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Database: UniProt
Entry: A0A1L0D6C7_9ASCO
LinkDB: A0A1L0D6C7_9ASCO
Original site: A0A1L0D6C7_9ASCO 
ID   A0A1L0D6C7_9ASCO        Unreviewed;      1042 AA.
AC   A0A1L0D6C7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=CIC11C00000005414 {ECO:0000313|EMBL:SGZ52060.1};
GN   ORFNames=SAMEA4029010_CIC11G00000005414 {ECO:0000313|EMBL:SGZ52060.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ52060.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ52060.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ52060.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; LT635758; SGZ52060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0D6C7; -.
DR   STRING; 45354.A0A1L0D6C7; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000182334; Chromosome iii.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17998; DEXHc_SMARCAD1; 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; 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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182334}.
FT   DOMAIN          508..675
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          876..1034
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          108..146
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1042 AA;  119298 MW;  4FABBD588F6C4EC2 CRC64;
     MAFQQTPKKE QNVLQVPSSS PINVRSSPVA AGHAMPSHHD AEEEKRKEEM KKRFYAHKFW
     PVLQKRFYYL TEPEIFKGMV KGKGNLRDIC LWLGDNIPLS ERMNQYDNER TVRRLEEENA
     KKQAAAAEQE NRRQEEARAL ELAEVLLPPS PLIQSPAPQV YEDEDASPVK VAGKARQKRS
     LLSMEAVKAP DTKIQLMKPK VSILEKYRNR TNTQTRIDSL FLRANGEMKK RKLVRADDMD
     ESTPATSQST TPNAIGLPGV LTQAFGFKEE AIPRLTTSKN LSVEIDELDL LEEKIRANRK
     KKKSSSSRTS HSDDELEEDV FSDDMSAEDD DDHYSNGLTS IDGQILEFLN SSSVDDIVEI
     CNVQPKIADL LISKRPFKTI YEVSEDRFDD ATPEPETKRR GGQRKAMGMR IVESTEFSLK
     GYKAVDSLVK KCSEYGNLIS SQMDRWGVKI TGEGELSMVE VDANEEDNED DDIVSNKRSL
     PYVKHKPTLL APDIELKNYQ QVGINWLNLL YHNKLSCILA DEMGLGKTCQ VISFMAHLKV
     TSDKKRPHLV VVPSSTLENW LREFNKFCPD LIVQAYYGSQ AEREDLRYEL QEMQYDVLVT
     TYNLATGAPP DFKFLRSQHF DMIVYDEGHM LKNSSSERYN KLMRLKADFR LLLTGTPLQN
     NLKELVSLLA FMLPNLFVEK REDLQGLFNK KASVDGADNY NPLLSQQAIN KAKTMMTPFV
     LRRKKAQVLK YLPGKSHEIV KCKMTAKQRE IYSDYISQGK ATKLERERRK NLEGKEAEEA
     RKIPIASSSN VMMSLRKASM HPLLFRTIYT DDILKEMAKK IMKEPEYVSA NRHYIYEDMQ
     VMSDYELNAL CEKFPKTIGS YVLDKEKWLD SGKITKLLEV LDNVIERKEK VLVFSLFTQM
     LDILEKVLSF SNITFLRLDG QTSVDTRQDI IDRFYEDETI PVFLLSTKAG GFGINLVAAN
     NVVIFDQSFN PHDDKQAEDR AHRVGQTNEV MVTKLISEDT IDENILMLAE NKLQLDQSIS
     NDTNETKFEE KAASMFEKLL FN
//
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