ID K1Y1W5_MARBU Unreviewed; 1976 AA.
AC K1Y1W5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=SNF2 family helicase/ATPase {ECO:0000313|EMBL:EKD19119.1};
GN ORFNames=MBM_02356 {ECO:0000313|EMBL:EKD19119.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19119.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19119.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19119.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JH921431; EKD19119.1; -; Genomic_DNA.
DR RefSeq; XP_007290245.1; XM_007290183.1.
DR STRING; 1072389.K1Y1W5; -.
DR GeneID; 18758291; -.
DR KEGG; mbe:MBM_02356; -.
DR eggNOG; KOG1015; Eukaryota.
DR HOGENOM; CLU_001161_1_0_1; -.
DR InParanoid; K1Y1W5; -.
DR OMA; IEGIQFM; -.
DR OrthoDB; 2787289at2759; -.
DR Proteomes; UP000006753; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18007; DEXHc_ATRX-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; IPR044574; ARIP4-like.
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; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:EKD19119.1};
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:UP000006753}.
FT DOMAIN 1279..1480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1679..1833
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 152..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1203..1230
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..836
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1976 AA; 221764 MW; 0063935C2DF6A541 CRC64;
MTSNNADDPW DWGVDRLFQE LYTWPNPDGF LKPDPVALQN TLKEQNVTGA VFLMSIDKAA
VRKDLAVQGL NQRTFVLAAI SYFKLKSKKW LAMNPHVQPA RSFPPSNSLG GFQGSSTDAA
ASVVDLAHRQ LLAEAAVGAK AFGTPIRTPS DDLFVNKEQP DFEESTAKRR KLDVADPSAE
QAPQFEDDDQ GSKFSIYTSQ GPIINDPAIN PGVDQSTPKA EQNQVAGSNL PDSPVKPKRR
LNLAELTTEP LPENVVRNRH DPSAADFVAH LLGPTPLEGF LSIYDQIGGE ETALEGILPA
YHQIGNQQVD DAQRRLAPII IDTDIDEYRN KEVAAYYSCF QRDRVNQVAE DNLAHDSDAD
AAMQLHLENS SQPTDSQSHV EGISVNAYTT KSNRSRDSLQ RVVAYLGKGK LPVDDVFYEG
IKFGQELNVE DMTKDDYEIS LHMGSAKPPG LVRYVNKLMR NFLLSKAAVT RESRATVTLI
SKINKGNQPV TQNLTRVSKI IRPAKFTDSL LAVDIRRNGQ VFTAVRTYYE GDDAKSGLMG
FFQTPSFTLY YHNSKGKCRA RREKVVDWPQ LLGDKSVDEF KSLDPFQVMS MRPEPQGADP
DFLAKKWGGA ADDTELPLFG ESGSEDDFEE DPVFWREWEQ EQGHVLPIVH QRSKKRSVIT
AEEVNAAIDE AITNLITNWQ DKQQPKIEKT AYRIWRKSHN HGTEWEDVEA FEERIGYLQS
RLSKLREEFH TLPWSRYSEV VGKAYVMEPT VFEREYLRWK IAVLKQDDVP DKPMKQAKSA
SATVMESGAV DNNQKKNSLD DDSDGLGDFV VSDDEDEVDV PEHSSVASDD DDDEAGFIGS
GTPRSVKSLL EDQSEQDALA NDQPKPVSAT SQVESSHSEQ DQPSDKELDP NLDELFTTAS
KFSTPRKSTK SDAKPNAFID LTADSPPKQS DSSSGVLIDL CTPEKPASMS PVRSIPKIKM
KPLRSPSPGP VKSAIYGELP PDVDPAVISQ FSYGFYEALG DRERLLVRIF HKMKQHDRDR
QLEFFAHFSD VKLWAMMKST IQEHLKSEGS VQGDPNREGF DRLTILVQIF LMFIACKFFP
WNDEPLPDAS LHGALHNKEK HYPRFFQIGC QVYRYFNDSF RALQPASPSP EISRSSTVGL
IVSDDDSDDD SDEGPIKRQT RRPRRSREIT INTTTDDDVQ AEDSLPLKRK KTILEDAGAR
SLRERNRERL AEQERRRQTL KAKLAQYGSS LDRGVEFYQI NDAAAEGQKP IFVHEDFRRC
IKPHQMNGVR FMWNQIVTTD GEENMQGCLL AHTMGLGKTM QTICLLVAIA EAAASPDESI
SSQIPDSLKQ TKALILCPAG LIDNWMDELL GWTPPDILGN LWKLNSFDIS ERLDAISEWH
EAGGVLLCSY DGFRNMLTNS AGKKQGARLT QEEHMRVQDQ LLNGPNIVIA DEAHKMKNTS
SKLTKVATQF RTLSRIALTG SPLANNVGEY YAMINWIVHN YLGSLKEFDR KYKNPIEAGL
FVESTQPERR TCLKKLKQLN EELRLKVDRA GMQVLKNELP PKVEFVLTLP LTDIQRKVYS
MYIETLNASR NQLTKDGEVK TTTLWSWIAT LSLLCNHPYC FSTKIQERKG APESDKDRGE
LSSARAPNDQ DDTTVADVVN VPLADTGLSQ SFVNEVMELF NSEDLHSVEL SYKASILCQI
LDCAKAVGDK TLIFSSSIPT LNFLEQLCRT QGRPYKRLDG KTNILKRQAQ TKEFNKGVDE
VYLISTTAGG LGLNLQSANR VVIFDFKFNP IQEEQAVGRA YRIGQLKPTF VYRFVCGGTF
EDNIHNKTIF KAQLASRVVD KKSPLVAARK SLGEFLHEPK EVPQKDISHV RGLDPVLDKV
LDLNPGIIRK IVQTDSFEID DDDRLTAEEN KEVLEQIRSD QLQRLQMMPV EIPAPVLAVQ
QSPRVSHITP TLPQRARFTP PQRPPFENST SGRAGPAASH YFEGYAPIMG GFTRRE
//
