ID A0A0V1CUX5_TRIBR Unreviewed; 2400 AA.
AC A0A0V1CUX5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Prion-like-(Q/N-rich) domain-bearing protein 25 {ECO:0000313|EMBL:KRY52966.1};
DE Flags: Fragment;
GN Name=pqn-25 {ECO:0000313|EMBL:KRY52966.1};
GN ORFNames=T03_1664 {ECO:0000313|EMBL:KRY52966.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52966.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52966.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52966.1};
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 -!- 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:KRY52966.1}.
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DR EMBL; JYDI01000095; KRY52966.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CUX5; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR006149; EB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR45985; -; 1.
DR PANTHER; PTHR45985:SF3; CHITIN DEACETYLASE-LIKE 4; 1.
DR Pfam; PF01683; EB; 20.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00181; EGF; 32.
DR SMART; SM00289; WR1; 17.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
PE 4: Predicted;
KW Amyloid {ECO:0000313|EMBL:KRY52966.1}; Prion {ECO:0000313|EMBL:KRY52966.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..2400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876255"
FT DOMAIN 137..183
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 202..249
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 280..326
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 339..381
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 390..422
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 432..464
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 474..506
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 516..549
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 559..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 601..633
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 643..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 684..717
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 727..759
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 799..831
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 841..873
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 906..938
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 953..986
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1001..1033
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1044..1076
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1140..1174
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1195..1229
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1252..1284
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1332..1364
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1851..1886
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1915..1949
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1970..2002
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2003..2043
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2058..2094
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2223..2255
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2270..2302
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2321..2354
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 2361..2393
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 2148..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2150..2172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY52966.1"
SQ SEQUENCE 2400 AA; 257792 MW; 5D7C16C313CCC168 CRC64;
LVAMLFSKFI FSISLIYLAV SILGDDSSLQ TIRNKQPSRS LFKITSVSAK LTSDKQHRQT
DDNTNSAVVP KLFVGSTAGV VPPGGICSDD EDCSGYPFAF CMGNCMCKDF AINAGSTCSM
NKGNCGIGQV YVSEAGICMN VASPGSPCQY SQQCSGAEVG AFCISMRCRC VYGMTETSDG
KCTFINSNCT HRGMIWIAEL GECKPVIAPG ARSCTHRQQC TASYRDSHCF MTQCSCPPER
PIAVDGTCGI SCSLGQTYSG VLNRCVPTAQ PGDRCQYSSQ CHALFPGTIC DRSICRCPND
FYWTGTHCTD SCPDGYQPNP KTGVCKPGCR EGQIDYEGEC LNQVSPDHPC IISAQCTGGS
SCTDGRCQCP PGKSNIQGVC TRAKSRPGGS CEHGEECTDG SYCLKNRCVC PKGYVLHNQR
CTTPLLVPPE SACGPDVACG GGSFCVNNIC TCPNGYIVIN QQCQLPDAVP PGSKCTETDH
CSGGSFCLYG ICRCPTGMVI VNQRCQIPIE VMPGHTCRVG IDICIGRSYC VEGTCRCPEG
MVIERGVCRS PSIVLPGFKC DSMTHCGGGS VCVDGVCTCP KGMTIINQRC EMAKTAPPNY
SCRNQEICTG GSSCVRGVCI CPKGQIPVGD ICKGSLDQQS KQRCVTDDQC VKGFSCVSSR
CVCAGMLLPN GVCKTSRLAS LGSKCVAGLD VCTGGSSCIG GTCTCPSGTI AIDGRCRIRK
RVPQNFTCFQ NTDCTGGAFC QNGVCVCPGQ TLLIDEICQS VMLFPPSAVV PDPKRSIILT
SSVDVDTSAV QPTARLLESC TSGQLCINNS TCLNGTCQCP VGYYAAHSVC RRKILVLPGD
PCDGATLCGH DSKCVDGRCV CLDGFEIVNR RCRKTEKKKS GTFIQNSFTG VKMSPNLYIT
ALPGERCDRN TVCTGGAFCE QGKCTCSPGF EVHEGICKWK PIQPATVAYP GQRCVEGVTK
CLNESTCLLG TCTCPPGFVL HDKYCKLTAA PLLDWAMPGQ PCNSQTQCRG DSTCIGGLCT
CPVNQVIINN ECTFAKVTVS PGFSCDANSI CTGGSTCIGG ICQCPTGESI EGYRCVTRIS
VAISSPPGSY CRPDIGVCTG GSYCRNNVCV CPQEKIAIAN QCVSSKEQIA LPVLGMKTEQ
CGKELPCRTG MICVDGMCRC KPGSTFDPAT ATCIYSSTQN NDYPRSSQPV TPGKSCISSK
FQYCVGGAIC ENGYCLCPQG TVHVSDQCQS LRSLFSNNNA QREKREVKLG AQCAATIHCN
RGAICVRGIC TCPQHWKFVD NYCVPLIYTS TQSMIIEESD QYYFSICASI LPLLHLHPNG
LNVVLAVMPG ESCKNGEICS GGSACSDDRC VCPEGSELKN YVCSKLADRF AGPCPAENRM
TSKCQLPNCF CSRSGFAIPN RIPAFDTPQM VILTFDDPIN EVTFDLYRQL FDGRFRNPNG
CPIKATFFVS HEYNNYHQTQ WMYWKGHEIA VNSITHETLS DSSVEDWIAE MAGLRKLLQQ
LAAVNVSTVQ GIRAPQLSVG GNAQFTMMQS QGFLYDNSMS VNPGKDGPAY WPQTLDYRLS
WHCEAAVCPD ESFPGIWAVP INQFYGNYIN DINQYMRGAM VRAVMTRTST PETVLRLLLD
NFNRHYRTNR APFVLTLNAD FLRVLPGDGG YKALERFLAK LSTRPDVWVI TMDKLISWMR
MPTPLSKIKQ FAPWQCDDFT REQARPCQVP RVCSFETAEP DIGNRWISTC AACPLEYPWA
KRASNVPQSN VHYYQSGDPC NIITDKHLMV NPNIQTAYMQ CVPSSHGLNG RWQAMPCPPG
QTFQFGKQRC DFDFAQVAVR ADDGGVPSLP SVLSSTVGTI FGTLATFVGQ PCDGKYCFGG
SECHSEKGIC TCPKGTVLSA NSQFCHSETA AVHIENEEIF TRAKNFTLQA SPGSSCKHGA
VCSGGSKCDP ARFVCTCDDG TVDHDGRCVN IISDDPPASP KLLKKSLGDR CEPLHSCPPG
ASCVSGICAC ISPMIQDGDH CRPLRASVHQ KASQLCQGGS VCSSVTLRCA CPLGTKETDD
HCVDFSSHKN ILASVGEHCE ANTDCIHGAY CHTGSGKPHC ECLSTHVEIE HSCLRVIYPG
QHGCSSDKQC SAVYNGASCK RGICVCPEGT GAVSQTCSKE VHSVSEHKLP EATTTELPSV
SEAPVYSASS PGGTCTDSAQ CLGGSKCYMN ICVCPEQNMH AVNGICIYKT PSVVQSFVTA
GSRCNENQIC AGGSTCRNGI CICGHGTVQQ GNKCIKTFMP GVQLPTLLKY CISDNMCKGN
SICINTRCAC PNGLRFLNGQ CVPERSYVFS PQQNTFPTFA SCSHDTDCKS GSVCVQGRCV
CPPDTEMTTD GSCESYKLGS YCDKDESCGR QAICIRGRCC CAPGTVQQGN FCLPFNNGSF
//
