ID A0A0W8C5Z8_PHYNI Unreviewed; 1719 AA.
AC A0A0W8C5Z8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=E3 ubiquitin-protein ligase SHPRH {ECO:0000313|EMBL:KUF79492.1};
GN ORFNames=AM587_10010118 {ECO:0000313|EMBL:KUF79492.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF79492.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF79492.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF79492.1}.
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DR EMBL; LNFO01004808; KUF79492.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8C5Z8; -.
DR EnsemblProtists; KUF79492; KUF79492; AM587_10010118.
DR OMA; PTCVHRF; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR011011; Znf_FYVE_PHD.
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; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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; PS01359; ZF_PHD_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1317..1362
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1418..1576
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 193610 MW; 187F7FCD16F25D36 CRC64;
MPRRKSTPSK RQLTSPPRSV SKRSKRGGQR PAFQRQRTEP LHLSSVATAG GWVKDDVLGL
EIPVDSTISP VLTTLCSDNA PELQIDLTLL ENDQVKLQVK GQADADSHLS LAELFPDTYE
AWKPHIVTLA EGGLLSLHIN AKSEVEKDQW SFSFVVSVAW RKYMESCFPN SLGPMVAVPR
ANPMRPMHRV MIWLLKKTHD AQSQLADVDM TCRCRYWKEI EVLYDRFVGN NTAVSAQFKS
QTFAMPEIYA RIDVTEQLNC DIRDYEAFEA TSADLLPTLR RYQKAAVSWM LSREKPSTQR
NRSLPLCVTF NEGMARKLQA YDPFCAAFYT TAPSTGMLQT HQEQLRPIGM NFSLIHGGIL
ADEMGLGKTV EVIALILSHR PSSLGPRLLS THLSQCQIST TEGDEDSDVV ACICGSSEDH
PMGLVQCEFC DTWHHQLCTG YRVNESNSGS DSFSNSHNLW DFGTDQTVHD ATATWSSGGF
MCYHCQSHER PTFACRTTLI VSPEPIHAQW EHEVSRHVRA GALSVIRYPG VRALKARLED
KGPSAEWQVL ASPGLVLSRY DVVLSTYEAL GADLRYVPTT EGKDRRTSTR SQVKRYAFVG
SPLVALRFWR VCMDEAQVGV ENTRLQAALT LARLSAENRW VVTGTPFSSR VSELFGYLRF
LRIPPYTSSE AEDYRSGQNL QLLQAEHNER EGLDSGFFRE VVEHNFTRGA VERVLDLLLW
NGYDEAGTVC GGGILWRTGK KHVLDQLGLP PQKSEVVWCH FTAVERHFYD QQEKRIVSLI
QQRQQQQQLA QTGQVIDRDD PLWQDLLVLR QLCCHPQVGG ARQAWGSSGN TTSRAVMTMD
AFLQELVNKA KRECEEDQRQ LIGAQNGLAA LLVLKDEISE AALKYMAVMR PIRTNWPHFR
ADLLPRLHIL QNLEKCVRQL YSLPESGTHD DSEALSGMSN TEDPKKVCLL PELPALQRRV
SSTGLLPDSN DLSEEEHTEI SRECALLGQN ARQIRRYYLL QADMMHTRAL TNFKEISQMI
DDSQQHSAGG RTELLCTSGN WWNDALAIIE QSELLLVREL EALAKRRREL FDRLAALSEG
TPTDADVELS GNCKKCRDGG TGPVCIHCQL YKELEAYRRH FLGVDKTISI KTTIVDLFDV
DMEDEDTSND SSGGLSTSLY VEIFKEISGC ARSALRAQED GRELALEIQT GMQTETDFWQ
KLQREWQAAK KLFQAQHQRL GALDELVMAC SQLRLRHPDE PPGRTKAERL YKLERQEIPV
RTAELEAERV AADLVLKNKM AQLRYLLQLQ SESGTRQAQQ AHALEASPES SPVRPLCAVC
LQEFPQRRAV LLCAHVFCTR CVSDLKGGRQ HARKHIRCPT CRRVCPVDNI TVVVEQLASE
STSTRSEDLS QNEAVSEVPR QPALPQRNSG SLGSKLDALL ARVEILRQEN PAVKCLLFSQ
WSQMLELVMQ PLRRVGVRCF MYGTKRQLPK LLEHFQACPA ACVLALPFKV GANGLNIVEA
TEVLLIEPLL SSSIEAQAVN RVHRLGQTRQ TCVHRFIVQG SVEERIFHLG HKLKADNTRE
EQECKEEIND DDEELQRLGV APGRKEQEKL TMQDLQELLR GNSGDSAASA AAATVFWDEL
VTLNGNCVTR TAAYEFLERR HATQIRTEGQ DRSRGPQTKL FGKFVELVVA EELLSLLHTD
ELNSIEAAER IDPQLLHNQQ EQIKEQVCVW RKAQEDDTA
//
