ID A0A0V0X393_9BILA Unreviewed; 2135 AA.
AC A0A0V0X393;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA repair protein complementing XP-C cells-like protein {ECO:0000313|EMBL:KRX82486.1};
DE Flags: Fragment;
GN Name=mus210 {ECO:0000313|EMBL:KRX82486.1};
GN ORFNames=T06_4124 {ECO:0000313|EMBL:KRX82486.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX82486.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX82486.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX82486.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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:KRX82486.1}.
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DR EMBL; JYDK01000021; KRX82486.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd22752; OTU_OTUD5-like; 1.
DR Gene3D; 3.30.200.90; -; 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; 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; 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; IPR036985; Transglutaminase-like_sf.
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; PF03835; Rad4; 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 SUPFAM; SSF54001; Cysteine proteinases; 3.
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:UP000054673}.
FT DOMAIN 154..251
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 695..1078
FT /note="WAPL"
FT /evidence="ECO:0000259|PROSITE:PS51271"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2110
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 337..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX82486.1"
SQ SEQUENCE 2135 AA; 240100 MW; 44D1A9E6EF3646DF CRC64;
LSNVMTILPK KKGGSKDSRS QSHDHSSSSS NSGSLNVEDA ALIGLRNAQH TTVDSPTVPR
RPVSHSAYDL PEGESVFFGS GSRKRLATVN PGRQERGHRT KQKNLSHTLP STSTAPVKQG
YNSEDEYDEE LNTGVDEDQL DRNFEDALKT AKGFIIKKMK ADGACLFRAV DYFSQFVTES
FSDYIARKSL SYSHGNHIEM QAMAELFNRP IEVYQYNIEP INTFLSNKNT NDPPIRLSYH
RSIHYNSVVD PFKATIGVGL GLPQYFPGLA ERNLMNDARL ISERDVIEEA MLKDKMDATD
WEATDEQLQE QIACESYLQW LADERKRHGN VAEDAKGANS SKDSSATEDN TSRKLPACGD
TAQDLTSQPS TSQFLLNDYT LTGWNAEEEL LNHVLALSQQ EYIDSLSHKR EDEDSACCSS
RDAVQSTTNI VSEYPQSENS NDSNQTYAKV KGLNGCSRVT HETKADTASA LFDAVLEDIK
SHESCATASS SVLAGKAKFG NRSKNLVSEA PATSHADFSE AEALPDSQDS QKSFSRGIAN
ICLNEEAGLP SVDAGLSSPV SATNCSKRFF SDKHGQFASS VSPSKRKATQ LKEDRQVDAS
SVYSFEEEEE EDKVGLTELE TDVEYPTKFL TSSSPNAKSS SKTTFTKKEV NAAKAKHDIA
TPSVSVSKFH GIRQRKTVKS VVCGEEISQN KTQCIRKEKP LYTVVRNVKQ AHECHESGEA
QEYNDDVVYL LGALSEENTS NMRCLSLITL LQKCVSAAFR NFLKAHGYAK QVLHALKDAH
GNDCLALATA CLFYLLSRDR LCLVVDECSL GLLVNLVKPM KVDVTNEEFL KCKGKIWKVL
CDWRTEVESS NIRKVLIMFD LTEKNLNTSF LALESLVFIS SRSDSDAFKQ EMRLNGGVEI
AALRVADETK KISKAKGDEA CIYPLLCLQR ALRILENVTT KASQNKGYLV TNDSLGMLDS
LLTLFDFCLN GIIAKEKSMP NVEDKNSPSA QVSSLLLIVF SELFRLLCNL SNNNEICCSK
LSASGGFIRR CVECVTFYIP RYLPESKRYD MQILFMSFVI NYIEHHQSGR RVVIHSEVQL
LDGDKLVVFS MECQVVLSSL LLVDHFPKHP EYSKFCREER DEYKKKQANE VNNAKEQQRE
HKVTSTSENS DYNHALSTNS TVSHGRVSNY YSQHDRVTPP AVVAPSTSSV SHQDISREND
ETNDAYTTFN VDDLIELENA NNRAKTVGIP PTVVENLQAA ESSSRPPKPT FDRSTKPKLK
TKTTTTTSTP VRPPLPVVAP PPSSTPVSKY SGLQPVIIPK NLVFRFLDAA ALNTAQEIET
CGILSGKLIQ SSFVVTHVIV PKQSEQPNAL YEEVATEMAS QTTRKRKVAT STYFDKPRRG
ASKRSQARAC ESTGQIDDSV GTVVENESHA QLNAKGKRQK QKQKQLSPKQ KHDDDDDDED
SKRNKRKRQR ESGLHSRKEM KKGNSHKLRL SNSVVDDDDV NDDGECFLKP ANAKMRNKIS
ECKARKKCDE NNDDSDHVVH KKREKKRIAK VKVVETNSSD SEWEDVKDVE IIDRPSTSTA
NIQLHFKQPE NPSASKKKTL LQRLVSKVTK LARIRRHKVY LLAEIAHGIF LSKCCNDEQV
RATAMSLIPI EMDIREPELR TRNFASKFIR WFHKNYPLKY LEPCGSLSTD PVDYLLSKMS
SGKIYSFRDW TLVFVSFARC IGFDVRIIMA LRPTDMFDLS VTEVLVTDKL NEKKAEKRKK
LNSSSRVNDD RSNQDELGVS VERKVADCQS IPPNSMCSAA AHYCFSFDNE HAVRDVTIRY
ASNYGTVDFK RRRLSDSWFQ LTLDLFQPAN KLRNRLEDLF LEKMLSEKPL PKKRSDYKNH
PLYVLKRDLL KFEALYPADL QPVGYIGQEA VYPRTAVMNL KGKEAWIREA RVIKANEQPY
KVVKGRPKMT VPKELRVDRP LNLYGIWQTE PYIPKPAEDG IVPKNEYGNV ELYQMSMLPP
GTVYMIQPGL LSIARKLNID CAPAVVGWEF HCRSSHPIIE GCVVCKEHKE ILEAAWLEEQ
VHIAVKEKER KTMRALKNWR KMVRSMLIKA KVEKKFLPST KSAGSELSQS DGQLIHNQRN
NSTASTSVED LNKSAWPQCR HQFDMHFDTE ERLSD
//
