ID A0A1B0FM68_GLOMM Unreviewed; 3421 AA.
AC A0A1B0FM68;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY004942-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY004942-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY004942-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 {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCAG010023908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CCAG010023909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 37546.A0A1B0FM68; -.
DR EnsemblMetazoa; GMOY004942-RA; GMOY004942-PA; GMOY004942.
DR VEuPathDB; VectorBase:GMOY004942; -.
DR PhylomeDB; A0A1B0FM68; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 5.
DR CDD; cd14294; UBA1_UBP5_like; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR22826:SF210; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00435; Spectrin; 3.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00150; SPEC; 6.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 5.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50030; UBA; 2.
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 Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 1306..1480
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1498..1605
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2095..2277
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2295..2402
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2743..2852
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 2895..3382
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 3187..3228
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3257..3297
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 244..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3421 AA; 390028 MW; B7684345A26DF3EB CRC64;
MDGQRARDIL TLLQERVVFL TGGRDRRGGP LLCFPATPRR DRLKPEDLRR LLSYLIMIPS
DSAKNLGFTV IIDMRGNGNC AANVKTILKV MQEHFSANIH NVVIIKPDNF WQKQRASISS
HKYKFETSTI SIETLNKVAE ANQLTSDFEG TQVYDHQQWT EARLAIEDFF WQASDLADRI
DDLQEDLQRN DFAEDVNGAR HALDHHNEMK KKILKLPVED LDLQGKKLLS KINFGVGCSG
GPSNASGTEC GSHDSATSTQ TQNSSPGFRV ATNNPDMSAA INKALRQTDL IHSGQQRLLN
LWQHKKSKLD QCFQWRLFEQ DCEKMFDWIL HNRDVFQMSY VEIGHNYSVA KSLQDEHQKF
AVASMNVSVN IDRILAVASR LIESQHYAAQ NIKTLATRLD RTWKDFAAGL DERTAVLQLS
VLFHHKAEQY CNSVSSWAAA CQASQPLPSD IQSLETAIRT HQSLYEAMCQ AYTEVHSTSK
KLLYQLDHLV QVCNQPPPPG MPDHRKNSSF NKYERQNPAA DYSEGASHVL AVIHQILGHH
RSLEAKWHQE KIRLHQTLAL RLFQEDVKQV LDWLKNHGEV FVRKNTGIGR NLQKARVYQK
SHEHFENVAQ NTYSNAEKLL AAADELARSG EADPNEIYSV AHELEIQVAN FAKRVEQRRR
RLDIAVIFYT HEKEVISWID QLRADVSTDE TMLSQENLEG IERLLQQYRE QQDSTIKGCM
QTIAQGEALL QEMRALEYSD NTGSISALET TLEKLSKQKV ELEELWTARK FRAELILRLR
YFERDAMELS SQLEIWSEEL QHADLSRDYQ KAEQLIRMHN ESVSDIQNAT YEVLEQGQEL
LQIFESAGFI SMADATHTAQ ARIEYLLNFL REREIDLEEL SEAKRAKLEQ AVQLCQFQND
ANQVISWIRN GEAMLVASFV TPNSLQEAEQ LRKEHEQFQV AIEKTHTSAV QVKYRADALI
NANHYDPQSI REISDDVTKK WQQLVTYAEE RHKLVTASIN FYKTAEQVCS VLDSLEREYR
REDDWCGGGG SSDKAQTIVQ LISKHQEQKE AFLKACTLAR RTAETFLKYA NRSQQYYKYQ
SQGNCENRVK AILDKLLTQE NQVLEFWTQR KKSLDQCQQF VLFERSAKQA IEWIHNTGEA
YLSSRSNLIG KTREETENLL KEHNEFRGTA KETRERVKLL IQLADSLVEK GHAHASSIKQ
WVASVDQRFV VTHESILFFF LRKHGIFCLN RYKAFSNRMD SYRGQLEKSL GMSTMPADPD
PNTSISSVSG SSTDRHSDPS LEAKLTTSTT AVSKEINEEK RKSARRKEFI MAELMQTERT
YVKDLEICIK NFLEEFRTGH GVPSTLIGKE DIIFGNIREI HNFHQKIFLR ELEKYETMPE
DVGHCFVTWA SKFDMYVIYC KNKPTSNNLL VQHAGTYFEE LQHKHKVEHP LPAFLIKPVQ
RITKYQLLLK DLLSCCEEGH GEIKEGLEVM LNVPKKANDA MHLSLLENCD ITTDSLGEVV
LQDAFQVWDT KQIIRKGRER RVFLFELYLL FAKEVKDSNG SVKYQYKNKL MTTDLGITEH
IEGDETKFAV WTGRSPMLSD CRIVLKANSL DTKQVWAKKL REVMQETCFS GTSLTLPKSP
AKNSSSSQRS SRDLDDPLTE NDHDRCSLAS FGSGNTTDSD NKIRPAILFQ LHGSEPIEQT
DYVVAESKSK LNFKSNITAG DDKSPTVLIQ SSHDDNTTPP TSTTSEDSRI SPFDFSSSKT
VMKPKTRRKI SLPWSRQTSI TKNLVLSRQH TIDSPGSFHL TQQQSGCKSK VGTYEATWVI
SDYIALAGSN KLTVTKGQQV EIVEAPTSAE PDFCLVRLNP PNDDGVVQEG FVPISILKPS
PVAQKATFAR KEKCDSGEQS NSRGKSDPLT SSTKRRGLGG RKWLPQIGRK PTQHKIEKPP
EKALTKKLSE KNFKLPAKQT DDNSMIASTS PMSSTAMSQL NTSQQELELD EEVGLELPPP
MKPIQEPHII ANGPPAFTKD TKDNPTALAN AGKMNGLSEI EQIVKEKTEK HEEKSKILSG
SSSRLGTAAC GGNSTGMETC SNADLVYPNN ENNTSKNSGE NSYMKSSEIE STHKCRLPAL
TELISTEELY IKDLGDIVNG YIAELRNANS DIIMPNDLKS PKWLIVFANI EAIYEWHRDS
FLKLLLQCQK SPGDLGSMIK HYEHKFQMYI TYCNNKPKSE HIVTEHVQYF DQVRQKLGHR
LDLSDLLIKP VQRLTKYVLL LNTITKQIEQ AGMVEEVPSM KEACNVMNAI CKNVNDTMVL
QRLKNFDGKI TAQGKLLLHG SLTCIENARN ATERKMREMH VFIFEQSILF TEKHNSKIQF
SSPTYVYKSH IQVNKMQLEE LPNNRFLLKS TDPNRPDLNM ICHASTIETY REWLDTIRKQ
LQIQHDFLNA LTRPIAYQQQ QQAKGKQHIL NNNNNNNNNN NNNCLHVTDI IARKQDTSSY
IISKKLRTSP ETCSALLCDI FAKQPHHYYY YHYYHYIFKI SCSKENVLKY FAAFIENKHK
IQNANTNTNR NTFTNAYTSF HIVIYQNFIC LSIIIQLYKD SREILLNCSS TMDFLCKYLS
NIRIPCDKQP IYKDECVYSF DTPETSTGLY VNLTTFLGFG ENYVLKYAEK TGNKVFLHIR
REKFAKDNTM ETNKEETGPK SKITRLAIGI EGGFNNNETT KYEYKDTYSI VVMPDIKIKM
PYPSHELPTI VNQSVEAVLA QDSAIMKLQK EALTGSWDGE IRQISKYSDE LKQLDNGRKI
PPSGWKCEKC DLTSNLWLNL TDGSILCGRK FFDGSGGNDH AVQHYQEFGY PLAVKLGTIT
ADGKSDVFSY PEDDMVIDTK LAEHLSHFGI NMAAMKKSEK SMVELELEIN QRIGEWSLLT
ESESTLQPLA GPGYTGMRNL GNSCYINSVM QVLFTVPDFI KRFVGKGAET YFSEFPLDPA
NDFNIQMAKL GNGLWSGKYS SITQNALDES LGISPAMFKN VVGKNHPDFG TKQQQDAYDF
YLYLINLLER HSRNEFNPAE ALTFAIEERV ECLTSKKVKY TRRDEYCLPL PIPLEKATNL
DEVTDYLEKK STSAIGKEGD KDIIRHNIPL HECLERFFSS EHIEQYYSTA IKDTTSAKKS
SRLVNMPDYL MMHLRKFTLG DDWVPKKLDV SVQMPDELDM SKWRALGKQP NEEELPEIDL
IKHINFTFDE NMVSSLMQMG FPQEACKRAV FHTKNGGIDV ASDWLMEHIG DSDFSEPFVV
PDCETGNIAG KMKSTFVPNP ESLALLMSMG FDELKATKAL KATNGNLERA TDWIFSHIDD
MDVDDTDTST SSGNQNQKVY RDGIGKYKLV AFISHMGTSA QVGHYVCHIR KDGQWVIFND
SKVALSQKPP KDLGYLYMYK PCDLTERQTY LAKYVSASNG ENLQPELRKV EKKKKKNQFW
G
//
