ID A0A1V2YH38_9FIRM Unreviewed; 2185 AA.
AC A0A1V2YH38;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=HYR domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BEN18_05930 {ECO:0000313|EMBL:OOB78868.1};
OS Epulopiscium sp. Nuni2H_MBin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884656 {ECO:0000313|EMBL:OOB78868.1, ECO:0000313|Proteomes:UP000189057};
RN [1] {ECO:0000313|Proteomes:UP000189057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OOB78868.1}.
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; MDJM01000035; OOB78868.1; -; Genomic_DNA.
DR STRING; 1884656.BEN18_05930; -.
DR Proteomes; UP000189057; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR032179; Cry22Aa_Ig-like.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR24273; FI04643P-RELATED; 1.
DR PANTHER; PTHR24273:SF32; HYALIN; 1.
DR Pfam; PF16403; Bact_surface_Ig-like; 3.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS50268; CADHERIN_2; 2.
DR PROSITE; PS50825; HYR; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000189057};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2185
FT /note="HYR domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038357052"
FT DOMAIN 1667..1781
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1683..1768
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1826..1958
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 2002..2061
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2062..2125
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2128..2185
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1251..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1014..1087
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1251..1280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1968..1983
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2185 AA; 232223 MW; 9525CBC4FA16E9CE CRC64;
MSKKLKTKKV VAGILATGVA AGAVYSVSPT AVTFATGDDP DKSDGPQLMV GEDETARMSA
VDLQHAINNS SKVDPFILHT SVVLEDLFDS ITIGAGQALI IGLGGELIVS ENSSVSIESG
ASMTVGGGIV VNNGTVSCDS GGLVNGSIGG NSVITSSVEY SIASWSSPNT TTPSALSLDS
QDFVMTLSDL QTYYAILDSA TVSVDGSDID ATDKWVTKED YDEFKDAIQL VENALVTTGA
TSEHFATLNA ALTKYEDSMQ AGRKPVEVTD QTGFDAAIEA GALYITIVTD DEDGITIAAD
SAINNEELEI TIESGTLTVE AGASITVKSI TIMPGAKLVD STTDTSGITG EIIIYGNGSY
EGDGATTETI DSITVSSSDE LAEALEAGYS TITIDTSFTL DSTFTYGDTE EIVVVDETTD
SIKFIINDGV TLTIDNAPLT IATIDIEVNG VLDLVSIDTT DTTIGAISGA GTVIVYDEDG
LDLVAEANAP NITIDAADAD GSVSISETID ASSSILTIAA NVIVTVDGAL NDVKSIVIEE
GGVLDLTGEL TLGSYGTISG DGKVIVYDEA NLKIVLEADA PNVTLSAADT ITISDSLTGT
NTDLIIDSCA VEVAETGTLT VKSIVLENNG TISGEGTWTG QVLGVTLSDT TLLLDIDQEI
VLEAILNPET AINQDVTWEI DGKSMIDYDE NYTGLTLDIT AISAGTVTIT VTTDDGDHTA
TCTLQIIDAS KLDDEDLLDM LNELAQLISD AEDLLANVTI SEDGTDVLQY YEWVTQEDYD
ALAEAIESAK DDWSDTDATV FTLTPAISDL EAAIAKFEAS TEFGKSSDFN SLRLELEERI
TQATANLNSV EISEDGTDIE TTLQWVTEET WNAYKQAIAD NDIGNNASIG VHDLTTAIAN
LAEATTEFDK AKQDGTSTDS GSVDSVDKTD LSDAIANAKE HLASVEISVD GSDIATDLYW
VTPATQGYYQ AVIDTAQAVY DNDDATQDNV TAAITNLETA AKTFDAAKAL GSFKEETGEV
ENELEDNLNE ELEELTQEEM EELVEDLQAE VDKVEITQDD LKSPSILAEV LNAIESVQQT
LVQLVDNLLE SLTTPPDIDV KSRKINPDKG TLTQRGTQVV YEFYITVEYT NLLTRTTETE
TMDLGPFEMV LSDTTLPTVE ATAPSLDDCE IKTTTTSALT LDVTGHDTWA AGITKVTATN
GDSSVDLTDY DVVDGSLTIN IDDLIATAGE YTITIVSTDF DNVTFTLTIV EDDEDGDTDT
DEDDDTSTDE DDDTSTDNEA EAPSFEDVTT TSAITLDVAG HETWADGITA VTAKIDSTIY
DLTEDVTVVG SSLTIEIDKL IATPGVYTIT IVSDGFDNVT FTLTIEDEDG GTDTDGEDDY
VGPTINGKEF VLNEDGTQGS ITIDLGDQDE DFTLTSLFDD LLDSDGNKIT VDDDSIIFAD
ADGNVIVAGE VTAPGTYTIS YSFSDNDVEY TVTFTVTLVE SAEDDDSELS EYLEGLLEDL
GVDIEDIEEI QSLDFRDIDL SNADEFDFTG LELFTGLQQL IVDGNLMEVT NFIDALELLI
DALENKDDFE LELDFSGIDF DDDEIAEYMA DWNYGVKIRP FRSVQSYEPS ESIIIEAFTS
TADILAKLPT HITITSALNY EFEVAVTWSG PFSTDTVGDL TYTAAFASDV VEYDLVEGVE
APTVTVTVVD TTAPEFDYTG ETQFTVAQNA TFTVPTITAT DAVDGQITAV PSIDSVDTTT
LGTTTITYTA TDNSGNTATM TITVTVVADA TTDNDTTAPV FNYTGATSLT VEQGASFTPP
TITATDAVDG DVNVSVTGTV NTSVIGEYVL TYTATDSSNN TATMTITVTV HKDQTAPVIN
YSGSTSTTIV QGGHYTIPTI TAVDNVDGYV TANYTVTRNG IPVNTVTTNT VGTYVITYTA
TDSAGNTSAP LVITVRVIYS SSSSSGGNYY PSYNYPNFST SSSVSQVVTD DDDEDEETEQ
DEDVVTNTSS TVVVTPTTPI DISKVFSDVA MSDWFYADVA SVYTKGLIRG VTDTEFMPYE
SATRAQLATI LHRLDGNVQV PSFSGFLDVS NGAWYTPSIA WATDAGIYNG YEDGTFRPDL
EITREQLVTV LHNYAHYKGY NTSKVSAISS YSDSDQVSAW ATPAMQWAVG NNIIGGKDGN
ILDPSGTATR AEIAAIITRF INNVR
//
