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Database: UniProt
Entry: L5MJ87_MYODS
LinkDB: L5MJ87_MYODS
Original site: L5MJ87_MYODS 
ID   L5MJ87_MYODS            Unreviewed;      1421 AA.
AC   L5MJ87;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Putative DNA repair and recombination protein RAD26-like protein {ECO:0000313|EMBL:ELK37803.1};
GN   ORFNames=MDA_GLEAN10009024 {ECO:0000313|EMBL:ELK37803.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37803.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; KB099991; ELK37803.1; -; Genomic_DNA.
DR   eggNOG; KOG0387; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR029256; Heliccase-ass-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF14773; VIGSSK; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT   DOMAIN          1..123
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          318..468
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          521..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1164..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1229..1263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1421 AA;  161073 MW;  CA97BC37336BC5B8 CRC64;
     MFLIVAPLSV LYNWRDELDT WGYFRVTILH GNKKDNELIR VKQRKCEIAL TTYETLRLCL
     DELNSLDWSA VIVDEAHRIK NPKARVTEVM KALKCNVRIG LTGTILQNNM KELWCVMDWA
     VPGLLGSRIH FKKQFSDPVE HGQRHTATKR ELATGRKAMQ RLAKKMSGWF LRRTKTLIKD
     QLPKKEDRMV YCSLTDFQKA VYQTVLETED VTLILRSSEP CTCSSGRKRR NCCYKASIST
     NSHGETVKTL YFSYLAVLQK VANHVSLLQA ASTSKQQETL IKRICDQVFS RFPDFVQKSK
     DAAFETLSDP KYSGKMKVLQ QLLNHCRKNK DKVLLFSFST KLLDVLQQYC MASGLDYRRL
     DGSTKSEERI KIVKEFNSTQ DVNICLVSTM AGGLGLNFVG ANVVVLFDPT WNPANDLQAI
     DRAYRIGQCR DVKVFRLISL GTVEEIMYLR QVYKQQLQCV VVGSENAKRY FEAVQGSKEH
     RGELFGLYNI FKLRPQGSCL TKDILEREGL VEAGVMTATT WLKEEPQEHH REPPREPDGQ
     EHRGAEPPAK DACGLCSDLS DDELVDNSRV QPAKGKASDL SKAPGPPGQL TLLQCGFSHL
     LETKWKAVDD NENTASXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXKDVGTSK
     HQKLANILNP REICVFEKSK KILEQPISSE SDKKNFKNTA DHHCILQNVT ESEDSDVILP
     TQYTTEKSLQ SRIKSRPPAD RSEDSETENP IEITNDGDDR KTDVRESGLI SKQLNPKSVT
     LKSIMKRRGS SDISDESDDI DISSKSRVRK QRATSSLRFK RKKENKRELD TFSKTMKKAN
     QLYATDEDCN SQVIDDFSSL DDDFFVSHIG FSKQKHRPNA IKDKIGFSSE LPRHKKNSTL
     VPRKPMKFSN ESIANQEQIY ESMDKFLDGV QEVAYIHSNQ NVIGSSKAEN HMSRWAARDV
     FELKQFSQLP ANIAVCTSKT YKDRMKADTS THAKEVQQAS EGGVSCPLYI AHPVSQKKKK
     VYHTDQTTFI LGETPRGVRR KQFEEMASYF NLSSVKEFAQ HITNATSEER QRMLRDFYAS
     QYPEVKDFFV DSAAGFIKPV HEAGKRGRNK SEKRESSIKE KLPDSKTLSF KDSTKKNSQI
     CSPKRYTEKS VRPQSHGFCR EELLSNNAET PKLPMSSAQG TDSEKHSQVS KDPTASSSLS
     SESEACERRL ENTMKDQQGL TRMGISRNEP LFKLENKKIK NAELEKISVA GLLGDTSILD
     DLFKSHGNSP TRLPRKILSG PMEKAKRRPK DFWDILNEQN DHSLSRLTDL AVIETLCDKV
     PLAAPSRTGE PETSLWKSNE NFLWKKVNSS DADENTTKTQ E
//
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