ID G4UAF8_NEUT9 Unreviewed; 2209 AA.
AC G4UAF8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Sec63-domain-containing protein {ECO:0000313|EMBL:EGZ77811.1};
GN ORFNames=NEUTE2DRAFT_101106 {ECO:0000313|EMBL:EGZ77811.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77811.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77811.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL890999; EGZ77811.1; -; Genomic_DNA.
DR STRING; 510952.G4UAF8; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000008513}.
FT DOMAIN 540..723
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 761..970
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1390..1566
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 31..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2209 AA; 250275 MW; 46BB4013EEECF316 CRC64;
MTDHHRDVSQ YKYSAMSNLV LQADRRFVTR RTDEATGDPE SLAGRLSIKD MGSRVARDSA
PKPKKAGAMP DVERGSLREG ADILQREKKK GKLESATRGG GILTGADALI EGLRYRPRTQ
PTRDAFNLIL TIVAEHLGDV PHEVVRSAAD AVLEYLKDDD LKDFDKKKEV DDILGVSMGP
KQFNELINLG KKITDYDAQD EDEDAGDARQ EGDDEIDGRQ GVAVNFENDE DDDGMVDVVR
DESSDEEDFA EDEELPDSNE VVDGEGGQEE MVEDILNGEA MVIDSAPEGK KSGSDDNSIP
ARDIDAFWLQ RQIGRLYPDA HIQHDKTMSA LKTLSGEPDE PGGEEKQLRD IENDLMELFD
YEHHELVQKL IANREKVVWL TRLARAENEE EKNTIKREMA SEGLRWILDE LEGKTDGGQK
KIKMDIKMDI DSGAFADKEG QKPERPEGQL VGGLQPRKLI NLENLIFDQG NHLMTNPKVR
LPEGSTKRTF KGYEEIHVPP PKKRNDPSDA HVPISEMPEW AQIPFSTAKS LNKIQSKCYP
TAFGDDGNML VCAPTGSGKT NVAMLTILRE IGKHRNEAGE IDLDAFKIVY IAPLKALVQE
QVGNFGKRLE PFGIRVAELT GDRQLTKQQI SETQIIVTTP EKWDVITRKA TDLSYTNLVR
LIIIDEIHLL HDDRGPVLES IVARTIRKTE QTGEPVRIVG LSATLPNYRD VASFLRVDTN
TGLFHFDGTF RPCPLRQEFI GVTDRKAIKQ LKTMNDITYH KVLEHVGQNR NQMLIFVHSR
KETAKTARYI RDKALEMDTI NQILKHDAGT REVLSEASNS VNNTDLKDIL PYGFGIHHAG
MSRADRTDVE DLFASGHIQV LVCTATLAWG VNLPAHTVII KGTQVYSPEK GSWVELSPQD
VLQMLGRAGR PQFDTYGEGI IITTQGEMQY YLSLLNQQLP IESQFASKLV DNLNAEIVLG
NVRSRDEGVE WLGYTYLFVR MLRSPGLYQV GAEYEDDEAL EQKRVDLIHS AATVLKKSNL
IKYDEKTGKL QSTELGRIAS HYYISYGSMD TYNKLIQPSI TDVELFRVFA QSAEFKYIPV
RQEEKLELAK LLAKVPIPVK ESIEEPTAKI NVLLQAYISR LKLEGLALMA DMVYVTQSAG
RILRAIFEIT MKKGWASVAK LALNLCKMAE KRMWPTMSPL RQFPNCPVEI IRKAERIDVP
FSSYFDLDPP RMGELLGLPK AGKTVCSLVA KFPRVEVQAQ VQPMTRSMLR IELAITPNFE
WDVDIHGLSE SFWIIVEDCD GEDILFHDQF ILRKDYAESE SNEHIVEFTV PITEPMPPNY
FISVISDRWM HSETRLPVSF RKLILPERFP PHTELLDLQP LPVNALKAKD YSALYPDWQQ
FNKVQTQTFK SLYETDNNVL ICSPTGSGKT VCAEFALLRH WAKKEHGRAV YIAPFQELVD
LRFQDWQKRF ANLRGGKDIV KLTGETTTDL RLLEQGDLIM ATPLQWDVLS RQWKRRKNVQ
TVELFIADEL HLLGGQMGYV YEIIVSRMHY IRTQTELPLR IVGLSVSLAN ARDVGEWIDA
KKHDIYNFSP HVRPIPLELH IQSYSIPHFP SLMLAMAKPT YLAVTQLSPD QPALIFVPSR
KQTRATARDI LTACLADDDE DRFLHVDVEQ IQKLLDRVQE AALAEALKHG VGYYHEALSL
NDKRIVKHLY NNGAIQVLIA SRDVCWELDC TAHLVVVMGT QYFEGREHRY VDYPLSEVLQ
MFGKALQQNK AGRGCGVLMV PAVKREYYKK FLNEALPVES HLHNFLHDAF VTEISTKMIE
SGEDAINWAT FTYFYRRLLA NPSYYSLTDP THDGLSQYLS DMVEATLKDL AESKIIDFDE
DDGTVAPQNA AMIAAYYNIS YITMQTFLLS LTAKTKLKGI LEIVTSATEF EAIQIRRHEE
VILRRIYESV PVKMAEPVFD SPHFKAFVLL QAHFSRMNLP IDLAKDQEVI LTKVLSLLSA
TVDILSSDGH LNAMNAMEMS QMVVQAMWDR DSPLKQIPNF TTEVIKTANK YGIRDIFDFM
EKMNPEENAD YASLVRDLGL SQAQLAQAAE FTNNKYPDVS LEFELEDKDN IRANEPAYLK
INIEREVDED EEFDPTVHAP FYPGKKTENW WLVVGEESSK TLLAIKRVTI GKKLNVRLEF
TVPTPGRHDL KLMLMSDSYV GVDQDPAFSV MVEEGMDVDE SDEEDEEEE
//
