ID A0A261CS72_9PELO Unreviewed; 1836 AA.
AC A0A261CS72;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|SMART:SM00181};
DE Flags: Fragment;
GN ORFNames=FL83_00493 {ECO:0000313|EMBL:OZG25377.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG25377.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG25377.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG25377.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) 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:OZG25377.1}.
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DR EMBL; NIPN01000001; OZG25377.1; -; Genomic_DNA.
DR Proteomes; UP000216463; Unassembled WGS sequence.
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; 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:SF11; LIN-12 AND GLP-1 X-HYBRIDIZING; 1.
DR Pfam; PF01683; EB; 7.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00289; WR1; 8.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1836
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012424224"
FT DOMAIN 97..133
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 304..338
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 355..387
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 497..533
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 542..577
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 590..623
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 681..714
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 784..817
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 847..881
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 893..925
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 944..978
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1009..1041
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1188..1222
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1306..1338
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1352..1386
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 1399..1431
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG25377.1"
SQ SEQUENCE 1836 AA; 199434 MW; 1AA81999BC1E61CA CRC64;
MRVLLAISVI YHITIAQQVG INVPCNKELD GLLTADPDGD ERAFMSCQGV GVGTIGFWER
KLCPNNMVFD FINQQCKEQK KKARKQQTLS IAILNNSCAN GETCIGGSVC DLDTLRCMCP
YGTTPKLDTL SCESSQPPFV SATVDGPAQF FNSFNGANGL RNNNNNNNNF LPFGQQEVPD
FQPNNNFKYG NNFGNNPIPN TNGNGNNDFN WNPNFNWNNN NNNNNKQAPM NNMNNGAGSS
EFNPFQPNPN QKFVFNFNKN QEVQNGNNQN HMNNNNNNNN NNNQNVQVPE VKPKVTTLAI
PGASCKSNEI CVGGSICTLP IGICLCPGDL EARDGECVLP AASTISVQKV GIGALCSDLA
ECDHGSSCVM GRCTCVSPLV QHEGKCVLRQ QQKLVVQIMT PPPTLPPVQV PIQTLPPQTR
PPPPPPVQMT QPPIQTPAQQ IFYQTTRPPM QTFMTTPPTT QYIPKQIYTS PPQMPKSSIK
INQMKIGGSK QAGVGVRCSL NTDCMIGAYC NGNTNPPSCQ CLSTHVNIEG RCEKVIYPGQ
VGCRSDLQCH AAHSGTHCID RICVCPEGQK AVDQTCVSAN EPVTSPPGGS CSNLRECTGG
SVCREGWCIC PDPSMIVNRG ICIQSGPKPT LPPRTSVPQV PLPPRLPINN VHVPQVTITK
AQPFVVTEAP PQGKKIVPGG RCGPIDVCVG GSNCIEGFCL CPAGQQPSNN GRCEKFTTTS
RQTTLPSTTT TQGTTYTTTT APPPTTSVFS FTIADLLSTR RQPAFIEIPT HVPLTTTVIQ
TDDECTAIGL ICKGNTVCIN KSCQCPENYV LHHDGCVSPE EAARRKARGK ARHEATTARV
YSKPGESCTQ GQTCVGGSTC SFRKLCECPQ DKSEISNGHC VTPKKIEAAP GTSCNENSFC
TKGSTCESGL CRCQPGYIAV SGTCVALPMS TTPKMKVMAK PLESCESGEV CEGGSSCDYD
TGICMCPPGQ IVFNVQCMPP PTQPQITTRV TVPTKAAPVV TPKPRHSTDC EQDANCGENK
ICVSGKCKCK PGFVDNSGNC EPLEDIDVIE RPIPVSYAKH KVATLSERML PREQIETSNI
EPVTIATPAR QESETQKPRI VGPPIRRPRP KNKNSGGSGG GASGTGTGGR AYKTGNGSAN
CPPGNEPTRD DSGKLIICNG LEPNCPPRSY CYITSGGIRG RTLKYGQACD RYQDKCINGA
KCIDKICKCS PGFLLAPNGW CEGFDLAKAI ENNKQSVGTT PPTKANRIVQ TKKQQVYTTT
TTTTTRAPLQ QKVVPQDFPT PPSSIFGFPD RRTTKLVPKV AAVGSACRPI DICLGESVCT
NGFCHCPENY IRQNGQCIST ESKHKVAKVG ETCKNREICA GGSICDYDRK RCICAAQHVA
IRGICKQKSA PAFAAPGDTC SMREKCTGGA TCIEGMCTCD DHHFAEDGYC RPIEARSSKV
QFVNGAGLRF SSMQVPNRQR AQPCNEAECK LPNCFCSHNG RQSPGGLRPE ETPQFIVLTF
DDAVNGKTFP DYKKLFENDV LKNPNGCDVK ATFFVSHEWT NYDAVNWLVQ KNMEIASNSI
SHESLENENT NRWLNEMDGQ RRILAKFGGA PEEQIVGIRS PQLALGGDNQ FEMMVGAEFL
WDNSMSANPG IHGEPFWPQT MDYQVAWDCH EASCPKSSFP GIWTVPLNQF HGSYMRQIDS
FRRASMLRAA VDLNNTVDEL EEIIMRNFER SYSANRAPYV LSLNADFLQL GGHNTGMKAV
QRFLNKMSAH KDVYIVTIKQ LIDWMKRPVP VNQMKSSKAV GCPISFNRNP SLSTCDKPNK
CLYSTPSLSS QEHQFLTCLP CPTMYPWLEN PAGGIV
//
