ID A0A0L1ITZ3_ASPNO Unreviewed; 969 AA.
AC A0A0L1ITZ3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative helicase {ECO:0000313|EMBL:KNG82880.1};
GN ORFNames=ANOM_007524 {ECO:0000313|EMBL:KNG82880.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG82880.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG82880.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG82880.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-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:KNG82880.1}.
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DR EMBL; JNOM01000308; KNG82880.1; -; Genomic_DNA.
DR RefSeq; XP_015403803.1; XM_015552780.1.
DR AlphaFoldDB; A0A0L1ITZ3; -.
DR STRING; 1509407.A0A0L1ITZ3; -.
DR GeneID; 26809328; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000037505; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KNG82880.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 390..577
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 717..767
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 808..953
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 109482 MW; B594F000B8484B04 CRC64;
MSLRPLLNPT DEDDGDDWTD DMRRVRPRLE VPVDWALNPS EDHIDSIVYP TDMSFNHSFG
DQDSIFVDQL EPIPGLDAPP FDQSSFLQPV PDDVGLSGTS MTSTPGMDFT DGPAGSVDVS
MVDVASSEQG KQVCYGMLVH EKVKLVGKGQ ELETKILALK ENNQHIHTLS IQPSGDGSLF
LRFPDGTDLG YLSRKMEQAL EALICLPLFE IDALTNLNSL VESLRRAGKP ADAATRVSIN
VYGRESDRDE VGRELSKKDL FLQHPDDCRV GIKYDNPHIL RLDGMDETDT EDDEDVNEEG
VLEATPERDE GFDETIAEVF NSLQRGDHLT ELGGSETLNR TLYRHQGEAL DFMIQRETGD
ISEDKYRLWQ PKSVGRGQLY CHIITGNEQQ EQPDESGGGI LADEMGMGKS LTTLVLTAKT
LREARQWVET KALPGASLAE TPSRATLVIV PSRVLINTWE REVDDHLNGG MKMMRYHGRS
RKELISNIDR YDIVITTYNT LAKEHDAKIL GKGQSPLHNF AWYRVVLDEA HMIRRRSTTF
HRAVVELRAR SRWCLSGTPI QNSLGDLGSL LAFIQLKPFH DPRNFSHWIA NPFGVRATKR
KAIERLTHLL EAVCLRRTIE RVNLPGQRSE LRRVQFTPEE RANYELTRKD MKRFIHQQAG
EHNQQAETFG MFQVFLQLRS FCNHGTYQPR FSWAKRNLLE DELDPVCSMT RDSLNRCSGC
RQPLPVMPHG RQPKYVESCK HVLCDDCSWG SSIQSDPEER RHCPLCESLR GSRYRGHIPT
ASNQRNRSDA DYLNADGHSS KMRVLISDVQ RDIGATKSII FSCWTRTLDL IAKHLKVSSI
EFERIDGKTP TSQRQNILDK FDGTRAVPVL IMTTGTGAFG LNLKSVNRVF IVEPQWNPSV
ESQAIARAIR LGQEQQVLVT RYLVENSIEE AMCSQQTQKL KISQMEFRKD LEASAAGDEG
TSDYPSAMQ
//
