ID A0A0N1P4F2_9EURO Unreviewed; 1023 AA.
AC A0A0N1P4F2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AB675_623 {ECO:0000313|EMBL:KPI45596.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI45596.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI45596.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI45596.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) 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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:KPI45596.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFJN01000001; KPI45596.1; -; Genomic_DNA.
DR RefSeq; XP_018005559.1; XM_018146517.1.
DR AlphaFoldDB; A0A0N1P4F2; -.
DR STRING; 1664694.A0A0N1P4F2; -.
DR GeneID; 28738386; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 7..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 286..592
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 790..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1023 AA; 112797 MW; C9262A283DE6F60B CRC64;
MEASLLAGLN PAQRAAVTSK VPVLQVLAPP GSGKTKTLTS RVAHLLAHRD YNPQNVICCT
FTIKASREMR ERLRALVGEQ LESKLILGTF HSVCRRYLAA YGTKIGIAKG FGIADSSDSK
SIVKRIIKEH DIKLEPQTAR SKISWNKARF RTVASLEAEL AKSKEPAQSK QDMITVFREY
EDELKNNNLL DYDDLLLRCV DLLRAQPTCV ANVEALLIDE FQDTNIVQYE LMKLFASARN
HITIVGDPDQ SIYGFRSAEI ENLKRMQAYY RDAVVINLEE NYRSGGAILK LAQDVIDQDT
ARPDKKLKST HCHGALPVLR RLPNSFEEGL WIASEVKRII ASTGGLIGHA DIAVLIRSGY
LSSRVEKAFT NAGIPYRMVG GTRFFDRAEI RLIVDYLRTI SHPDNNAAFL AIINVPSRKI
GEKAIESLAK LSEEHKLPIF RVVQKVLAGS LVPEKKLSKP SEQDLSRLIS IINKARDKME
DMQPAQVPSR LIEYVVEVLH LQAYLQKKYK DDYEDRIENV QELIAYASDM TVMSTTETLP
TVEGIAQEQI DQCQEALDQF LANIVLSSEV EQDDKDDPKP RVTISTIHSA KGLEWPVVFI
PSVYDGSIPH SRAEDTDEER RLLYVAITRA QALLNISFPL IGSRDQGLNA HDLTPFLPES
LHYRTANKAP LFTDSIIADI ARILRRETPS PADIAQGVTS ISNSESLEDD RWPLDGRPAL
GPEQDIMTGG WIVGAGRLQP ADSSFQSTQG IASYQTTMTS SRSFSTSNTS MNAGFTTAGQ
QMRSINTMHQ GHTLQDSPAP PAPATNAPRG IQSFFSRRPS AAEAARQAWS ARPSQSAPVS
ASKGGGRSGT QPQSLSQSVS NLPTMPSISD RHGTSDPQQL LPHLSNHRLP AFNAMGRAAA
PGRVLTGQTG SVGVKRPRPL PLEELSPNRS KRVYHFLSSS PTQELFDENG EVTIGTKEDF
DTAMKVGKQN TPSCGTNSHP GGSTKDSGTE RGGPALQRPP VDPRKRQLGV RGSFVPWNER
KRK
//
