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Database: UniProt
Entry: A0A165NUM7_EXIGL
LinkDB: A0A165NUM7_EXIGL
Original site: A0A165NUM7_EXIGL 
ID   A0A165NUM7_EXIGL        Unreviewed;       572 AA.
AC   A0A165NUM7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KZW01246.1};
GN   ORFNames=EXIGLDRAFT_830205 {ECO:0000313|EMBL:KZW01246.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW01246.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW01246.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW01246.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR   EMBL; KV425895; KZW01246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165NUM7; -.
DR   STRING; 1314781.A0A165NUM7; -.
DR   InParanoid; A0A165NUM7; -.
DR   OrthoDB; 206891at2759; -.
DR   Proteomes; UP000077266; 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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032423; AAA_assoc_2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR   PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16193; AAA_assoc_2; 1.
DR   Pfam; PF12002; MgsA_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000313|EMBL:KZW01246.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          13..36
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000259|SMART:SM00734"
FT   DOMAIN          153..271
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          40..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  62420 MW;  AA9B29124C5FA2AB CRC64;
     MSFKNGAKIR PRFVPCPVCA VQVAEDAIND HLDSSACKLD STQDTVPSSS QSSTATKVGV
     KTPAKKPLAP IFSSAKRERE PPVPSSTFKS TQQRAVIDVD SDQQQPPAKR QKTTAENLQA
     AQPLAARLRP TTLAEFVGQQ HIVGSDSLLL SNSTGSVILW GPPGCGKTTL ARLLAQDSGA
     TFKELSATSS GAAEARSVCE EAKGALKMKG RRTVLFLDEI HRFNKAQQDV FLPYVEAGHI
     RLIGATTENP SFKVNGALIS RCRVFVLERL TSEDVTTILS RALERHNSAL SSADTTPPPE
     PIVMSDPVRD TIVALASGDA RTALSLLELV ITSLSQTPAR RPTEANLIHH LKRSVATSYD
     RTGDDRYDLI SALHKSVRGS DGSAALYWLA RMLTAGEDPL YIARRLIVMA SEDIGLADDA
     CLSLAIATHT ACQTVGMPEC RINLAHCVAR FAEARKSTRS YEAYNRAEEV AKKDPGAPVP
     MHLRNAPTGL MKGLGYGKEY KYNPAFAHPV FQEYLPVEAL ENAGVEESER EFLRKDEAEA
     KKDKVWNNSM LEQWEWFKNG GQAWEGRPLE EK
//
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