFVR MSEDDLELNL ARVKDDALRE ALNFGIGLHH AGLVESDRQL AEELFANNKI
QVLVATSTLA WGVNLPAHLV VVKGTQFFDA KIEGYRDMDL TDVLQMLGRA GRPQFDTSGI
ARIFTQDSKK PFYKHFLHTG FPVESTLHKV LDNHLGAEVS AGTIGTQQDA LDYLTWTFFF
RRLHKNPSYY GLNISAEEQN TMAAQATAQD FMVELVGKSL NDLAESSCVL VDSATGEVDS
TPLGKIMSYY YLSHKTIRYL VSHAKRDPTF QDVLSWMCSA TEFDELPVRH NEDLINAELA
QNLPLSIDCM GDAPLWDPHT KAFLLLQAYM SRIDLPIADY VGDQTSVLDQ GIRVIQASID
VMAELGYLPA CQMLMTLLQC IKSARWPEDH PLSILPGIPT EKPPSGLPGT LVSLSSQPAG
AIAALVKKLN LPFNFTRITS QLPQLSVSVA SVSAQGIAVS LTRRNQPTTP ECKVYTPRFP
KPQTEGFFLI VCSALPNGMD GELLGLKRVS WPPVSRRNGN GKGKGNSGAG SSRGGSANDN
KGSLLTVRSN VKFPEGIFRE STSTSTARVN IRVISDSYVG MAWTVSNVEV NLDTGIETQT
VEEPIVPTKD
//
