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Database: UniProt
Entry: A0A2Y9SIK5_PHYMC
LinkDB: A0A2Y9SIK5_PHYMC
Original site: A0A2Y9SIK5_PHYMC 
ID   A0A2Y9SIK5_PHYMC        Unreviewed;      1676 AA.
AC   A0A2Y9SIK5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=E3 ubiquitin-protein ligase SHPRH isoform X2 {ECO:0000313|RefSeq:XP_023978283.1};
GN   Name=SHPRH {ECO:0000313|RefSeq:XP_023978283.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023978283.1};
RN   [1] {ECO:0000313|RefSeq:XP_023978283.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023978283.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_023978283.1; XM_024122515.3.
DR   Proteomes; UP000248484; Chromosome 10.
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:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
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          1433..1480
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1515..1669
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1676 AA;  192822 MW;  FDE9FAEB9D4CBA95 CRC64;
     MSSRRKRAPP VRVDEEKQQQ LRWNMHEDRR NEPLTLTDDE QSFPGLDSSS AHCVILDDSL
     KEEVAHKDKK RCSEVVSVSK SVEEETSGIF SPLSLKLNIV ISPYHFDNSW KAFLGELTLR
     LLPEQSLIEN FSERSFTLMR SESSYQFVIY VHSECEDVEK KERGLNEPIS ICDKGIQVES
     SFSGEMLEDL GWLQKKKRIK LYQKPEGNHI IKVGIYLLEG GLAKLDFLSD ANSRMKKFNQ
     LMKRVMEKLY NFIIPDVLEE DEEDSESEPE GQDIDDLYHF VKRTHQQETP SNQVDVQHPA
     LTPVLRPYQR EAVSWMLQQE HFKSTPASEN ALHFLWREIV TSEGLKLYYN PYTGCIIREY
     PNAGPQLLGG ILADEMGLGK TVEVLALILT HTRQDVKQDA LTLPEGKVVN YFIPSHYSGG
     NVKNTETQNM EFEPKEKVQC PPTRVMILTA VKEMNGKKGV SILSIYKYVS SIYRYDVQRN
     RSLLKRMLKC LIFEGLVKQI KGHGFSGTFT LGKNYKEEDI HDKTKKQAVG SPRKIQKESR
     KPGSKDTDSE YLPSNTSDDD DDPYYYYYKA RRNRSKLRKK PVPSTKKEKS QLNINLNSQD
     HCPATGDSAV TDVTTSESTC VFEVKQKHAA KDQAESLNPV GHDMPHSNIT GPYKSSDYHF
     ECICGEVDQV DRKPRVQCLK CHLWQHAKCV NYEEKNLKIK PFYCPHCLVA MEPVSTRATL
     IISPSSICHQ WVDEINRHVR SSSLRVLVYQ GVKKDGFLQP HFLAEQDIVI ITYDVLRSEL
     NYVDIPHSNS EDGRRLRNQK RYMAIPSPLV AVEWWRICLD EAQMVECPTV KAAEMAQRLS
     GINRWCISGT PVQRGLEDLF GLVVFLGIEP YCVKHWWVRL LYRPYCKKNP QLLYSFIAKI
     LWRSAKKDVI DQIQIPPQTE EIHWLHFSPV ERHFYHRQHE VCCQDAVVKL RKISDWALKL
     SSLDRRTVTS ILYPLLRLRQ ACCHPQAVRG EFLPLQKSTM TMEELLTSLQ KKCGTECEEA
     HRQLVCALNG LAGIHIIKGE YALAAELYRE VLRSSEEHKG KLKTDSLQRL HATHNLMELL
     IAKHPGIPPT LRDGRLEEEA KQLREHYMSK CNTEVAEAQQ ALLPVQQTIR DLQRKIYSNS
     PWWLNVIHRA IEFGIEEELV QRVRNEITSN YKQQTGKLSM SEKFHDCRGL QFLLTTHMED
     LSKFQRQVRD AVKNLEGPPS RHVIESATIC HLRPTRLPLN CCVFCKADEL FTEYESKLFS
     HTVKGQTAIF EEMIEDEEGL VDDRIPTTNR GLWAISETER SMKALLSFAK SHRFDVEFID
     EGSTSMDLFE AWKKEYKLLH EYWMALRNRV SAVDELAMAT ERLRVRDPRE PKPSPPVPHI
     IEPHEVEQNR IKLLNDKAVS TSQLQKKLGQ LLYLTNLEKS QDKTSGGINP EPCPICARQL
     GKQWAVLTCG HCFCNECISI IIEQYSVGSH KSSIKCAICR QTTSHKEISY VFTSEKASQE
     EDIPVKGSHS TKVEAVVRTL MRIQLRDPGA KALVFSTWQD VLDIISKALT DNNMEFAQIS
     RVKTFQENLS AFKHDPQINI LLLPLHTGSN GLTIIEATHV LLVEPILNPA HELQAIGRVH
     RIGQTKPTIV HRFLIKATIE ERMQAMLKTA ERSCREKWRL CPEMTRQQRI PDIEKQ
//
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