ID A0A094DPA5_9PEZI Unreviewed; 1427 AA.
AC A0A094DPA5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V498_10693 {ECO:0000313|EMBL:KFY68246.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY68246.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY68246.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY68246.1}.
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DR EMBL; JPKA01005731; KFY68246.1; -; Genomic_DNA.
DR HOGENOM; CLU_000315_2_8_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
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; PTHR45626:SF14; ATP-DEPENDENT DNA HELICASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05368; NmrA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 645..832
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1197..1355
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 210..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 155610 MW; 3CE0E77B65888F91 CRC64;
MTSTVVIGST GLVGSHILST LLQLPTISSV RTFTRRAPKD TGAKLNATVE DSSKWAASIS
AITPPADIFF SGLGTTRAQA GGFENQRKID YDLNLEAAQA AKKAGVKVYV LISSGGANPN
SMMGYPKMKG ELEEAVKALG FEKTVILRPG LIIGGRDHLR TAEYAIQGVA KLFGAVSGGW
LSDGWAQDAD VIAKAAVSGG LKALAGEGPA SLTLGHSGRN KTPRESTQLP NSTNNALPQN
QRLAKPHQTN PERFIDSSVI EISPGARPIL ISPTSEPSVE WSTPHSPSLS DFGNSTSLFD
YQSAESSGFF PESHQTTNSP VPAAFGTKQK ATKGHPQNHS SAMVNERSPA KAPPKPAQQH
DPDASRPVAP YPANPALQAP AQPSFAPQFG QPTMPQSPLT KVNGPGNKTQ SKYNTNSSMF
IPSKPARPQF QQPRAEPSSY GVPPGAATPI SKPSAPIYKT TQPAPPTVYG SFGTQYPGGF
QSVNNQGGGF KPVNNQGGGF KSVNNYQPTI QPVGQYQNPI DLTRDSYGNI IDLTKESYRD
RLAPAAPYAF VDPKKAAEDL KALLEGAIED EDDDIPKTRS RKKKLDAKAD GLTSMLKGLA
VTEDAPVDED DEDEDDGTVE GVKVKLLPHQ VEGLGWMKDR ELGTRKKGTV PKGGILADDM
GLGKTLQSIS LILTNPRPSG SDLEDGKRKF PSSMQKCTLV VAPLALIRQW ELEIKDKVLP
SHALRVYVHH GPQRTKNHND LKNYDVVVTT YQILVSEFGN SSQDSEGIKV GCFGLHWYRV
ILDEAHTIKN RNAKATQACY ALRSEYRWCL TGTPMQNNLD ELQSLIKFLR IKPYDDLKQW
KDQIDRPMKN GRGDVAIKRL QHYLKIFMKR RTKDILKKEG ALNPGGKPSV AGAASSTGFK
VTERKIEKVF AKFSPEERLF YDRLEKRADK SLEEMMDGQN VNYASALTLL LRLRQACNHP
KLVAGKLGKD GEALGAEAAT VPSTPRKKAA ATGDDLDDLA GMFGDLGVGS KKCDICQLEI
SKDLAKAGAI RCEECESDLL MSTKKPTSRK DRISAIRARN SDIQEEKVKT RKSPPRKARN
RNVIDDSDDE DEGSWIVGED QRGPTKLGKA GGTDDENAEG EGIDVGSDES DKSTNYDTAD
ETELSVVEDV TGEIITIKSD PPSDNESEVE VEGASDIDDS DLDADDAKLS TIVTSTKITH
LLSILGKEAD EHKFIVFSQF TSMLDLIEPF LQRDGYKYTR YDGSMRNDLR EASLKMLREE
KSCRILLCSL KCGSLGLNLT AATRVVILEP FWNPFVEEQA IDRVHRLTQK IDVIVYKITI
ADSVEERILE LQEKKRELAN QAIEGGKNGG VGKLGMKEIM QLFRRDAEYT EPPLNEAAYQ
HTQTRVLAPS REASEESGAS GARGMRRSPP VGGQRRVVEE HPVYGRR
//
