ID H0XG71_OTOGA Unreviewed; 1688 AA.
AC H0XG71;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=SNF2 histone linker PHD RING helicase {ECO:0000313|Ensembl:ENSOGAP00000015061.2};
GN Name=SHPRH {ECO:0000313|Ensembl:ENSOGAP00000015061.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000015061.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000015061.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAQR03075570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000015061; -.
DR Ensembl; ENSOGAT00000016826.2; ENSOGAP00000015061.2; ENSOGAG00000016815.2.
DR eggNOG; KOG0298; Eukaryota.
DR GeneTree; ENSGT00730000111123; -.
DR HOGENOM; CLU_001726_1_1_1; -.
DR InParanoid; H0XG71; -.
DR OMA; VKQAHQQ; -.
DR TreeFam; TF324273; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd00073; H15; 1.
DR CDD; cd15547; PHD_SHPRH; 1.
DR CDD; cd16569; RING-HC_SHPRH-like; 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; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR048695; SHPRH_helical_2nd.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_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; PF00271; Helicase_C; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF21324; SHPRH_helical-2nd; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 439..513
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 1437..1484
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1519..1677
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 193690 MW; AD91882A397D5F54 CRC64;
MSSRRKRAPP VRIDEEKQQQ LQWNMHEDRR NEPLTLSDEE FPCLGSDATS AHCIILDDSP
EEEVAHRDKK RCAEAVSILK SIKKEESVGI FSPLSVKLNV LITPYHFDNS WKALLGELTL
QLLPEQSLIE RFSERSFTLM SSESSSHFLI YVHSKCEEVE KKQKGVNKPI HIREKSLLVE
SSFSGEMLED LGWLQKKRRI KLYQRPEGNH IIKVGIYLLE AGLAKLDFLS DASSRMKKFN
QLMKRVMEKL YNFIVLDVLE EDDEDSESES EGQDIDELYH FVKQTHQQET QSIQVDVQHP
ALIPVLRPYQ REAVHWMLQQ EHFRSTPSGG NTLHFLWREI ITPEGLKLYY NPYTGCIIRE
FPNSGPQLLG GILADEMGLG KTVEVLALIL THTRQDVKQD ALALPEGKVV NYFIPSHFGG
KVKDTESQNI EIEPKEKIQF PPTRVMLLTA VKEMNGKKGV SILSIYKYVS STYRYDVQRN
RSLLKRMLKC LIFEGLVKQI KGHGFSGTFT LGKNYKEEDI CDKTKKQVAG SPRKIQRESR
KSGNKDTDSE YLPSNTSDED DPYYYYYKPK RNRSKWRRKP VLSAKKGKSQ PNINSDSQGH
CPATSDSGIT DVTSSQSTSV SEFKQEHEAK DCAESLNPAG SDMPPSNIMS PCNTSDYRFE
CICGELDQMD RKPRVQCLNC QLWQHAKCVN YEEKNLKVKP FYCPHCLVAM EPVSTRATLI
ISPSSICHQW VDEINRHVRS SSLRVLVYQG VKKDGFLQPH FLAEQDIVII TYDVLRSELN
YVDIPHSNSE DGRRLRNQKR YMAIPSPLVA VEWWRICLDE AQMVECPTVK AAEMAQRLSG
INRWCISGTP VQRGLEDLFG LVVFLGIEPF CIKHWWIRLL YRPYCKKNPQ HLHSFIAKIL
WRSAKKDVID QIQIPPQTEE VHWLHFSPVE RHFYHRQHEV CCQDAVVKLR KISDWALKLS
SLDRRTVTSI LYPLLRLRQA CCHPQAVRGE FLPLQKSKFK ESAFSFSTMT MEELLTSLQK
KCGTECEEAH RQLVCALNGL AGIHIIKGEY ALAAELYREV LRSSEEHKGK LKTDSLQRLH
ATHNLMELLV AKHPGIPPTL RDGRLEEEAK QLREHYMSKC NTEVADAQQA LQPVQQTIRE
LQRKIHSNSP WWLNVIHRAI EFAVDEELVQ RVRNEITSNY KQQTDKLSMS EKGLQFLLTT
QMEELNRFQK LVREAVKNLE RPPSRNVIES ATICHLRPIR LPLNCCVFCK ADELFTEYES
KLFSNTVKGQ TAIFEEMIED EEGLVDDRAP TTTRGLWAIS ETERSMKAIL SFAKSHRFDV
EFIDEGSTSM DLFEAWKKEY KLLHEYWMTL RNRVSAVDEL AMATERLRVR DPQEPKPSPP
VLHIIEPHEV EQNRIKLLND KAVARSQLQK KLGQLLYLTN LEKSQDKTSG GVNPEPCPIC
ARQLGKQWAV LTCGHCFCNE CISIIIEQYS VGSHRSSIKC AICRQTTSHK EISYVFTSEK
ASQEEDIPVK GSHSTKVEAV VRTLMKIQLR DPGAKALVFS TWQDVLDIIS KALTDNNMEF
AQISRVKTFQ ENLSAFKRDP QINILLLPLH TGSNGLTIIE ATHVLLVEPI LNPAHELQAI
GRVHRIGQTK PTIVHRFLIK ATIEERMQAM LKTAERSHTN SSVKHSEASV LTVADLADLF
TKETEELE
//
