ID A0A2B7WRR2_9EURO Unreviewed; 1486 AA.
AC A0A2B7WRR2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ79_08569 {ECO:0000313|EMBL:PGG99302.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGG99302.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGG99302.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGG99302.1,
RC ECO:0000313|Proteomes:UP000223968};
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:PGG99302.1}.
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DR EMBL; PDNB01000206; PGG99302.1; -; Genomic_DNA.
DR STRING; 1447875.A0A2B7WRR2; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000223968; 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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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; 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:UP000223968};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1125..1163
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1229..1381
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 722..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 168929 MW; 54A5BE3CDBA89D4A CRC64;
MSVVTCEASV SGPVPEALTA LFVKKEGADT STEPPGKRRK LGRTNVSYID NDVDHLPGYL
TLARLVLKIT FSSALRNGNT LSLGQENCSR MAIPVFIKGA HMQPAPTPSP VRKFDLRLAI
NQSNVIFDET LVYDTRQGDF PVPSQIPSAY RSRTTSPVTC SMTTLRKCED NESSFVLDSK
VFWKDTIKFE NINPTALQTF LLYLPKKPQD PREQFHFGRL IRKDNNWSPS EFYDSVHVPT
KFFDLPSSAI PDSVQCQLFP FQRRAVRWLL EREGMEVLPD GQVQGRRASS ESRLPDLFSK
IQDADGRICY ASRLFRVLTT DISEWSSIER TLKGGILAEE MGLGKTVEII ALICMNRRPK
PSGGLPVLRQ WPALTDSGAT LIITPPAILE QWQQEISSHA PSLRCMYYQG INRTKLDNEE
LVKELASCDV VLTTYSVLQR EVHYAEDPPA RALRHAKKIL PRKSPLVQIS WWRVCIDEAQ
MIETGVSNAA RVARIIPRQN AWAVTGTPLR KDMTDLLGLF LFLHYYPLCY SLDTWIRLYS
NHKPLFKEII GRLVLRHNKD TIRSELHLPP QKRVVITIPF TAVEEQHYDQ LFEQMCDDCG
LDTSGGPLTE DWDPNSRYTI ETMRQWLTRL RQTCLHPEIG GGNRKALGAH SGPLRSAAEV
LEVMIDQNEG RIRAEERTLL LSQIRRGQLL ENASKPQEAL ELWQAALTLA ESNVRDSRIQ
IDNERKRQHS AEPNGVQGLT EDEEDIDGKD EKGTGLGSHR HRLRSALEIE HICKFFIANA
FYQIKTNTEL TKPDSDEFYS LEKLEGQNYE AAKYIRKEML AEISRRVSRS IEKVQAKVDD
DSFVKVPEMS PNLDISGMES RRLLDKLGDF CEAMNKLTDQ YLEWRKHMVK LLLQSLIDEE
DDAKLEGDEY ESSTKHQDEM YVYMEALRAI FADYHDAITG QTNALIASEV KRGLEQAQIG
EGPSPELYIA LMKTRKNLII PHELGSLRGI LTEMRSLKVS VEWQEARGSS RAHAELGIIE
RILEDTSQIF SEHSKTSSNL EKEVELFRDV MNQRLEYYRQ LQQISDTVAP YDEESKGKPL
DVALFDSKLD YEDKLQAKIS ALKSKYRYLI HLRDESGAEE STRICIICQS SFEIGVLTVC
GHKYCKDCLR FWWRQHRTCP MCKMRLKSND FHQITYKPTE LVAQEEKPIA HYGSDHSVKN
SIYSDISSGV LKEIRNIDIG GSFGTKIDTL ARHLIWLRRH DPGAKSIVFS QFKPFLDTLS
RAFSHFKIGF SSIDSRDGIE RFKRDPSAEC FLLHAKAHSS GLNLVNATHV FLCEPLINTA
IELQAIARVH RIGQHHETTV WMYLVSDSVE EAIYDISVSR RLAHIARKQK EEEKSHSHDS
GIDEEEAQSE SMETVIDAAN SLELQDAKLG SLMATSAAEG ERVPEDDLWQ CLFAKTGKWK
SRGNSENSEL MQNEVNRLLR ADAADGRIEQ AENEQVMANG DATACL
//
