ID A0A099P936_PICKU Unreviewed; 1053 AA.
AC A0A099P936;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=JL09_g469 {ECO:0000313|EMBL:KGK40566.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:KGK40566.1, ECO:0000313|Proteomes:UP000029867};
RN [1] {ECO:0000313|Proteomes:UP000029867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD108 {ECO:0000313|Proteomes:UP000029867};
RX PubMed=25159171; DOI=10.1186/s12934-014-0121-4;
RA Xiao H., Shao Z., Jiang Y., Dole S., Zhao H.;
RT "Exploiting Issatchenkia orientalis SD108 for succinic acid production.";
RL Microb. Cell Fact. 13:121-121(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGK40566.1}.
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DR EMBL; JQFK01000002; KGK40566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099P936; -.
DR VEuPathDB; FungiDB:C5L36_0C02440; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR Proteomes; UP000029867; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
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; IPR044754; Isw1/2_DEXHc.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 174..339
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 843..895
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 96..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 122570 MW; F594945E89E40ED3 CRC64;
MTQVENSGIE EVQDPLAQYR AGLQDYPGFK GSEIRDFQSL KEHYFVEDDK KKFDVQATAN
RFKYLLSLTP LFKHFLKVKA AKDENFSKVL ELIEKDDPDN KQSNGRGTDH RRRRTEKEED
AELMRSEETE IDPKVQVLEL EGEFTDSGYE FSKSPKYING SLRPYQIQGL NWLVSLNTND
LSGILADEMG LGKTLQTISF LGYLRYVKNI RGPHIVIVPK STLENWQREF AKWTPEVRTC
VLTGDQETRN QIIKDNISNC QFDVLISSYE IVIREKAVLR KINWQYIVVD EAHRLKNEDS
LLSQIIRMFH SKNRLLITGT PLQNNLHELW ALLNFLLPDV FSDSSTFDEW FSNDETGSDS
NESTNDQDKV VQQLHQVLKP FLLRRIKNEV EKSLLPKQEL NVYVGMTPMQ RKWYQSILEK
DIDAVNGANK KESKTRLLNI VMQLRKCCNH PYLFDGAEPG PPYTTDEHLV YNSQKMLVLD
KLLKRLGEQG SRVLIFSQMS RMLDILEDYC VFRNFGYCRI DGQTEHTERI VAIDEYNKPD
SDKFVFLLTT RAGGLGINLT SADVVVLYDS DWNPQADLQA MDRAHRIGQK KQVKVFRFVT
ENAIEEKVLE RASQKLRLDQ LVIQQGRTGL NAGQEKKSVA SNKDELLNMI QHGAADMLMS
AQIKEEGNEK HEIDDDELEK ILMKSQEKTG ELKSKFSKLG LDDLQNFSSN NDSVYEWNGK
NFQKKEVKGL AGVDGEAFNW ISLAKRERKG NYSVDGYYRE GTGDENELRQ PKHMNLYDHQ
FYPEELHYLY ELEWAYYKRV YKIKAKAEKN KSNEDLQLEQ AFIDHARPLS EEEKQLKKEY
LAQGYGNFSR RDFFSFISAN VKHGRYDIAS IAKEMPEKTY EEVKKYAEKF WKSFRDIENY
ERYIGQIEAG EDKLRKMNVQ REVLRWKVAS YDYPMRDMEI KVPYTTIAKR EWSEVEDRWL
VIQMLRLGID REDIYEQIFN EIQYGNDPVI EMNFWLQSRS AQEIGRRCQT LLGSIVREHE
AGSKKRGRTT GTGKGKSSGG ARGGTKSRKK RHV
//