ID A0A0C9MUN9_9FUNG Unreviewed; 1909 AA.
AC A0A0C9MUN9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SNF2 family N-terminal domain containing protein {ECO:0000313|EMBL:GAN11149.1};
GN ORFNames=MAM1_0485c10706 {ECO:0000313|EMBL:GAN11149.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN11149.1};
RN [1] {ECO:0000313|EMBL:GAN11149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN11149.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF836774; GAN11149.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9MUN9; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 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; SSF48371; ARM repeat; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1330..1503
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1687..1839
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 171..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1909 AA; 211777 MW; 1CC52D8FD245840D CRC64;
MATRLDRLVL LLDTGSTTAV RRTAAQQLGE IQKQHPGELY NLLSRVVVHL RSKAWDTRWA
AGQALEAIAA NVPVWDPCAA DATTDDTMDI DQEQDVHKLR FNQFDLASVL QHGKLLLGSA
GKEYDIDFSD MTPQERLELQ RRNLKERLGL ASQFMDVDLV DDTDLDNNKT NQAAKAVTKS
PSPSPSTSTA AVAANAPTPA VAEINMAGLS ARERNMLKRK MKLESKMKGK KEKVRVMDLK
GKSEPKAVKV ESKEECVEFE FTAQPQSDKF VVEVKKPTPS VDDTVDEVQR DWPFKMVCEH
LCLDLFDPAW EIRHGAGIGL RSILKAHGDG AGKRLGDKLK NEELHNAWLE DVAIRLLCVF
ALDRFADFVS DQVVCPVRET CSQTLGVVLQ YMTASSVEKV HENLLKLINQ DDPSFGGRSI
WEVRHAGLLG LKYTVAVRKD LVDMLVDGTT GAVILGLRDH DDDVRAVSAA TLLPITAEFV
RMSSKDRIRD VITTLWDCLI DLKDDLTAST GAVMDLIAKM FEQPGVMEIV REGCSLSELV
PRLHPFFRHT ITGVRTAVLN TLLTFIDCGT SAEWVDERVY RLVFQNLIVE EKVDIIEKTL
AVWKGLTISG KVDTQLVLQG TQNWLGSWFE ITMTPIGQPL DTASYFYKPP GAFGNGGTLA
TTTSAPVVDK TSKKMTKKAK TNQTSSSISG ETVAAAAATD SRDDGHNLDA GMIAQDFSLI
TTNQVMRCRI ACTTALGMAM STWPDDSMEM SYQEVILTLL TSQWALKRQL GAMAVEEWAK
AVLKTRYNAD CISHAPEDAI LANTHNFPKT LSNAMIANLD NAAKHTTGFY FELVHVLKRI
RGECQNLVNA FHSEAQVPME HIPTLPTLVP GEALPEQGPL FTIETATSVV GDTFEQLMGK
IPKIKGRAAV ITALDERQRR VVGSIGYFEE LKQKIEINVY ASTAGAVIEL GVLPAKLNPV
IRSVMNSIKF EENLELQERS AATLTDLIAL CERSQSRVNP NDKIVKNLCT FLCSDTTVTP
VLEDNQTKSG ILSIQKEETS GKAASAGAGA AAANTKEALT QDQKDAQLMK RGAEISLRKL
CDTFGGRVFE IVPKLLQCVT QKVMETFPEN ADRTNTVEKA DQAISEQFQL GQEVIDGLTI
LTMIVPYLSE GLWPQICEFI PYVCRALQSC YAVVRSVSAR CLAAIANVIT TKTMQVIVDH
VLPQLANPLN SYHRQGAAEL VYHLVQLLDT KILPYTIFLI VPILGRMSDA DEAVRLICTN
CFALLIKLVP LEAGIPDPPG MSAEMLAHRD EERRFLSQLL DSSKVENYEI PVKINAELRK
YQQEGVNWLA FLNKFHLHGI LCDDMGLGKT LQSICILAGD HFQRAQKFAE TKSPEWAASP
SLVICPPTLT GHWFHEIKNY CDNLKPLLYT GGPAERKRLR ASILKNDVII MSYDIIRNDI
EELSAITWNY CILDEGHIIK NGRTKITRAI KTVKSNHRLI LSGTPIQNNV LELWSLFDFL
MPGFLGSEKL FNERFGKPIL ASRDSKSSSK EQEAGALALE ALHKQVLPFL LRRLKEDVLH
DLPPKIIQDY YCELSDLQKS LYDEFAKSQA RSSVEEDLGA GVVTKPGEKP KGATHIFQAL
QYLRRLCNHP LLVVSDKYPN YRKVETFLNK TNTNIHSISN APKLQALKQL LGECGIGVTT
TESDSDPAAM AIGAVSQHRA LIFCQLKPML DIIENDLFKT LMPTVSYLRM DGSVDASKRH
EMVQKFNADP SIDVLLLTTH VGGLGLNLTG ADTVIFVEHD WNPMKDLQAM DRAHRIGQKK
VVNVYRLITR GTLEEKIMGL QKFKLNIANS IVNQQNSGLH SMDTDQILDL FNVGNDDASS
NNKKRAKNTD VVADGLGPAK AVLENLETLW DDKDYEEEYN IDSFISSLN
//
