ID A0A0M5J1C0_DROBS Unreviewed; 1746 AA.
AC A0A0M5J1C0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=CG8334 {ECO:0000313|EMBL:ALC44636.1};
GN ORFNames=Dbus_chr3Lg1802 {ECO:0000313|EMBL:ALC44636.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC44636.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC44636.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC44636.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012525; ALC44636.1; -; Genomic_DNA.
DR STRING; 30019.A0A0M5J1C0; -.
DR OMA; FKADNRR; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT DOMAIN 224..259
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 260..295
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 377..549
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 738..1706
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1119..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1746 AA; 195842 MW; 2869B8CF779139F3 CRC64;
MGTKESKHAC ISYEDAVKRV SDVELRRLKD AFKKSAGVGR LYLSRNAFQQ DVLCEGVPPK
ITDMLYAACG GTQRGISFKD LLCGLVLITR GTQEEKTKFL WNLYCNDAGT YINKSDYVRN
VNLAPFESVS LFAQSERANF EQFQDWVTKH RNATVLSNWL LADNCVSLTS ELETPTFYQS
LAGVTHLEEK DIGDLEKEFW RLKNTSQNGQ IDLQFLGPLI SPPIPKNALA GLFNAFDENR
DGHIDFKELC CGVSAACRGP GVERTRFCFK IFDVDRDGVL SHEETLQMIN VLLFVAKENR
DTQQYRELTK QHVISDLLEF AQRKSCDGLP SALTRDNVSL TAEDFMLWNV QCSLRLMQPL
LDLIFELCHI VFGLWPQCKH MEYDIVRGWL QREERRPYRV GQFWYLISRD WWLNWMQYTQ
HTAHTCEYCK RTASQRSAVD EALVCDESFN THSLEQHDSY SLGSASNSGS SGISAGRHCG
QLRPGPIDNS NLITVNTQRN IRTLTGEGGH LKRDTPLVQS HDFELVPKSL WKALNRWYGD
NLPLPRQVIQ PPNSEVELEL YPLYLRILLH QAQTTSNAAG GSNQFNSWSS TGSGGYGVLA
SGGGYAAIAA SSVLQPPKRY LAYTAAFSRL ATVRQVGEFL CEQLRLKPED IRLWHVPSSS
ATLDNSAILL EEDAMCLKEL LIRDNDQLLL EIRNKDLTWP EELGSLASAQ SGQVGANSND
RRRLTRSSIM SVHAPGATGL HNLGNTCFMN AALQVLFNTQ PLAQYFHRQM HRFELNTANK
LGTRGQLAMR YAELLKEIWT ATTRSVAPLK LRFCVNKHAP QFAGGGQHDS QELLEWLLDA
LHEDLNRVTE KPYSELKDSN GRPDKIVAAE AWSQHHARNQ SIIIDLFYGQ LKSKVSCLAC
GHESVRFDPF SLLSLPLPVE NYVYLEVLVI LLDGSVPIKY GLRLNSECKY TDLKHKLATL
CGLQPSLMLI CELWNSQIRQ VLADDEKLRT QSAKELHVYQ LPEQSGARTR SNSALSMHIE
QGLKDIQRSS ALITAQDSLS SLSTLQTSNR TASLSRALCN GHLSDGQDVE AELTKYNSQG
QGQVHELPTD DAGKESLILS CSPENNFMDD SAKQKRISST KLLHTESNTS SASYTNHSGE
NSMESSLTEP MPVAELAGEE GVCYSQTNKH SSGLSSALTL GAHSLERQAT IDNDDNVVEE
LAAEGEEEEE GEEPDQQITT SQPESTSGNQ TSSGVYSRRS SQPYKVGKYL VAVHRKITRH
DSYFLSYHKT RPSLFGVPLL IPNSEGGTHK DLYCAVWLQV SRLLSPLPAT TEQANHAADC
DDSLGYDFPF TLRAVKADGL TCAICPWSSF CRGCEIRCNN DYVLQGALPP INAATTPQMS
VKCPSLPNLE AKRAPEYTAS LSYTPTTKYF EDFTIAIDWD PTALHLRYQS TLERLWVDHD
TIAICRREQV EPVDLNHCLR AFTSEEKLEQ WYHCSHCKGK KPATKKLQIW KLPPILIVHL
KRFNCVNGKW VKSQKVVHFP FDDFDPTPYL ASVPQETILR HKELLELQRL PCSTSASDVV
NELDEVDASD KTPAEANEQL TVALQQETPQ VAVAPASNAL RQCKSSNAAK RQRLISTSLT
KTPIVDGEFE DYHQHKLKDD TDEFDPKYKL YAVVSHSGML NGGHYISYAS NTTGSWYCYN
DSSCREISQK PNIDPSAAYL LFYERQGLDY EPYLPNIEGR ALPNASTMQL EVDETEGELK
KMCTIS
//
