ID A0A061H1V3_9BASI Unreviewed; 2489 AA.
AC A0A061H1V3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|SMART:SM00487};
GN ORFNames=PFL1_06001 {ECO:0000313|EMBL:EPQ26353.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26353.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ26353.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26353.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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DR EMBL; KE361645; EPQ26353.1; -; Genomic_DNA.
DR RefSeq; XP_007881730.1; XM_007883539.1.
DR GeneID; 19320081; -.
DR KEGG; pfp:PFL1_06001; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000796_0_0_1; -.
DR OrthoDB; 103295at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45626:SF26; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G09120)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 2.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1397..1763
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2407..2489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2435..2451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2489 AA; 273392 MW; 3F57D4DFD03B3ED1 CRC64;
MPAPRRASRV SYVSLITSSS DDDGDRQQEQ HVGTRSRRAS KASSKPPVKK RRIKDDDSES
DGFVPSSALS ESESQDEHDE DVDDDDDDDA AYRDGRTRRA ASESDDTPSI EADNGGDATD
DSSTPPETPA NGDSTASGYF AGKEPFVDLT NAATAKGKGK GKVKDASVST PASAKLAGFR
SLFSTPMSSN AGSSRKRQAT LSDMFGAKSK PTPTPTKAAP KAGSRLKREA DDGDDDAELL
DLDDFSDDSD DMPSVRKKPK KSKAAKPASK VILSQSSSKG WKSSFAHKRR FIRMGFVPTP
EAVRHNLAKA SSTLSDGKFP PIHDLHDIFS DMVSRAPGVL ELARALQNRP LRVATMCSGT
ESPLLALELM TRAIKEQHGI QIKVEHVFSC EIEPFKQAYI ERNFSPPILF RDVTELGGDR
AHTAYGALVD VPGNVDILIA GTSCVDYSHL NNKKKGLNDG GESGRTFHGM LDWVKRHRPA
LVVLENVKNA PWVGVAETIV AEAGYDVSFS NTFDTKNYYI PHTRQRGYLL ATRNTTDCLP
ENWDLLVSWL VRPASSPFDA FLLPSDDPRI QKVRQQFAHG EGLSKGRSTI DWSKCQSRHE
RARDEEELGK TRPLTAWEEG GTCKMSHDGW NEWAVRQPER VTDLLDITTL RFAALDQDPM
YKSKIWELSQ NVDRNVAASR PGIAPCLTPS GIPFIPIRGA PMIGLEALSL QGLPLDELLL
TRETDDQLQD LAGNAMSSTV VGACVLSALL VARGDFEREQ IEGGRPSLPW GSSCNERDAV
VRSSDVVVDL VAEGGDAIAG VDSLESRTLD LTSSERVAMP SLLKDAVDSS QLCICEGRTL
TTDRPIYRCT SCDHTACESC KGRPVHDFEL DARPRTQPDE FGERLKRALP MRLQADAFAL
DDITTLARQR PSVEMVFALL WSQRVSEVLG GAEFRFQELL RQKVWQARFV APGARLDLIL
DPIAPHWRIF VDARPEEPAG SHLRAALMQP VARMALDPLA TDVDLFHGSW EICVPTGNTV
SITLTSSGDH VPTWQSALGL GGKFADTKRF AEIHVKVPEE AKAQLDCDIE GVYDLMPQCG
TANASLHARR GDRDGAGDGR KLYLFIDADR YKDASGDRFV FSTDIGRLPY PLQRPAVGRL
PEGWKPKLPK VHQRDAVEQV KLQIDGTWIT APALKVKPGV SLDGQINIAT TPVELDLRQK
GCERALAVLE CSAPVPRAEH NRIWPINGAW GQVDLLHKTN TTFGHLAWLV ERVPDVSAFD
DWMPAKHGAL SLATAACKRC APAEPDIQWL AMPGRPVVPI ENTQQAGPYE QALKNRPAPF
VMHLRLSDGL AQTRFGINAA TLMHRALSRL PSNPHAGLVE LSWRLTKLDK SLNMFSLPRY
TIKSNRQDAE SPSPDIFALE LRKEQKRSLT WMLAQERKDV EPFHEEEISE GLLAPFGWRA
EGRATRPVTV RGGVLADAVG YGKTAISLAL IAASPDRDRL PELPEGDEDA LIPTKATLVI
VPGHLCKQWQ REVAKFCGNS LSVRVVTSKN ELNKLTVRDV LKADIIIMSV TVYRSDTYWE
TLARVSAANP LPNRPGRFFN AALKRSLAAL RNRVKELTSE DGVRQLAQSI KKRVDFDNSH
MTSHRARGRL IGQAYADAHG GGAKVKNEEK GADKGLHKDL QPKSKAEPDP WNLASPVVRR
DWKEMTCPPL EMFLWNRVVV DEFHYIAEAA DRTLAGVTSL QARAKWILSG TPPTADFSDV
KSIAVFLNLH LGVDDDADTI KDSVRRAREK NRTAAEKFNN FREMHSAAWH HRRQQVAQRF
LDAFVRSNEP EIGELPSEQL IKPIRLPAAE SALYLELAHA IENLDLRHQR KVFKGKGKAR
GTSTLAATKK IAADAFVIDD DEEDASDSDG GGKAKAKKGT GKAAATTTAA ANKVGGKKGD
PDLEMSHRDR RLIETLGNSA SPEEALLKRA SVYDDFAGVD LSQIKGVNNA IKACEYIVRE
RRKQLEDCKR QLERELPLTL EQHLLVLYHF GFRDDNRQFF RDFVRNANNA SWGDSESKDM
VRQILEEADC TMDGITREAA RRRFGGANKG ALQVALKRRE KERAAAAKGG AAKDGGAAPK
KKLDPKDLAW EEEYLLRAMV HQLTRLRNEL VGRVNALRFF TAVRDCQRAH LDGVEVDIVC
PSAACKHGGE RLKLDDVSIS STCGHAGCRD CVLREAYIGQ CPTADCAALA KPTSVVNASS
LGVEDDGAAT RYGTKLALLC SLLKRLPDEE RALVFVQFET LTATVAEALQ AYGISFVQLT
GSASRRSSLL EAYQDDCGAR VLLLNVDDES AAGSNLTVAN HVIFVGPLLK QEQQQYDGTM
TQAIGRCVRY GQTKKVFVWR FIAMETIDQD TIEKRERITL DVDELEARFD EAAGGALVLE
DVKGTKGTKA GKGVGGGGGG KSGGSGSGKR GRAAASESDS SDEEVGRRGV AARRSVNKRR
RAAAEPIVLD DDDEEEDDDD DDEEDDDDE
//
