ID A7TG87_VANPO Unreviewed; 1552 AA.
AC A7TG87;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Helicase SWR1 {ECO:0000256|ARBA:ARBA00040599};
GN ORFNames=Kpol_1055p13 {ECO:0000313|EMBL:EDO18657.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO18657.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: Catalytic component of the SWR1 complex which mediates the
CC ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading
CC to transcriptional regulation of selected genes by chromatin
CC remodeling. {ECO:0000256|ARBA:ARBA00037570}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR EMBL; DS480386; EDO18657.1; -; Genomic_DNA.
DR RefSeq; XP_001646515.1; XM_001646465.1.
DR STRING; 436907.A7TG87; -.
DR GeneID; 5546958; -.
DR KEGG; vpo:Kpol_1055p13; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_4_1; -.
DR InParanoid; A7TG87; -.
DR OMA; AFQQWFG; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR014012; HSA_dom.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 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.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
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:UP000000267};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 416..489
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 751..916
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1286..1439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 74..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..497
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1552 AA; 177593 MW; 330486D036178DDF CRC64;
MAKIIEEKLK RRYKLAEDSF QYNLLVNELF YLREFVSLIE FDPAHRNDSE NFDRFLKDNK
LSLDDLDEVG ELSKDTANDK TDSIPAVRKK RNLRGTTTSS SNGTNVRPSD GIEKSWLNDI
NQIVDEKYDE LINIIGGGAT GASEGSPKEK IHNLTKKNID HKKKNGPSSS SSKTAAAATA
TATSTTKQQT VKNETIKQET VDVVPSKSKN RSKKITNNVK IEDEVDDTIE TVPPLKLIKN
SSKRKNGGKA SITSENTDND VKNIYHDYTH NDNINNNDED DDNDYGNNDD DYDFYFTSSS
DEDTKRPLTK RQRLAPNRPH INLIVHPPNQ TITNPGHVIK QKYNNLSEYL DSFKSMDEDI
TIEEYNKYID EQREVVGQIR KGLESGALKY DPVTDSLQPI TEKDTRLIQS YRPPPISYMY
KEQNLQTHQD HLINQGIYMS KLLQSNKKAR ISRARKVSQM IEQHFRHIAG AEERKLKEEE
KQRKALARTA MQAVKRRWTL AEKAFRVLKK DEEEELRRIQ GKKHLSKVLE QSSQLLGAQL
NQQQDDSEVS SIDNSKNESD LSSSESNNDD FLTSSDEEIE QELETSISEK SNTVDEALTT
EELKLKYREL ENVKSIVNTS EGNDITTQNE SESDSVTTEE SSENDELEED EVSVSESKNI
GLGSLFENTA SGEESESDES VDFKMGESDA DDMNISESED ETMEKSPTPA SEKSEFKLGE
TDPVSVVEVP TPPLLRGTLR IYQKQGLNWL ASLYNNKTNG ILADEMGLGK TIQTISLLTY
LACEKQNWGP HLIVVPTSVL LNWEMEFKKF APGFKVLTYY GSPQQRKEKR KGWNKPDAFH
VCIVSYQLVV QDQHSFKRKK WQYMILDEAH NIKNFRSTRW QALLNFNTQR RLLLTGTPLQ
NNIAELWSLL YFLMPKTITN GSGISGFADL DAFQQWFGRP VDKIIETGEN FEQDLETKET
VNKLHQVLRP YLLRRLKADV EKQMPAKYEH IVSCRLSKRQ RFLYDDFMAR AQTKATLASG
NFMSIVNCLM QLRKVCNHPD LFEVRPVLSS FCIGHSVAFD YTDKNRVVEN LLSYKGYKNN
VNLNTLNMVF TNNERLMTSF HSRDISKLKC IEEFTYELER LRNERRADID ESKLAVDINV
ASEFFKQLGT QKFDETISSL EMKKDINILR CDKKPVYGSN LIKLLDITDS DKTHLDSVSP
LIEPLQTKIL NNKKIIETFA VITPPVVTLD MRKMALGLNG TSSLPGNSKD SLALSLRNME
NPLHLLQTKL TIAFPDKSLL QYDCGKLQKL AILLQQLKDN GHRALIFTQM TKVLDILEQF
LNYHGYLYMR LDGATKIEDR QILTERFNND PRVTVFILSS RSGGLGINLT GADTVIFYDS
DWNPAMDKQC QDRCHRIGQT RDVHIYRFVS EHTIESNILK KANQKRQLDN VIIQKGQFTT
DYFSKLSVRD LLGADATENI VNDDKPLLEE GEDATKDPRS LEKMLAQAED EDDIRAANMA
MKEVEIDNED FTEEIKNNDS DASEENSEYN QYEGTRHIEE YMLSFIAEGY YF
//
