ID A0A182QCW3_9DIPT Unreviewed; 1292 AA.
AC A0A182QCW3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF007624-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF007624-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF007624-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; AXCN02000643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 69004.A0A182QCW3; -.
DR EnsemblMetazoa; AFAF007624-RA; AFAF007624-PA; AFAF007624.
DR VEuPathDB; VectorBase:AFAF007624; -.
DR OrthoDB; 51419at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03772; MATH_HAUSP; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 249..377
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 396..702
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 146849 MW; 106CDE47B6290DE3 CRC64;
MDDLDQRQPQ EQQQPPRRRV GFRWGKPHRT APNEPDRPDK AVPPPPPTPP PSPEATAPVA
VTGASEEGDE EDQSVVAPPA DTDCTAPSLP KAEQAPNKGH KEKDSIPPAG DGGVVEEQRG
VGIEEEQVAD RRRSGGASGG GLGFHLLTRF LTVLGGKRAH RTAAKTGKEF LPTEGLNAMD
YDKTVEAMDT QDDNEIDPPN IQNLTNAVVA PPTAAANGGG GGADAANPDG GGEAMALDED
YMNDEVRSEA TFSFTIPKFS RLTDSVLSPP YYVRNLPWKI LAMPRTNDNA VSPGKGLGFF
LQCNGESTSN NWNCSATAEL RLMKVDPNAD PFIRRIRHTF CMQENDWGFS SFMNWQEILD
PANGFIDNDT IRLEVYVIAE PPRGIFWDSK KHTGYVGLKN QGATCYMNSL LQTLYFTNQL
RKAVYKMPTE ADDDCKSVAL ALQRVFHDLQ TQNKPVGTKK LTKSFGWDAL DSFMQHDVQE
FLRVLLDKLE NKMKGTSLEG TIPKLFEGKM ISYIKCQNVD YTSRRTETFY DIQLNIKGKK
NIQESFKDYI ATEILDDDNK YDAGEHGLQK AEKGILFSKF PPVLHLHLMR FQYDPISDNS
VKFNDRFEFD EMINLDPFLE SPEDTPATYI LHAVLVHSGD NHGGHYVVYI NPKNDGKWCK
FDDDVVCRCS RNEAIEQNYG GHDNELNLRH SSNAYMLVYV RESVVHQVLE EVKESDIPEE
LLERLNEQRR IQQVRRTERT EASNFVNLNI LLADYMEVHQ KSDLFDATTA AYRTLKVRKT
MDLATVVVQV GRAFKVEPGQ YRLWEVKKPS NQKPHKFEYI DPASTETCSK YASPETKHSC
TIFLELPLPG RTVLEPAKIT FEDTLLFFKF YDPVEKRLNY CGHGLYKPST TVAELARDLN
RRAYFEPDTE LQLYEVVDIN KAQKISDPFQ TLQTALSLLG HGTIVVFEKL HPPQENLEFP
TCEAYFKDLF CRMEVVFLDT LIPNDTGFTL DLSSESTYDQ IAKAVGRRIN VNPYEIQFFK
SKNYSDLPGQ PLSHSFGGSL RDVLQYTKTK TIRKLFYQKL SININELENK KQFRCLYLMP
NLKEEKELIL YPNKNGTVRD LLEEARKVIE FGESSTKQLR ISELSKNRLS PGPSDDTPLD
QLHDYTENPF VQKSTIGNQI MYRIEEVAED ELSLGEHELL VPVLHFTKDI SSVFGIPFFI
RTVQDETFAA LKERMKKKLG VSDKEWEKYR LAIITEHIDY IDDEMIQIKL ETFRGEPGGD
PHARTFLGLE HINKNTKRSR FNYMEKAIKI YN
//
