ID A0A068S214_9FUNG Unreviewed; 1623 AA.
AC A0A068S214;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Helicase swr1 {ECO:0000313|EMBL:CDH55892.1};
GN ORFNames=LCOR_06991.1 {ECO:0000313|EMBL:CDH55892.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH55892.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH55892.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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:CDH55892.1}.
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DR EMBL; CBTN010000033; CDH55892.1; -; Genomic_DNA.
DR STRING; 1263082.A0A068S214; -.
DR VEuPathDB; FungiDB:LCOR_06991.1; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000027586; 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:0004386; F:helicase 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 Helicase {ECO:0000313|EMBL:CDH55892.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT DOMAIN 380..454
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 757..922
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1303..1453
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..628
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 187179 MW; D1D5E05F2C01CD56 CRC64;
MTMVDHDPAK GESHDPTSSR PGRKKGRRAL MIEKGPDTLK RPRTLFDTDG NLSKHNILSP
DSSIARSTRN SQRQLQPPTP TKRARDSVST TTTHSRGRGR GASTASRGRG RGRGNNNDKS
RGVKRLAPDE EHSQHDTTTA TSSSSSRGCG RGRGRGRGRG AITNNNKRQR SDDSTRLPRQ
TYLMANASTP LDRYRNDVLT EKAEELATIY DHHTETVREL YHLELHQNML DYNPGQKENI
YDQRFKKYAE AYDLWDSANE HLQHHSRSSG VNTRHQTLPL IGALQDVFEE KIKKEEVAAG
RLPSKSTTTL YTGSEVRRFT RQYRTLSDYL ASFVSIEDNE DVTPAQAEEL IKKEIAIRQR
IERLNANGGF STRLQSIANR RPQGELQRSN THHDIVVSQA LHASKLFASN TRHRRNAARK
CAKAIERHWE LIRTHDERRH REETRRLMRL AKKTAQHVMR KWKVVERVCE ARHKEILKEE
QAMEGRRHLE MILEHSEQML GVRMEELAAT NEEEDEEEMD QPKIEEIDQE QPPIDIIPES
PPQQRSAGND DDEFSEEDMD EKDHMISDED ESEDDDDELN ELNADQDLDI EQLLKKYNYR
LEEDSEEEEE EEEDQPMNDA EEPASPDAEH DDDNTSKTMI PADTLPQHDD QQPDNSHHEE
KEDEQIEKME GSDDDRTVTV YGSDMSDIEE NEEKSVENEG KQQPSPPSPP SESVTPKPEM
AQPTGTTLST TKVNIKIPFL LRGTLREYQH VGLDWLASLY NNGLNGILAD EMGLGKTIQT
ISLLAYLACE KRIWGPHLIV VPTSVILNWE MEFKRWLPGF KILTYYGTPK ERKEKRTGWS
KENAFHVCIT SYQLVIQDQN VFRRKAWQYL VLDEAHHIKN FRSQRWQVLL NFNSKRRLLL
TGTPLQNNLL ELWSLLYFLM PNGVSQSMPI GFASQKEFQE WFSHPVDRVI EGQQEMDADS
RAAIQKLHTV LRPYLLRRLK RDVEKQLPEK HEHVVYCRLS TRQRFLYDDF MSRAKTKETL
ASGNFLSIIN CLMQLRKVCN HPDLFEERPI ITSFAMHDEV LWTGQQLETR VRKRLGFNNG
GLDSMNLVIV NNEHLSATVA SEYDNIDASK YFVHQIARYQ TQIDIAESRG ITMQNRYNEL
RQYAARYDYH DFKKYYKFRQ LQGCYASRSR WESMLHVNSM RCARRPLYGA SLIQLCESAT
ASRESAFFPT QHDNRHFFDI STHLRKAVVS YQDRINAHMD IIDRYGFVTP GTVIQRSPIQ
EEQQYQEHQG SLDVDILHPL RTRLSIVFPD KRLLQYDCGK LQKLDALLRQ LAAGGHRALI
FTQMTRVLDV LESFLNMHGH RYLRLDGATK IEQRQVLTEQ FNNDPRILAF ILSTRSGGLG
INLTGADTVI FYDSDWNPSM DKQCQDRTHR IGQTRDVHIY RFVTEYTIEE NIFKKANQKR
MLDNMVIQEG EFTNDYFQKT DWWRDLPEVT GSIADTTTPT TTTAAVKINP PPDASNIDIE
QALLQAEDEN DAQAAITARN EMEMDDREFN ETRQSNSPSV SSPSGPSLSV PATPAPESEG
QTFLYEEDDV EEADAAAVDE QDMQLSVGHV DQYMLRFWER EMYGHYLGFG GLPEPGQDTQ
IVD
//
