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Database: UniProt
Entry: L5LNR8_MYODS
LinkDB: L5LNR8_MYODS
Original site: L5LNR8_MYODS 
ID   L5LNR8_MYODS            Unreviewed;       319 AA.
AC   L5LNR8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Zinc finger Ran-binding domain-containing protein 3 {ECO:0000313|EMBL:ELK27660.1};
GN   ORFNames=MDA_GLEAN10001438 {ECO:0000313|EMBL:ELK27660.1};
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:ELK27660.1, 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).
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DR   EMBL; KB109991; ELK27660.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5LNR8; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   PANTHER; PTHR45766:SF7; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3; 1.
DR   PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT   DOMAIN          34..190
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          231..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  36190 MW;  BDBB16382D88E884 CRC64;
     MIRRLKTDVL TQLPPKIRQC IPFDLPSAAA KAGAVKDYIK MMLQNDSLKF LVFAHHLLML
     QACTEAVIEN KTRYVRIDGS VPSSERIHLV NQFQKDPETR VAILSIQAAG QGLTFTAATH
     VVFAELYWDP GHIKQAEDRA HRIGQCSSVN IHYLIANGTL DTLMWGMLNR KVQVTGSTLN
     GRKERLQAEE GEKEKWDFLQ FAEAWTPNES SEELRDEVLF THRLEAEAGR SWGREQAFPE
     TDRLKKGRER SSLAPASALE KGRERRSPGE DQEQRVSLKG KEDNPGQEES QEAQVPRVPS
     SQSSYPCQPN TFKRCEVYE
//
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