ID G7E1X1_MIXOS Unreviewed; 2188 AA.
AC G7E1X1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Sec63-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Mo03557 {ECO:0000313|EMBL:GAA96884.1};
GN ORFNames=E5Q_03557 {ECO:0000313|EMBL:GAA96884.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA96884.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
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:GAA96884.1}.
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DR EMBL; BABT02000108; GAA96884.1; -; Genomic_DNA.
DR RefSeq; XP_014567162.1; XM_014711676.1.
DR STRING; 764103.G7E1X1; -.
DR GeneID; 26263496; -.
DR eggNOG; KOG0951; Eukaryota.
DR HOGENOM; CLU_000335_1_0_1; -.
DR InParanoid; G7E1X1; -.
DR OMA; QTEIQYY; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000009131; 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; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
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:UP000009131}.
FT DOMAIN 525..709
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 720..936
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1375..1551
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 224..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2166..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2188 AA; 244979 MW; 97F196BF79C11322 CRC64;
MAGKDFSQYQ YNAMSSLVLS ADRSAIRQRQ DEPTGEPETL VGRIDPKAMG SRITRDTANV
DKKKRKAVTA AASASADDEI ALLERKKRAK ASSGAMSSGY RDIVDATDET EGIRYRPRTT
ETREIYQLLL STAAAILGDQ TAEVVRSAAD LALETLKDAN LKDFDKKKEL QELFGATLTT
AQFTDLINLA KKITDYNADE TDEAALRNRE GEIDDEQGVA VVFADEDAED DEEGGYVVRD
GESADDDDGV EDSDNAIDED DGQPGLLDGD GQDDDVVIGG TNGQTGAATD GKSSSSTIIE
RIHARQIDGF WLQRLISQSY ADPQEATTKT SEAMDILSAE QSTGECENAL VTLFDFEHFD
LVATLVRNRD VIVWCTRLAR ADDDEKVDVE VAMRERNLGY ILKELRGGAI TNGATKPATN
GKAIIDIPKT ANITAGSLVQ PRKALDLEAL AFAEGSRLMS NKKIKLPEGS IKRTKKGYEE
IHVPEPKPAP AVEGEKVMID ALPEWTRPAF AGAVSLNRIQ SRLYPVAFGD DEPILLCAPT
GAGKTNVAML TILNEIGKFR DESTGEIDYN AFKIVYIAPM KALVQEMVGS FGKRLEPFGI
QVSELTGDRQ LTKQQIAATQ IIVTTPEKWD VITRKSTDTS YTNLVRLIII DEIHLLHDDR
GPVLESIVAR TIRRMEQTQD YVRLVGLSAT LPNYHDVARF LRVNPNKGLF YFDATYRPCP
LRQQFVGVTE KRAIMRYQVM NEVCYEKVLE QAQAGNQTLV FVHSRKETAK TAKALRDAAV
ERETITAFIQ SGGGERLVLE EEASKASDPN LKDLLPYGIA IHHAGMNRID RGTVEELFAE
KRLKVLVCTA TLAWGVNLPA HCVVIKGTQI YNPEKGRWVE LSPQDTLQML GRAGRPQYDK
YGESVVITNQ DQLQYFLSML NQQLPIESQF QGPKLADNLN AELVLGTIRN RDEGVAWLGY
TYLFTRMLGS PALYGVPADY EEDDPSLIQY RADLIHTAAA SLERAGMLRY DRKSGEMFTN
DIGRVAAHYY INVASMSTYG KHLKPDINMI ALFRIFSLSE EFKLIPVRQE EKPELAKLIE
RVPIPVKESI DEPSAKINIL LQSYISQLKL DGFALVADMV YVTQSAGRIL RAIFEICLRR
GWAALTHQAL ALCQMVEKRM WPSMTPLRQC KGVTADIIRR AERKEFPWYR YFDLEPPELG
ELMGRAEIGR AVHNLVHQVP RVELSAHVQP ITRTMLRIEL TITPDFQWNE RAHGGAESFW
ILVEDVDGEV ILFSDQFLLR QRFAQEDHFV TFTVRLLEPL PPNYFISVIS DRWMASETRL
PISFRHLILP DKFPPPTPLL DLQPLPISAL RDGEYSAVFQ REFNDFNKIQ TQCFQALFTS
DDNVFVGAPT GSGKTVCAEL ALMRLWSQSE PGRAVCIEPY PDVVETRVAE WQNRLGKLRG
GKNIAALTGE TSTDLRILSE SDLVICTPTQ WDLLSRRWKQ RKNVQQIALL IADELHLIGS
EIGPTYEIVV SRTRLIGAQT EHKTRIIGFG ASLGNARDLG EWMGANSQTI FNFSPGARPL
PLQVHLQSFN VPHFPSLMLQ MAKPAYLAII EWAEARPVIA FVPSRKQCKL TATDLLTYCL
ADEDQNRFLN ADVTELESTL ELISDEDLKD TLRHGIGFYH EGLSKRDRKI VEQLYGLGAI
QVIVASKDTA WSIPMKAHMV VLMGVQTFEG KEHRYIDYPF ADVLQMMGRA CRPAEDTSSR
CVLMCPQVRK EFFKKVLNEG LPIESHLHLS LADHLNAEIV TKTVENKQEA LDYLTWTYMY
RRLAANANYY NLQGVSHRHI SDHLSELVES TVSELSASKC LQVDDDMDLS ALNLGMIAAY
YNVRHITIDI FSLSLTERTK LKGLLEIVSS AAEFEDVPIR HREDLLLQKI YDRLPVKLAS
PDFDQPRIKT NVLLQAHFSR LRLPADLASD QLVILGRVLN LLSAMIDVMS SSAYLNATYC
VDLQQQVVQA VWRSNGPEPV LKQIPHFTPE VIKRFVDAGV ESVYDLIDLE DDDRDKLLQM
DNKQKSAVAA FVNAYPSLEV TKEVIDESDL SAGAPITVMV TLSRGEDEEV SSVVAPFFPL
PVSEQWWAII GDPKTNNLLS IKKTALISAQ TLKLEFILPQ GHHELELSVL CGQYIGCDQS
FELSLDVKEG QDSDEEDEEE EDEEMEDA
//
