ID A0A2B7XG84_9EURO Unreviewed; 1501 AA.
AC A0A2B7XG84;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=E3 ubiquitin-protein ligase SHPRH {ECO:0000313|EMBL:PGH07628.1};
GN ORFNames=GX51_01637 {ECO:0000313|EMBL:PGH07628.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH07628.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH07628.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH07628.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PGH07628.1}.
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DR EMBL; PDNC01000013; PGH07628.1; -; Genomic_DNA.
DR STRING; 2060905.A0A2B7XG84; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000224080; 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; SM00490; HELICc; 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 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:UP000224080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 328..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1129..1167
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1234..1389
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 720..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1501 AA; 170428 MW; 61101748DF80CE39 CRC64;
MSIIKDVVFV SGPVPDTLQA CFTKPKQQDP AETAPGKRRK LNTGIWDSQD IGASLFPGYL
TLAHIELKIT FSSPALDIHA ISSDHEDGIA IKGPLKVIPE WDPKLPPEPP IKQYKIKLET
NTSDIILQET LDFYPRNHDP LIAARLPSIY RTRSSPYALS MSTLRRVEGD QLSFILETKV
FWKDTLKLGK RGPLQNAAFS TYLPGAPKER PPQPFRRKDW RQRRVKETTW SPSDFYGSVH
VPPKNLDLPP STIADVVNCQ LFPFQRRAVR WLLEREGVEL LPDGRIRELP PSPGSNLPDS
FSEITDADGH ICYMSHLFYV LASDLKGWSS TKTLKGGILA EEMGLGKTVE MITLISLHRR
PAPEARLPIL RQWPALTESG ATLIIIPNTL LDQWKQELSS HSPHLRCTYY KGINRTKQSD
EQLVETLASS DVVFTTYNVL QREIHYAEDP PDRSLRSEKK VIPRKSPLVK ISWWRVCIDE
AQMIETGVSH AARVARLIPR HNAWAVTGTP LRKDMNDLLG LLAFLRIYPL CDWLDAWVRL
YEIHKPLFKE IIGRIVLRHN KDMIRDELHL PPQKRIVITI PFTAVEEQHY DQLFEQMCEE
CGVDALGAPR TGDWDPNSKS TIETMRRWLT RLRQACLHPE VGGAGRKAFG ASSGPLRSVA
EVLEVMIEQN EHRIRTEERS LLLAQIHRGQ LLENAGQPKE ALKVWQSALA LAEANVKDSR
VQLENERNKE QSTGPEVARN TLNDEDDGEE GKGEKNIRLA TYRNRLRSAL EIEHICKFFI
ANAYYQIKTS TELTTPDSEE FFALEKLEVA NYEAAKLIRK EMLAEIDQRV SRSIRQLQAK
VNSTGLVQIP KMSPRLDFSG MESGRLLDKL ESLCEAINKL TQQFIEWRTH SLKLLLEQLV
DEEDNNANLE GNEYESSTQH QDEMYVYMEG LRTLFADYHD AITGQKNPLI EYDVKRGLER
ADKGNGPSPK LYISFMKTRE RLKPSDELGS LRGILTELRS LMVSLEWQEV RGSTRARAEL
GIINRILEDL SQMSSDHAKV SSDLDKEVQL FHNVMNQRLQ YYRQLQHISD SVAPYDEESR
GKPLDVALFD NSLMVEQKIQ EQISALRSKY RYLIHLRDES GAEESARTCV ICQSTFEIGV
LTVCGHKYCK DCLRFWWRQH RTCPMCKIRL KSSDFHQITY KPTELVAQEE KSASAHIGSD
HSQKNSIYSD ISSGVLKEIR NIDVEGSFGT KIDTLGRHLI WLRQHDPGAK SIVFSQYRPF
LEILARAFSY FKIGFSSIDS HDGVERFKND ASIECFLLHA KAHASGLNLI NATHVFLCEP
LINTAIELQA IARVHRIGQH RETTVWMYLV SDSVEESIYD ISVSRRLAHI AQKRKQDGEK
IRKNPLEAGV EEGEENEYEG ASIETVIEAA NSLELQDAKL GNLMAGTAAE GERVPEGDLW
QCLFAKTNRR AKSREDGGNV EAMRNDVDRF LRAEAAEGRI MDAGDGGNGE VLTNGDANAV
V
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