ID A0A182WHB6_9DIPT Unreviewed; 1284 AA.
AC A0A182WHB6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN009768-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN009768-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN009768-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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR STRING; 112268.A0A182WHB6; -.
DR EnsemblMetazoa; AMIN009768-RA; AMIN009768-PA; AMIN009768.
DR VEuPathDB; VectorBase:AMIN009768; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02670; Peptidase_C19N; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 921..1278
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 280..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1284 AA; 140048 MW; 98B94E05BB8931EA CRC64;
MSSGGNIYAI STERFRAKVV NVPLTHGGIN AGGGGSGSSS SSLMSGSEAV ATGSPITAVP
TDALAIDDRI DIEPGMTLQI VEQPSSKIAL IKIKDFYGTA TANSRIGGTP STGNSVQANP
YENRIFQCQA ANLQRIPSDI WPYIIAILDP QDRCEFAKRP KVFGSVKQLR TGDIVMVSWL
AKNRHVTYDC IIRYVGPVPK IGPGYYFGLE LLNLENGESP QKDDIDFVSD YMNCEPRLAL
IVAANWIKFP EHEASGKQHH HKRNLLDSLV CGARDLNNRL SRRTGSSSKH SADDATGKGG
AVRSGKVING EYPPYARSYT PDLTSSSSAG GSNRKSTDIG TLYDSFSCLQ MDPAGTKAMH
HKKIAASISS PNLSKQDSSS STGSSGRYVN SHPMDSYGDE YHRFVEHGQQ HQHHHHHHLA
DEAYRSSGRS SQNSSNNSTL KHSKARSGKV ARSSGSNSSV NSAGGGGYHS VSKQSTILSL
PDRDVVVIDS NEIDEAIKSA SDVIVVDPPP VLSPTDNREV ELMDLLGSSS WPAEAGEVAA
ILSGGNSSDK KTQTPSTTTL ASGLGYGNGL TTGTGYNTSG STSSNSTANS NQSYHSHNGT
STAGRYERNK SLNPLAHIGS PKPVETLSSG SRKVRTSDTK PSTVDVATMT IRIMLWSMLP
DTYDKDSFDG IPLTVLEHFD WEDEPETERR SGSDVEEELN DGAAGTGGYI TSNGIGPAAV
SNGNDSNTTI TANGLLPRIG SISPESDNGG PPAVSPLQEL PNDPSLGVGS MVEVTLDAFE
TAGSTPATTD PLLYGVIRWI GPLPTAGSNH RKVMVGVELE DEPIDPKLET TNGTHNGVRL
FKCPANRAIF VHTSQCSRDR RFQDIPPMSP CTSRTTQASS AGSKTDTTMF GKVDCPVVKG
RMPPLKILKL EELEEICGKF KGIQGHHNSC YLDATLFAMF TFTSVFDSLL FRPKEPEDNP
QYEEVQRVLL EEIVNPLRKN HFVRADRVLK LRQLLDRLSS VTGLMSEEKD PEEFLNSLLA
QILRADPFLK LSSGLDTFYY QLFVEKDERL NLPSVQQLFE QSFLASNIKL KEVPSCLIIQ
MPRFGKNFKM YPRILPSQVL DVTDIIEDSP RQCWVCGKLA EYECRECFGK MQCEGLEGTA
ICKSCIDSVH HHSKRLNHKP VPLSVPQDFI PMAPHCEVPR LYMELFAVVC IETSHYVAFV
KAASGQDAPW CFFDSMADRN GEQNGYNIPK MVPVPDLPRW LTEEGSRALN EEAVNDKMLP
EHAKRLLCDA YMCMYQSTDV MMYR
//
