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Database: UniProt
Entry: A0A0J6Y369_COCIT
LinkDB: A0A0J6Y369_COCIT
Original site: A0A0J6Y369_COCIT 
ID   A0A0J6Y369_COCIT        Unreviewed;       815 AA.
AC   A0A0J6Y369;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=DNA repair protein rad-5 {ECO:0000313|EMBL:KMP03071.1};
GN   ORFNames=CIRG_02763 {ECO:0000313|EMBL:KMP03071.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP03071.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS028094; KMP03071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6Y369; -.
DR   STRING; 404692.A0A0J6Y369; -.
DR   Proteomes; UP000054565; 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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.30.70.2330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022771};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          364..508
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          644..811
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  90562 MW;  0F246DCA9CD5165A CRC64;
     MHNATPKNFK NPDIRATGGS SSGASRGGKR KAPALIDLTA DDDDEVALSS QARSAPRQYV
     PSQTLSQPAL PPENFLSLSQ RLPDTQAELE EEANAAAVVE SSQEYYNGQA TKGEYVNIRR
     EPGNPYDSNA IRIDNVMGDQ IGHLPRQLAS KLAPYIDSAD LLVEGVLAGN KGVYECPISL
     RLYGTSEPRQ QLELVARMKR QGLPVAELLM KNSDRKKRQL QELKAAAANS SRARKNIGRG
     EEWNKSDNAF GVNMAPPGGH SDEKNKNQES IDDIIGQSVV FNPREMSQVV EKFGADEKEL
     AAMPMAECPA SLSTELLPYQ RQGLAWMLDK ESPQLPGIGR EDVVQLWKRQ AQAYKNIATG
     YVTNQAPPLA SGGILADDMG LGKTIQTISL ILADLKVASA QSSRTTLIIS PLGVMSNWRD
     RLLPMSSRRM RLKFSYTMGQ ALKPKQGLFS MRWRRVVLDE GHTIRSPRTK GARAACALEA
     DSRWSLTGTP IINNLKDLYS QLRYLRISGG LEDFSVFNSA LIRPLKDEDP NTNLVLQALM
     ATICLRRKKE MGFINLRLPP MQYPSWPRRR VSLWNILTGK SRMLPIHTYL RLSCAFDKQV
     IERQHKCPLC RAELADTSNL VHPAVALGED DSKVDVDPEE SSSKIQALIK ILTAHGQAPG
     SKTVVFSQWT SFLDLIEPQL VKHNITFTRI DGKMSSTKRD VAMATLTNDP NCTVMLASLN
     VCSVGLNLVA ANQVILTDSW WAPAIEDQAV DRVYRLGQKR PTTVWRLVME GSIEDRVLDI
     QKRKRDLMTT AFREKNSKTG EQQRARLADL EKLLQ
//
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