ID A0A0G2HVM1_9EURO Unreviewed; 1151 AA.
AC A0A0G2HVM1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EMCG_03690 {ECO:0000313|EMBL:KKZ61810.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ61810.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ61810.1}.
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DR EMBL; LCZI01001234; KKZ61810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HVM1; -.
DR VEuPathDB; FungiDB:EMCG_03690; -.
DR Proteomes; UP000034164; 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; 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 PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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.
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 597..764
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 951..1101
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 128008 MW; 41F69858BE97E237 CRC64;
MEDLVPDTPL RNQKIDQSSF PVGSDVENDD QGSSDFEETV ATVPLYKHPL PTQTLFTPAT
QQFTQTSTQP TQIIDRNPNH LFSPSAQNSS IVQVATSSPL APKSSAYRPY NTPRAGVLSN
SMAPIGTQFR APTMVKVPIK RPPVVDLDDD GPTYRGGSSD EDDIQFVGTT DIKRSTFAKN
PKSPDKERIL ESPAAAAAAN GGVNRFKEIT ASAFYNPSAN DNNNRKVSEK RSVDRIIKVE
RIRNVFPGKS VQLILDALVS KRGHYEDSLE YLAKLDDYLP TDPISDDELS LDHNVPQVEP
AKQQIKARTR IQDKWTSSQR LPTQKSGADR DGSAPRKRLI RGARTRSSSP PSGPSPAPAP
VSKKPGRLIR GKKTRPRSES PEIPIVEIDS SESDHPEDSE DDGILETKVL KFFNSCSVAD
LSDIAEIQEN IANTIISKRP FKTLNAVRQI TQADEVNGKT SNAKPKKYAK KPIGDKVVDK
CLDMWTGYEA VDALVSKCEA LGKPVANEMK RWGVDIFGTK TEGELEIVSL NNKNMSNRTH
DSGIGTPSSR RSSSVDDDEL KPNNNSRKKQ QYISQPAIMS ESITLKNYQI VGINWLNLLF
EQNLSCILAD DMGLGKTCQV IAFLAHLYEK GVKGPHLIVV PSSTLENWLR EFSVFCPKLN
VMPYYANQTV RAEIRQQIED TRDSINVVVT TYTIAKAKID AAFLRAMDFC VCVYDEGHML
KSSKSMLYEK LIRIPAQFRL LLTGTPLQNN LQELASLLGF ILPSVFRERK EDLEYIFSAK
AKTVDGTHTA LLSAQRIARA KSMLTPFVLR RKKHQVIDLP PKITSVEYCE MNEAQKEIYT
HEVETVRQLV ADRAAGKKVG NKSANILMKL RQAAIHPLFY RRYYDDKTLS RIAKACIKDE
KWAASNPDQI YLELCAYNDF EVHTLCEQNP TALSKFVLKN DEWMHSGKVD KLCELLNRFK
ENGDRTLIFS QFTTVMDILE HVLQTLQMPF FRLDGSTSVE DRQSILDAFH EQVEIPVFLL
STKAGGAGIN LACANKVIIF DSSFNPQEDV QAENRAHRVG QTREVEVVRL VTRLTIEEQM
YALGQTKLAL DQRVSGEDDG AVAAKKGEEA GLKVVEEMVI AKLEEEGKKG GNGPAVTTTA
AAAEKAEAEV A
//
