ID F7VLX4_SORMK Unreviewed; 2276 AA.
AC F7VLX4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Putative SGS1 protein {ECO:0000313|EMBL:CCC06502.1};
GN Name=putative sgs1 {ECO:0000313|EMBL:CCC06502.1};
GN ORFNames=SMAC_04895 {ECO:0000313|EMBL:CCC06502.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC06502.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06502.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC06502.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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:CCC06502.1}.
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DR EMBL; CABT02000001; CCC06502.1; -; Genomic_DNA.
DR RefSeq; XP_003347587.1; XM_003347539.1.
DR STRING; 771870.F7VLX4; -.
DR GeneID; 10805018; -.
DR KEGG; smp:SMAC_04895; -.
DR VEuPathDB; FungiDB:SMAC_04895; -.
DR eggNOG; KOG0351; Eukaryota.
DR HOGENOM; CLU_001103_16_0_1; -.
DR InParanoid; F7VLX4; -.
DR OMA; MAINWTT; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 1225..1406
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1427..1579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1823..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1991..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 894..924
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..593
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..774
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2000..2025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2041..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2151..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2276 AA; 249561 MW; 5BB21E540640D71D CRC64;
MAEREGTSFN CTSSSNTPPS PPPQQQQEQY QNTSDTTRSN QQSLSRLSTS FGSNDRSTSS
GAGSLLTSST PTSLTPSSVQ VPPSNSSSAS SSSTSLGSSL SSWVPHSLKV LYHFTAGSVA
ASAASGTGES TVLNPNASGG VLGRLLTSST AQSTLMTRNN LGEQVSWLKR SGNTIAIPQG
PVYPAATSAT GANTSATTSI GAIEDQNNFV YPTSAVTNPN TGGGGRGAGG GPRTFVVPAL
PSPLVPVPAQ QQQQQQQPPL GPPPPPPPPQ QPFINPTSTS THTTPRYTKS TPTTNTSSTT
NDARPATRQQ IAPEVGSTDQ DTVGGVGGMA KLSVKNILPR PHLVSLSSST GSGSGTSASG
RRQKHHSSSS NNNSNSSNNN NNNNSQQQQQ QQQAQQHAHT TSTYAQRPEP TPQQRRPPQN
LLTPASTTGA ASVGPLQRAY SASLASRQSP STNLICPKTD SSAPQALHLK NKQNIRNPAP
TPDSPIVDDH IFSDAVDLTE EFDDDRDVKD KEHTDNDDTV ASSSLTGFGD DKLLWREEFA
ERATPAGESQ RGGSRPRQVK KRKISNDYSV KDEEVSLFDD DDNEEDEFMD INDLVEGDQQ
STPKPKATSR SVSMRLPPTV SLQRGRSPKR KEASFEKRTA TEDQQVERYE EPSFLSSPNV
DNSRKRKSSE SPKGLRTPRP RTKQTEDIPA TTTTKKPRRS EVMDSEDEAF TPLSAGSPLR
SGGTTARELG LDEDTIMDTP SRPPVESTLP TLPTLPTLES VESRPPPPTM DLPSRKPLEP
LNTSRDQLLE SVERPSQQSS VGPSFTAAIT IGQSFAQSST LAESSLPPSM PPPSEDPLNT
RENSNLEEFD YQLHKPLLEQ FVRRPTILER ELSAVNNELQ ENMLKMRDCL RLPRDERDRA
REEVKKEKEM LKRRDIALKA LQEEHKAYLK KSKERQAIED EISRAYAEEN DEYEDQLMVQ
LDKLSDEVEA IERSLTLNIV AAGITERSFN FKEEEEMKPI IIATPTPSRR TEPPVLPSTE
YHNSQQVILQ TQHPAMQPAA QRMPPPPTPS FQTARQIPLS YQHRPTNNSF PDISAEEAMM
FEEEDPFMEE QHPPPSAPFQ ATLPQRNSPF KNVPHKPIHG HDYFDDEDDD ADLLAAVDSV
ETYTSTATHT NNQSRSRSVM STSTATTIKP RKRNEKANTK KAKPRQAELS MPPDKMKFPW
SNDVRKALKD RFRMAGFRQN QLEAINATLG GKDAFVLMPT GGGKSLCYQL PAVVKSGKTR
GITVVISPLL SLMLDQVNHL KNLMITAYAF NGDMNAETRR MVFQKLDTPH PEHELQLLYV
TPEMVSKNMQ FVGKMGDLYQ RNKLARIVID EAHCVSQWGH DFRPDYKAIG EFRKRFPGVP
VMALTATATH NVILDVKHNL AMDTCETFSQ SFNRPNLYYE VRLKEQNLVA RIAELIQEKY
DGQTGIIYTL SRKSAENIAK NLEEKHGIRA KHYHASITTE EKIKVQHDWQ AGDVKVVVAT
IAFGMGIDKP DVRFVIHQHI PKSLEGYYQE TGRAGRDGKP SDCYLYFAYG DIQSLRRMIA
EGDGDYEQKE RQKHMLNMVV NYCESQHTCR REEVLRYFGE EFDFRKCKDG CDNCRYGRIT
KSTEMRDFTE IALATIEVVK SQKTLTLGKL CDILMGKKKN EHAGICHFGI AKGSTQRELQ
RIVLQLNFHK ALGEKNIMNG AGMPITYYVT GPEAGAYLYN GKRLLLPVPS NKSVEPPSRS
KQRRGRVDED MTMDEPEPPT LPPLRRPPTS TNVSSPVRTT KKRTATGKVL PTLMADYEEP
SSDGPHGPLH ANGYERDDFV VSDRVEPDDE EEEAFEPVRP SRRGPSSRAT RPQHRQTTLY
DTLSHTQQHS NESMSQHLAT LGPPIRDPRT MQNPRYAQLD EVHQDIVDTF VEEAKIFEED
FRNKKGMRKP IFTETQYREM AIRWTRTLEQ MRAIPDINQD KVDLYGAKFI PLVERFYGNY
RDMMGPKYDN PFVTDGAEED QSGRNGRGKA GNKKGGGKEV VDLISSDEED GLPPARTASS
RNPAGRGQPQ PTGTRGLTQT QTQTQGRTQD KGRAVNRRGE PIQEAEEEDY GLSDLDEAID
PDATTASDNS DEEDEDSDLE ASRYFSGPTS TGPPVSKAVQ DARLRELQGM YGGSSKSSGG
YGAGSGRASG GSSSRASGSG GRGGGGKKFY RKKRAGSSVA GAGGVTKRKA SRKRGASTAP
KTARGGGAGS RGGGAGGGAG GGKRSGGGGS YGSYGGGGYG GGGGGGGMGG IGVMPH
//
