ID A0A178ALF0_9PLEO Unreviewed; 1690 AA.
AC A0A178ALF0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Helicase swr1 {ECO:0000313|EMBL:OAK97819.1};
GN ORFNames=IQ06DRAFT_296109 {ECO:0000313|EMBL:OAK97819.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK97819.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK97819.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK97819.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex.
CC {ECO:0000256|ARBA:ARBA00011826}.
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; KV441717; OAK97819.1; -; Genomic_DNA.
DR STRING; 765868.A0A178ALF0; -.
DR InParanoid; A0A178ALF0; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000077206; 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 GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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:OAK97819.1};
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:UP000077206}.
FT DOMAIN 328..404
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 785..952
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1386..1539
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..561
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..650
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1690 AA; 190656 MW; D963C69135BE5001 CRC64;
MEITSDADID PVSQRDTDNA LDAPDAVQNG SAAEGDATPV IKEEERPGPE NGDGGGVQRP
VKRRKLDDST PSRSASSRAV SPPWKAFAAD GPTTVFENGV RKSSRVNRET APPTPEPVKR
NARHTTKATQ TNGTPKNGVK QGARTAAGSA SAAKGKAASA SSKKAPAPAN PGSRKSERQR
TSSALVHPSS PSSPEGTRKR SGRPRRGTQA SSDEVGYDTW ATPATNGHDP YAGLYASPDD
ANSSMPAPRL RLRFRKPEPT LRHPRHVPPQ TTYTSLAEWL EHDDPLEGED AQRIDQEKAD
EEAARRLRIV EAAEHGVLSQ TRCSIFAPEP AEEPPQQYAH WDHVIAHALH FRKLLKEEKE
YHRKLAKTLA REAYDFWKNK FKRKSEEEIE QEETDRQILR YKQLVLDVKG AWANVKVEID
KERVARWEEE QMQLGHKAMD DMFNQAQEIL GRNAADNASS LVSDDREFEE EFDSGGSDAS
GNANLDDVMS SSSDSEDGEA HDEDANLTAD QLREKYGQLP DLPDSSSEVD AESNVEAEDD
DPEEGTPEPT PDPDLEDEAM ADLTENNLVH TNGFHNHDDA SKQKANDIDP ATIELEQVDE
ALLDSDEDGK ASESGSEAWS SDEESDMEED ESQESAEEGS GEEEDDDSDV GMMGFLAPSD
IKKLKEVAKQ RVEDDQAEDD QAEDDSEQPL PTNGYVLTPV EDSTEPYTNG HKDNAGEEEG
HVNGDSGLKP SVEPAGPEPM QDVVKTGDIS NSRSRRASSP PRREIPSLLR GTLREYQHDG
LDWLANMYDS ETNGILADEM GLGKTIQTIS LLAYIAVHRG IWGPHLVVVP TSVMLNWEME
FRKFLPGFKI LTYYGDINER KRKRMGWRNM GKDMYNVVIT SYQLILQDAA AFKMRPWHYL
VLDEAHNIKN FKSQRWQTML TLRTQRRLLL TGTPLQNNID ELWSLLYFLM PAGFAGEGRI
ASLEEFTLAL KDPTKQILDQ GRQKLDAEAQ KVVSRLHEVL RPYLLRRLKS EVEKQMPGKY
EHVVYCKLSK RQRQLYDGFM GRASTKEILS SGNYMSIINC LMSLRKVCNH PDLFETRAIV
TSMAMPKSVV AQYEIKDLLV RKRLHETTEV NKVNLDALNL VFARREQTQL GHARRVHHIR
ATRPLEDLVE RQTRRLNKAS EAPSTSLQST MAAMARREQT VVRDQLQHCL HLTRSRTQFM
PIYGKDIVDA VTVDWHDFTF GARREGRKVS RAKFLPPPPH YYPMQQPVAP YQHQQPQMFP
QAHMQPRHEQ VEQVTIRDYR GNLGFRAPHS IAASLEWSNE QVTHFFDMIP TLEQRAEAYE
PLITRFTCVT PAVTAEEIAP LSLSKRGVDL VRTSDLVRKR DPFHESRIRQ SIAFPDKRLL
QYDCGKLQRL ATLLRDLQAG GHRALIFTQM TKVLDVLEQF LNIHGHRYLR LDGSTKVEQR
QILTDRFNSD DRILCFILSS RSGGLGINLT GADTVIFYDL DWNPAMDKQC QDRAHRIGQT
RDVHIYKFVS EYTIEANILR KSNQKRLLDD VIIQKGDFTT DTFNKVTWRD ALDDGMGIDT
SDEAGAAMER VLGERAGLLG DARVMNTVED TEDRNAASIA QKEIVDEIHD DQVDFNESSN
ATRATSAAPA TQDEPLDADG NEIARRHVDE YMLGLYREEY GKEPYKPPTD RQKRNRKGQD
PHVRQRKKKY
//
