ID A0A0D2UGM2_CAPO3 Unreviewed; 863 AA.
AC A0A0D2UGM2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Helicase, variant {ECO:0000313|EMBL:KJE94231.1};
GN ORFNames=CAOG_004904 {ECO:0000313|EMBL:KJE94231.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94231.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KE346366; KJE94231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2UGM2; -.
DR EnsemblProtists; KJE94231; KJE94231; CAOG_004904.
DR Proteomes; UP000008743; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KJE94231.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743}.
FT DOMAIN 1..140
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 269..420
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 640..692
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 541..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 100130 MW; EC3288937A61AE4D CRC64;
MLGYIKNIKK IKSHNLLVVP KSTLTNWMNE FRRWCPSLRV ICFHGPKEWR AEFAQTTLAP
GDWDVCVTSY EITYREKAAL RKFNFHYLVL DEAHSIKNEA SRLATVLREF KTKNRLLLTG
TPLQNNLHEL WALLNFLLPD IFASSDDFDA WFSLTSSTDQ LEVVSRLHAI LKPFLLRRLK
AEVEKSLLPK KETKIYIGLT PKQREVYQGI LLKDLDVVNS GNANKVRLSN ILMQLRKCCN
HPYLFDGTEP GPPYTTDKHL LDACGKMSVL DKLLPKLQAQ GSRVLIFSQM TRMLDILEDY
CMWRGHTYCR LDGQTDHEDR ARMIDEYNAP NSSKFLFLLS TRAGGLGINL YTADTVILYD
SDWNPQMDLQ AQDRAHRIGQ KKQVRIFRFV TENTVEERII ERAEMKLRLD AMVIQQGRLV
EQQKALNKDD MLSMIRFGAD RVFKTEDAMI TDDDIDAILT KGEVKTAEFN EKLKELGEDR
LKSFSLDADE RSLYNFDGED YRRKRQANSI KNWIEPPKRE RKQTYSVDAY FREALRVTSN
ATEKDAGAGS SKAKPPRPAK TPNISDFQFF PSRLFELLQQ EIYAYRKQLG WKPTAPTPEE
IAASSGVDLV AEHEQECEKI DQSEPLSEEE TVERDQLLEQ GFSNWNRADF RAFLRGCEKY
GRWATALIAS EVESKSVAEV DEYAKVFWDR YREVADSDKY LERIELGESK IRRREEIQQI
LGAKMQLYRS PFQQLRVVYS TSGRGRCFTE EEDRFLICML YKVGYGNETA YDDIRRAIRA
APQFRFDWYL KSRTAVELQR RCTSLIQLIE KEMLDQQQEK EAAAPSDSSK RKKPSRETSN
KKPRLEDEDV DAPSPVPTKS SRK
//