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Database: UniProt
Entry: M7AVW6_CHEMY
LinkDB: M7AVW6_CHEMY
Original site: M7AVW6_CHEMY 
ID   M7AVW6_CHEMY            Unreviewed;      1672 AA.
AC   M7AVW6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   05-JUN-2019, entry version 38.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   ORFNames=UY3_14052 {ECO:0000313|EMBL:EMP28844.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28844.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z.,
RA   Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y.,
RA   Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M.,
RA   Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J.,
RA   Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G.,
RA   Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield
RT   insights into the development and evolution of the turtle-specific
RT   body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; KB560124; EMP28844.1; -; Genomic_DNA.
DR   STRING; 8469.XP_007067221.1; -.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR031937; PNISR.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF15996; PNISR; 1.
DR   Pfam; PF00443; UCH; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031443};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238,
KW   ECO:0000313|EMBL:EMP28844.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       59    135       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      192    735       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      59    135       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION        1     30       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION      359    412       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION      429    481       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION      830   1072       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION     1100   1140       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION     1161   1197       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   REGION     1218   1314       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COILED     1474   1494       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    373    412       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS    443    463       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS    467    481       Polar. {ECO:0000256|MobiDB-lite:M7AVW6}.
FT   COMPBIAS    833    856       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS    859    888       Polar. {ECO:0000256|MobiDB-lite:M7AVW6}.
FT   COMPBIAS    916    939       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS    973   1031       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS   1045   1061       Polar. {ECO:0000256|MobiDB-lite:M7AVW6}.
FT   COMPBIAS   1118   1140       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
FT   COMPBIAS   1175   1197       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                M7AVW6}.
SQ   SEQUENCE   1672 AA;  186464 MW;  16AADBD37D6768A3 CRC64;
     MRVKDPSRAN PEKNKRNKRP KRHQDEDSSD DIAGLTCQHV SQAVDVHHVK RAVAQNVWSI
     CSECLKERRI NDGDPVIPSD IWLCLKCGSQ GCSQNSEGQH SLKHFQTART EPHCIVINIS
     TWIIWCYECD EELSTHCNKK VLAQIVDFLQ KHVTRTEPSS SSKIIRLHEE NSEGSEILKG
     KSSANGASVP VKGINNLGNT CFFNAVMQNL AQTHMLNELM YEMKEKGIKL KISQAEDAQL
     DPLVVNLSSP GPLTSAMFLF LHSMRETGKG PLSPKVLFSQ LCQKAPRFKG LQQQDSQELL
     HYLLDAMRIE ETKISTVKEP FIDLSLPIIE ERVSKPVPLG RTSKCKNVQE ADLGQFNCSS
     ITAPNNQQPK ITRRHSLTKD KNQLNHERSL ARKSSSGEEE RSPVIMHEKR KLEVEDGSGV
     LYSEAINAAT ESTANGSQTE GSEKEVSRSE SSVDADSEAS EGESAAKQEV TGRSSNASGL
     HVDGLNHLVN IRLPHSKPSD SNNEMITSAI AKLSFNSIVN ESEEPISEDP SLSLSNNSVF
     SVEKSPLSQS PQNAFQTLSQ SYITSSKECS VQSCLYQFTS VELLMGNNKL LCENCTERKQ
     KYQKKTHTTE KKTEGLYTNA RKQLLISAVP AILVLHLKRF HQNITDAARV LYTLYGIVEH
     SGSMRGGHYA AYVKVRTPCK KLLEHIASNR NVQGLKEAVG ASAGQWVYVS DVHVQMVPES
     RVLNSQAYLL FYERIFSSAG QLQELDGVEE SLHLGQAKSS AQNGTLAGQI DWAALAQAWI
     AQREASGQQS VVEQQGMMPN GQDISGIEPG PNNHGNFQGD PNFNRMWQPE WGMPHQPPHP
     PQDQQWMPPA PGPMEIVPPS EDSNSQDSGE FAPDNRHIFN QNNHNFGGPP DNFAMGPVNQ
     FDYQHGAAFG PPQGGFHPPY WQPGPPGPPG PPAPSAPPQN RRERPSFRDR QRSPIAMPVK
     QEPPQIDAVK RRTLPAWIRE GLEKMEREKQ KKLEKERMEQ QRSQMSKKEK KASEEAEGDG
     PRLPQKSKFD SDEEEDDIEN TEVASVGKVS RSPSPAPQEE QSEPEMTEEE KEYQMMMLTK
     LLLTEILLDV TNEEIYYVAK DVHRKATKGG LGGYGSGDSE DERSDRGSES SDTDDEELRH
     RIRQKQEAFW RKEREQQLLL EKQLEGGLGG YGSGDSEDER SDRGSESSDT DDEELRHRIR
     QKQEAFWRKE REQQLLLEKQ LEGRDKSLAT TRPLFHSKSK ATMMARRSPS PAPPAQTQEA
     HCSPESSRRW LATRGTAPPW WSYSETSESE VDSARSSRLR SRRSWSRRSH QPDPAPAQWP
     FWTPWAYHQS QGQVHGPRSR TVSASFVPQS VPAPPMTAPP SSRVGLPTHM VLAPIPQSAS
     APALQVTARV EASAPSLPTP TVSVLPDLSA LALAGVQSSS LVPAPQPEYR MLRDPRGAKG
     SELGPPLLLS SLSSPDEAVA GTSAPALEDN RVLKQLLRRA AQSLGIQAEE VEEDLDPVMD
     ILAPSGPSRV ALPFIKSITE TYKNLWQIPA SLAPTAKKSE CRYFVPSRGY KHLYTPPPLV
     SLVVDVANQR ERQGFQGSTP KNRDAKKLDL FGRKVYSTAG LQLLIANQQA IISRYSHNTC
     SSMAKFTELL PQEAWESSLR SWRRRNWSCE RLCKRPWTLR MRPPALWPQG WL
//
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