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Database: UniProt
Entry: A0A060SH92_PYCCI
LinkDB: A0A060SH92_PYCCI
Original site: A0A060SH92_PYCCI 
ID   A0A060SH92_PYCCI        Unreviewed;      1060 AA.
AC   A0A060SH92;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=BN946_scf185014.g46 {ECO:0000313|EMBL:CDO73576.1};
OS   Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO73576.1, ECO:0000313|Proteomes:UP000029665};
RN   [1] {ECO:0000313|EMBL:CDO73576.1, ECO:0000313|Proteomes:UP000029665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM137 {ECO:0000313|EMBL:CDO73576.1,
RC   ECO:0000313|Proteomes:UP000029665};
RA   Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA   Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA   Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA   Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA   Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA   Pontarotti P., Henrissat B., Record E.;
RT   "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT   basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT   breakdown.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
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:CDO73576.1}.
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DR   EMBL; CCBP010000122; CDO73576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060SH92; -.
DR   STRING; 5643.A0A060SH92; -.
DR   HOGENOM; CLU_000335_0_4_1; -.
DR   OMA; LEMIACA; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000029665; Unassembled WGS sequence.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001650; Helicase_C.
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; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR   PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029665}.
FT   DOMAIN          79..266
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          695..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..894
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..913
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  118453 MW;  70F70470FC4CDF93 CRC64;
     MKLRGSTVRF LVISATVPNI MDVADWVGNR ANNGPALVKE FGEEYRPCKL SRFVYSVPRR
     RDANDFIFAK ALDFKLYGVL QQHCNNKPVL VFCPTRKGVM SAAELIHKEY EEAIAKKQTL
     PWSKPPHIEH SFSNKQLDKL AACGIGVHHA GIVREDRTAT EQLYLKKALK VLFATSTLAV
     GVNLPAHTVI IKGVKLFQNG ASQEYSDLDV MQMIGRAGRP QFDKEGVAII MCEQDLEVKY
     KALAQGQTIL ESSLHLHLPE HLNSEIALGT IKDMVSAKEW LHNSFLFRRI QKNPLHYDIR
     KEGNKSWEQR MDDLVADSVK TLKDTDLVTH EGEDDRLSST EYGDIMSKFY IRQATMVTIL
     KLPDTASVRE ILEAISCADE FSDIKFRAGE KQVYNKLRIH QDIRYTLKKI EKPSDKVFIL
     IQAILGAINL ADPEYRTGES QPYTESLPIL RHISRIARDQ LPQYTIAISE EEVSVREDGV
     EVELLIECGL AQNTKVQKSK KPKKQRRWDM TMMLTLTSDN TFIDFRRIST VALRESRTFS
     VTAKLTKPSQ AVIVYATSAW TQQASLSWIP VRRTHWCIIL VPPHLIDADE LEKARDLEGL
     EDIADFWDMS PDEDATPGGA TRLSKDAALD QDGTPQFTSN RGVMSAPKQL QNGNYECNHT
     CKEKARCRHL CCREGLAKPP PMTKKRIEML IAAADKSPRK QDGEGQDHTV AQPGIDAQDA
     RSKPKPRMKE PHKPVAVDAN RSLKKLEALH ERMGVEKSLQ LAEGIRIKLN TEYPSYSQQP
     FRKSKPEFDV EYSTLQNGSS VANSGVSVVL SDSDDDLPEP GGVFSSVPKI TTGLKSSPDS
     TDYADPDFDA LIAGLPVCEA GHTSNAVGRR ATPTNTRFSM SNDDRLSSTT DWLPDTPSRK
     RKTEHDGSRP YKRQKNDVAA SPSQDAVSLD RGSTLGEPLF EQALSDDMHS LFETRGSRSS
     ASSVAPALVD DGDSFVLDTS LFDIMPSTPT WTERNRDEHS KADSQVALGH HASTETRFVK
     THLNISRSPK PTDPEPEEVD DPLAELEAWL QSGAVEIGEE
//
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