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Database: UniProt
Entry: A0A0L0BXM8_LUCCU
LinkDB: A0A0L0BXM8_LUCCU
Original site: A0A0L0BXM8_LUCCU 
ID   A0A0L0BXM8_LUCCU        Unreviewed;      1319 AA.
AC   A0A0L0BXM8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=E3 ubiquitin-protein ligase SHPRH {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FF38_04850 {ECO:0000313|EMBL:KNC24755.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC24755.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC24755.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC24755.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC24755.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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:KNC24755.1}.
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DR   EMBL; JRES01001179; KNC24755.1; -; Genomic_DNA.
DR   STRING; 7375.A0A0L0BXM8; -.
DR   EnsemblMetazoa; KNC24755; KNC24755; FF38_04850.
DR   OMA; QLFEQMC; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
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; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat 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; 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; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
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; PF00628; PHD; 1.
DR   Pfam; PF21325; SHPRH_helical-1st; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00028; TPR; 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   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50005; TPR; 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   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          212..480
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REPEAT          653..686
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1054..1097
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1156..1308
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1319 AA;  153803 MW;  6EDDCFB70914999E CRC64;
     MGDQIILTKI AKLANTQEIS CDNKNVTFEC KGKKWLLLDG YKDVAKNIFQ LIQKCGQHRP
     KDFGFASTYD GYFVVVYRNI IRHKKDDFFD RLTEELFDTV YPYLKKPASS SSVMENKVLK
     TYVTTRLFEA LQLKHKEVMR EDLTNATQRS LSLPSRFLPT LCEYQKKSIL WLLKRELDQE
     SFPDFFEKLT AKDQETTVYK HLYSRYILAE PPDDLVLPPG GILADEMGLG KTVEMLALIL
     LNSCLEINLC PAMEMFFSNT MAKRKCLDFK LFCICNSNSK LNTIQCQKCQ LWQHQDCVNF
     FASDMDNEEV NTPYLCPSCW QLTVKEYGLL KTKATFIVSP NTIKMQWASE IKRHIQPTLK
     VFIYEGVLSG KWISPRQLGD YDIVLTDYNI LRGDVYFTQD NVSERSTRNK PRSMRANTPI
     LMLDWWRVLL DEAQMVESKT SKVASLVRMI PAIHRWAVTG TPIQNSLNDL QPLLQFIGFE
     AASEPYVWQQ IVNEFVHQHE QQLENSNAIA PTCPAMIDIL QKCMWRTCKT QIASELNIPP
     QEEIVHRIQF DNLEKLFYNE QHEECRNKFL ENVHKYSKRM TTISPQVMNI ILQPFLKIRQ
     TCSIPVVVAT SNVNRNHNFN SQQQKQFLQP QELHDYLKST NEISCKSELR AMASSHNGLA
     ALYFLQKKYD EAIKNYKAVL KLANDYSDMN IAVDSLLQIH ALHNLMQIKI IQSNISKINL
     DKYEKQYNQL EWKYLSAYAS TLTTVKSGYE AALDKLSTDI SENFIITMAD GLETLSSSDE
     SILLQKIHEE CLPKFGQTNV KLVEIQSSRS LLYVIQLWFN KLRDIWKTLQ TEIEDLKYFS
     ENVRARNQVS PAIWRNIMQL VNSVYDCHLS EIREVQKSKK DLEKQKKTPK KKILCKLCCI
     RNSMNAFECL LFDKVIDKES NDTEGLENPS FEMYLCKLTF HFVKNKHRIL TNIMEKCWLY
     LENMQLFCKR LIKFWIEMEY TIKAYDELNM CKMRITLTDD PEDKSIFKIM ENEIEGRLLE
     QQNELMNAQH QFTIKLARLR YIKHLEGNDD PGPCPICRLT EDDRYAVLEC GHHICFPCLK
     SIRLYVKGSH FKCSICRNLQ QNQKIYYVSR SKSKSIDSET IIKGNYSSKI TYIVRLILKL
     QREQIEAFQQ KQNDSNIEDE AKEINVKILI FSQWEPIIQA IALALNENNI KYRAQCTPKT
     IEEFKNPNLG ITCLLMPFVR GSKGLNLVEA THVFLVEPIL NPGEELQAIG RVHRFGQHRQ
     TTVHRFIVQE SIEEKIYNFI INSSSTSSDA TGLQRKWEFD NITLKDFENL FTLENRECD
//
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