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Database: UniProt
Entry: A0A0V1LNH6_9BILA
LinkDB: A0A0V1LNH6_9BILA
Original site: A0A0V1LNH6_9BILA 
ID   A0A0V1LNH6_9BILA        Unreviewed;      2443 AA.
AC   A0A0V1LNH6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=OTU domain-containing protein 5-A {ECO:0000313|EMBL:KRZ60754.1};
DE   Flags: Fragment;
GN   Name=otud5a {ECO:0000313|EMBL:KRZ60754.1};
GN   ORFNames=T02_10719 {ECO:0000313|EMBL:KRZ60754.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60754.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ60754.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60754.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
CC   -!- SIMILARITY: Belongs to the peptidase M67C family.
CC       {ECO:0000256|ARBA:ARBA00010981}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ60754.1}.
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DR   EMBL; JYDW01000026; KRZ60754.1; -; Genomic_DNA.
DR   STRING; 6335.A0A0V1LNH6; -.
DR   Proteomes; UP000054721; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd08066; MPN_AMSH_like; 1.
DR   CDD; cd22752; OTU_OTUD5-like; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR   Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR018327; BHD_2.
DR   InterPro; IPR004583; DNA_repair_Rad4.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR   InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR   InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR   InterPro; IPR042488; Rad4_BHD3_sf.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR015063; USP8_dimer.
DR   InterPro; IPR022771; WAPL_C.
DR   InterPro; IPR012502; WAPL_dom.
DR   PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR   PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR   Pfam; PF10403; BHD_1; 1.
DR   Pfam; PF10404; BHD_2; 1.
DR   Pfam; PF10405; BHD_3; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF03835; Rad4; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   Pfam; PF07814; WAPL; 1.
DR   SMART; SM01030; BHD_1; 1.
DR   SMART; SM01031; BHD_2; 1.
DR   SMART; SM01032; BHD_3; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 2.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51271; WAPL; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          154..277
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   DOMAIN          736..1240
FT                   /note="WAPL"
FT                   /evidence="ECO:0000259|PROSITE:PS51271"
FT   DOMAIN          1539..1667
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1374..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1481..1526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1700..1784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2045..2065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2389..2418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1720..1743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1744..1767
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         2443
FT                   /evidence="ECO:0000313|EMBL:KRZ60754.1"
SQ   SEQUENCE   2443 AA;  274624 MW;  889018ED3B2C5C4A CRC64;
     LSNVMTILPK KKGGSKDSRS QSHDHSSSSS NSGSLNVEDA ALIGLRNAQH TTVDSPTVPR
     RPVSHSAYDL PEGESVFFGS GSRKRLATVN PGRQERGHRT KQKNLSHTLP STSTAPVKQG
     YNSEDEYDEE LNTGVDEDQL DRNFEDALKT AKGFIIKKMK ADGACLFRAV ADQVYGDQEM
     HDTVRKLCIN YMKKNSDYFS QFVTESFSDY IARKSLSYSH GNHIEMQAMA ELFNRPIEVY
     QYNIEPINTF LSNKNTNDPP IRLSYHRSIH YNSVVDPFKA TIGVGLGLPQ YFPGLAERNL
     MNDARLISER DVIEEAMLKD KMDATDWEAT DEQLQEQIAC ESYLQWLADE RKRHGNVAED
     AKGANSSKDS SATEDNTSRK LPACGDTAQD LTSQPSTSQF LLNDYTLTGW NAEEELLNHV
     LALSQQEYID SLSHKREDED SACCSSRDAV QSTTNIVSEY PQSENSNDSN QTYAKVKGLN
     GCSRVTHETK ADTASALFDA VLEDIKSHES CATASSSVLA GKAKFGNRSK NLVSEAPATS
     HADFSEAEAL PDSQDSQKSF SRGIANICLN EEAGLPSVDA GLSSPVSATN CSKRFFSDKH
     GQFASSVSPS KRKATQLKED RQVDASSVYS FEEEEEEDKV GLTELETDVE YPTKFLTSKT
     WKSVYQHKWN TDSSSPNAKS SSKTTFTKKE VNAAKAKHDI ATPSVSVSKF HGIRQRKTVK
     SVVCGEEISQ NKTQCIRKEK PLYTVVRNVK QAHECHESGE AQEYNDDIVY LLGALSEENT
     SNMRCLSLIT LLQKCVSAAF RNFLKAHGYA KQVLHALKDA HGNDCLALAT ACLFYLLSRD
     RLCLVVDECS LGLLVNLVKP MKVDVTNEEF LKCKGKIWKV LCDWRTEVES SNIRKVLIMF
     DLTEKNLNTS FLALESLVFI SSRSDSDAFK QEMRLNGGVE IAALRVADET KKISKAKGDE
     ACIYPLLCLQ RALRILENVT TKASQNKGYL VTNDSLGMLD SLLTLFDFCL NGIIAKEKSM
     PNVEDKNSPS AQVSSLLLIV FSELFRLLCN LSNNNEICCS KLSASGGFIR RCVECVTFYI
     PRYLPESKRY DMQILFMSFV INYIEHHQSG RRVVIHSEVQ LLDGDKVISL PTVQALTRRI
     ANAQSADDEM NNEIEGSSQT TAKSLDMQQK SFQETVKAAL VIASKHMEEC TVAAHVGLIL
     GLLMQEDESI VSGIQHGMPG GTFKLVIETL EKFLDFMKEA NVTDAGAERT ITSPKMLVKE
     ITSEASNIQF YPNIAMKKYA RSAGELYFIA GVYELDNNVE LAYRSYTRFI VLLVDHFPKH
     PEYSKFCREE RDEYKKLMKN VRDAFDAAER LKVELTKQCE LQYMNALQKQ ANEVNNAKEQ
     QREHKVTSTS ENSDYNHALS TNSTVSHGRV SNYYSQHDRV TPPAVVAPST SSVSHQDISR
     ENDETNDTYT TFNVDDLIEL ENANNRAKTV GIPPTVVENL QAAESSSRPP KPTFDRSTKP
     KLKTKTTTTT STPVRPPLPV VAPPPSSTPV SKYSGLQPVI IPKNLVFRFL DAAALNTAQE
     IETCGILSGK LIQSSFVVTH VIVPKQSGTS NSCVAHHEEE MFTIQDDLGL ITLGWIHTHP
     TQSAFLSSVD LHTHCSYQLL FPEAVAIVCA PKYNEIGVFM LTSPYGLKVI ANCKRTGFHP
     HSQNPPVFQT CDHRPKWLLK QPGNAKLPRP PRRGASKRSQ ARACESTGQI DDSVGTVVEN
     ESHAQLNDSK RNKRKRQRES GLHSRKEMKK GNSHKLRLSN SVVDDDDVDD DGECFSKPAN
     AKMRNKISAC KPRKKCDENN DDSDHVVHKK REKKRIAKVK VVETNSSDSE WEDVKDVEII
     DRPSTSTANI QLHFKQPENP SASKKKTLLQ RLVSKVTKLA RIRRHKVYLL AEIAHGIFLS
     KCCNDEQVRA TAMSLIPIEM DIREPELRTR NFASKFIRWF HKNYPLKYLE PCGSLSTDPV
     DYLLSKMSSG KIYSFRDWTL VFVSFARCIG FDVRIIMALR PTDMFDLSVT EVLVTDKLNE
     KKAEKRKKLN SSSRVNDDRS NQDELGVSVE RKVADCQSIP PNNMCSASAH YCFSFDNEHA
     VRDVTIRYAS NYGTVDFKRR RLSDSWFQLT LDLFQPANKL RNRLEDLFLE KMLSEKPLPK
     KRSDYKNHPL YVLKRDLLKF EALYPADLQP VGYIGQEAVY PRTAVMNLKG KEAWIREARV
     IKANEQPYKV VKGRPKMTVP KELRVDRPLN LYGIWQTEPY IPKPAEDGIV PKNEYGNVEL
     YQMSMLPPGT VYMIQPGLLS IARKLNIDCA PAVVGWEFHC RSSHPIIEGC VVCKEHKEIL
     EAAWLEEQVH IAVKEKERKT MRALKNWRKM VRSMLIKAKV EKKFLPSTKN AGSELSQSDG
     QLIHNQRNNS TASTSVEDLN KSAWPQCRHQ FDMHFDTEER LSD
//
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