ID C1G9L6_PARBD Unreviewed; 1489 AA.
AC C1G9L6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PADG_03952 {ECO:0000313|EMBL:EEH47868.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47868.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47868.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47868.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN275960; EEH47868.2; -; Genomic_DNA.
DR RefSeq; XP_010759252.1; XM_010760950.1.
DR STRING; 502780.C1G9L6; -.
DR GeneID; 22583163; -.
DR KEGG; pbn:PADG_03952; -.
DR VEuPathDB; FungiDB:PADG_03952; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_1_1_1; -.
DR InParanoid; C1G9L6; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000001628; 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; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000001628};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1127..1165
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1489 AA; 169581 MW; 6497FFAB2A0EF024 CRC64;
MSIIIDEVVA SGPVPETLHA LFTKGEAPDI IREHPGKRRK LDEAQPSYED IAANLLSSYL
TVARFDLKIR FSSSSLSSGS ISSKRGSDNQ RKVPVFIKRA RFVGTSFESS ARQCHLRIAT
NQRDIVLDKT LDCSTCRIDL AIPGFLPSIY RSRSKFPVAC YMSTLRKAES DELSFILETK
ILWKDSIKFE RISNDALLPF SRYLPQNPQE PPVKTQFSHG RSIKECSWSP SEFYESVHVP
LKTLDLPSSA LSNSLQCQLF PFQRRAVRWM LEREGMEILP DGEIRVRPPS LSPGLPDSFE
QIKDADGRTC YASHLFRILT TDLRNWIPVE RTLRGGILAE DMGLGKTVEI IALICMNRRP
APPGGFPVLR QWPTLTESGA TLIVTPPTIL KQWQQEISSH APSLRCIYYE GLNRTKMGNE
ELVVDLASCD VVLTTYNVLQ REVHFAEEPP KRSLRHKKKV LPRKSPLVQI SWWRVCIDEA
QMIESRVTNA AKVARIIPRH NAWAVTGTPL RKDMDDVLGL LLFLHYYPLC NSLDTWIRLY
GNHKSLFKTI IGRIVLRHNK TMVRDELHLP PQKRIVITIP FTAVEEQHYD QLFEQMCDEC
GVDRSGAPST DEWDPDSKSL IEKMSHWLRR LRQACLHPEL GGDGRKTLGA NSGPLRSVAE
VLEVMIDQNE ARIRTEERSL LLSQIRRGQL LENAGRPREA LNIWQKALVL AETNVHESRT
QLENERKKEQ SAKLNGVHNI SDDEDDIDEG KGEKNSGLGA YRLRIRNALE IQHICKFFIA
NAYFQIKTNT ELTNPDSEEF IALEKLEEEN YEAAKLIRKD MLAEMDRRVN RYIKQVQVKV
YNNDLVHIPK MSVRLDISGM ESRRILDKLE NFCDAVNNLT LQYTKWRNHI VKLLLKPLID
EDDNAKLEGD EYESSTKHQD EMYVYMEALQ TLFADYHDAL TGQTNLLVAN EVKLGLNRAR
DGNGPAPELY ISVMKMRENL KIPKDLGSLR GIIGELRSLM VSIEWQEARG SARAHAELGI
LNRILQDSSQ TSSEHSKISS NLEKEVELFR NLLNHRLEYY RQLQHISDTV APYDEESRGK
PLNVALFDSK LEFEHNIQAK ISAFKSKYRY LIHLRDEAGA DESTRICIIC QSTFEIGVLT
VCGHKYCKDC LRFWWRQHRT CPMCKIHLKS NDFHQITYKP TELVAQEEKS TDHFVPDNLT
KNSIYSDISS GVLKEIRNIE IGGSFGTKVD NLARHLIWLR QHDPGAKSIV FSQYKPFLGI
LARAFSHFKI GFSSIDYHDG TERFKRDPSI ECFLLHAKAH SSGLNLVNAT HVFLCEPLIN
TAIELQAIAR VHRIGQHRET TVWMYLVSDS VEESIYDISV SRRLDHISRK RKEEENAYNH
VSRMGEGEET TSESMETVIE AANSLELQDA NLGNLMAGTA AEGERVPEGD LWQCLFAKTS
RGKSTGNGGN TEALQNEVNR LLRAEAAEGR IEEAVNGEVL TNGDTSADL
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