ID A0A074XGL0_AURPU Unreviewed; 1446 AA.
AC A0A074XGL0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M438DRAFT_338285 {ECO:0000313|EMBL:KEQ81192.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81192.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ81192.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81192.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL584993; KEQ81192.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XGL0; -.
DR HOGENOM; CLU_001592_2_0_1; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 310..514
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1109..1147
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1216..1371
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1164..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 802..829
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1446 AA; 162122 MW; 9271BBB4579A5BCA CRC64;
MASTVNTGVS SAVLKSQTPK QNLIAQGAEA FPAFFDNCRD AFQLEYSGRP RKRARLEDSV
ELSHSPLGSG ITIARVEIHL QQTSDAARHV GTSTVLEDDI EVGLVDSHGL DTSKPFFTLV
GHVGYKKSPL LEFRTTTSLL PDTVNLLSRV KSLEKRSRRN VRPGVCHSTC RLHQSNGPSG
PTYTLECSII WLNGESAFGA AAKKEDWDTL TQFYPEVKNN QSKSWTPQEF YSSVHSPSVD
APESELTKRK VLETDLYPFQ RRAVTWMLDR ESSNQESSRS RLSFTPAKDI NGQPCFVSHL
EGVICSASHL STFDEPKGGI LAEEMGLGKT CELIALISLN QRDSLDTNTV HANTIPALTK
SRATLIVTPT TILQQWMDEL ARHAPSLSVL HYKGVSDPAL TKKGAMPILE DFAQRDVVIT
TYSVLAKEVH YAVDPPERSL RQRERKHTRP RSPLVQTHWW RVCLDEAQMV ESGVSAAAQV
ASLLPREHGW AVSGTPLKKD VQDLFGLLVF LGYQPFCDSS AIWKRLIHQY GDLFKTLFGR
ITLRHTKDQV RHELRLPPQR RVVLTLPFTQ VEEQNYKTLF EEMCEECGCR PDGSPLNDDW
NPESPALLQN MRAWLCRLRQ TCLHPQVGGR NRKALGRGQG PLRTVAEVLE VMIDQNETSI
RTESRLAITT QLLRGHIIGN AKDDDHRAEK ALEIYKSALE KSEAIVAECR VEVSRAIARR
SDAEVTHNGI GGEESTEETS EGRSKVSLYS ALQLQHACAF FIGTTYFQMK SNTRITEPDS
KQFRDLEEQE SWYYDAAKLI RKELLSEDSA KAEELMRSIE QEKDDVILEP TKLTAMESPG
GVENVKLVHK ARDLASILNA QAELIEEWRA KVIELLLKPL IDKDEEGVET TGEEYEDSTK
SQDTLNAYLD ALRAVIADRS TCITGQSAPL VDQEMKHLTQ MAKLGNGHAP ELILELLAKR
NGLKQKPDDL LSLRGLVHEV RGIETALDWQ EGNARVRAEL HIIRDQAKQF AAITQEESDL
LKRLDEMIEL FSATMNQRLE FYRQLQQISD TVAPHKDDWD DTLDVAALEA ATRRQEQQTR
SLQTLKTKNR FLLHLRDEST NSDETQRICV ICQSSFEQGV LTVCGHQFCK ECISLWWSAH
RTCPVCKKRL VLADFHQITY KPQELQAQEE RSEPSSPGQS SSKISTESLY ADIGNDTLAQ
IKSIDLNGSF GTKIDTLARH ILWIRKNDPG AKAIVFSQFR EFLDVLGTAF KQFGVGYSRM
GKPGAVDRFK NDASIECFLL DAKTDSSGLN LVNAQYVFLA EPLINTAIEL QAIARVHRIG
QKRPTTVYMY LIGDTVEEAI YEISVARRLA HMQKRDQRRS KSTTPALGEA AIDAANSLEL
QQAPISKLLA QGNGGGELVP NDDLWSCLFS RAAKSQRQQT VVSAEMEAEV GRHLRQEAAE
NRRDGV
//
