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Database: UniProt
Entry: A0A197K7R0_9FUNG
LinkDB: A0A197K7R0_9FUNG
Original site: A0A197K7R0_9FUNG 
ID   A0A197K7R0_9FUNG        Unreviewed;      2189 AA.
AC   A0A197K7R0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Sec63-domain-containing protein {ECO:0000313|EMBL:OAQ33198.1};
GN   ORFNames=K457DRAFT_256504 {ECO:0000313|EMBL:OAQ33198.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ33198.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ33198.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ33198.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV442022; OAQ33198.1; -; Genomic_DNA.
DR   STRING; 1314771.A0A197K7R0; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000078512; 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; 2.
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; 3.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
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:UP000078512}.
FT   DOMAIN          519..703
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          741..934
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1370..1550
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1580..1791
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          16..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2167..2189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2189 AA;  248681 MW;  7C41F3D01613BEAA CRC64;
     MADKVAKDQQ YQYALNSNLV LHSNRSDNPR RGNEPTGEAE SLYGRIDPKE FGSRAMRDTA
     KIDEAKKKKS EPTEKDLERR KKRAEDKALR SAYGYSSVLA ATEDRESGGY RPRTRETRQT
     YELILTFVQR YLGDVAHDIV RSAGDIVLEI LHTDTLKDFD KKKGVEEVLG PVDSDQFSVL
     LNLGKKITDY APGAEETSTV GQDGEVKNVG DIDEQYGVAV VFDEEEEDED IYSLHSESEH
     EDEDTGLDTA QDVVVGGAGK ANQEEEEEAM EVDEDVAVRV GATEGKVDTS KKLQPHQVDA
     YWLQRFIATF YKDEIVAQEK TDAAMEIIAS ETINMRDCEN ELMALFDYDK FELVSMLTRN
     REVIVWCTRL GKASEQERTE IEANMREIGL DWIIKGLGHQ TGKKSDLRRR GAGQAPTAAG
     PTAVLPKEKG PAPTTSAPRQ LIDLDAMAFA QGSHLMSNKS VHVPEGSFRR QKKGYEEVHV
     PQPKKPTTDR PLKGKDELPA WIQDCFPDGL NQIQTAVYDV AYGSEENMLL CAPTGAGKTN
     CAMLTVLNEI EKHRDPETGV IDKDNFKVVY IAPMKALVQE MVENFGKRLK PFGLSVQELT
     GDRQMNKQQI AETQMIVTTP EKWDIITRKA TDRSYTNLVR LIIIDEIHLL HDDRGPVLES
     IVARTLRHME QSQELIRLVG LSATLPNYID VATFLRVDTN RGMFHFDGTW RPCPLKQEFI
     GITEKKAIKR FQVMNEVTYE KVMEHVVQTE GDQVLIFVHS RKETAKTAQA IRDMALEKDT
     IAHFARPDGG AREILLSEAE QASDPALKDI LPYGFATHHA GMTRPDREAV EELFTAGHIK
     VLVSTATLAW GVNLPAHTVI IKGTQVYSPE KGRWAELSPQ DVLQMLGRAG RPQFDKFGEG
     IIITNHSELQ YYLSLMNQQL PIESQFVTKL ADNLNAEIVL GTIKNRDEAV QWLGYTYLYV
     RMLRNPSLYG VSPDDLDDDP YLQKKRVDII HSAATILDKC NMIKYDKRTG KFQGTELGRI
     ASHYYISHNS MATYNQHLKP MMSHIELFRV FSLSDEFKYI PVREEEKAEL QKWLEQVPVP
     VKESIEEPTA KINVLLQSYI SQLKLEGFAL VSDMVYVTQS SGRILRAIFE ICLRRGWAQL
     TRKALDLCKM VEKRQWLSMT PLRQFKGINP ELIKKIERKE FEWVRYFDLS SQEIGELVGV
     PKAGKLLERY VHEFPKLDLQ SHVQPLTRSI LKVELTITPD FKWDEKVHGT AEAFWILVED
     VDGEMILHQE SFILKQQYAE EEHLMTFTVP LFDPLPPNYF VSIVSDRWLH SETRFPISFK
     HLILPEKYPP HTELLDLQSL PVTALRNREF EEIYSQTLSK FNPIQTQTFN TLYTLDDNVF
     VGAPTGSGKT ICAEFAMMRQ WNKKPVKGVR GRIVYIAPHQ EVVDARRQEW HAKFGDVQGG
     KTILSLTGET SADLKILERG DVILATPGQW DVISRRWKQR KNVQTVQLFI ADELHMIGGD
     IGPTYEVIVS RMRYIASQVE SKIRIVALST SLANARDLGE WIGATSHSVF NFHPMVRPLP
     LDVHIQSYTI PHFASWMIAM AKPTYTAITT HSPEKPVIVF VPSRKQCRLT VTELLTLCAA
     DDTPKRFLHC EEDVLRAHLE HVQDSALASA LEHGIGFFHE ALSKSDKRVV EKLFESGAIQ
     VVVASRDTCW GIPLSSYMVV VMGTQYYDGK DHRYADYPTT DVLQMMGRAC RPQEDESSRC
     VLMCQSNRKE FYKKFLFEAL PVESHLDHFL HDHFNAEIVT KTIENKQDAV DYLTWTFLYR
     RMAQNPNYYN LQGVTHRHLS DHLSELVETT INDLVTSKCI AIEDEMDVSP LNLGMIAAYY
     NINFSTVELF SSSLTPTTKL KGLLEIISTA AEYESIPIRH HEDQVLKRIY ERLPVKLSNV
     KFNSPHHKAN ILLQAHFSRT QLPADLASDQ ALVVGQVIPL LQACVDVISS NGWLPPALAA
     MELAQMSVQA MWDRDSPLKQ IPYMTNERVK RCEAKGVESV FDIQDLEDKD RDAALQVDER
     QMRAIAAFVN RYPSIEAEYG IEDENDIKAG QPVVIEVQLE RDGDEDDGEL SSVPAPFFPG
     KKDEGWWIVV GDPSTKTLLA IKRITLQRKL RVKLEFVCPR AGNQTYKLYT MCDSFLGCDQ
     EFDLELEVGE AEDDSDEEDE EDSDVEMQE
//
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