ID R1HIG5_9PSEU Unreviewed; 696 AA.
AC R1HIG5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Na-Ca exchanger/integrin-beta4 {ECO:0000313|EMBL:EOD58249.1};
GN ORFNames=H480_43670 {ECO:0000313|EMBL:EOD58249.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD58249.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD58249.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD58249.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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:EOD58249.1}.
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DR EMBL; AOUO01000766; EOD58249.1; -; Genomic_DNA.
DR AlphaFoldDB; R1HIG5; -.
DR PATRIC; fig|1292037.4.peg.8184; -.
DR eggNOG; COG2304; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR Proteomes; UP000014139; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00146; PKD; 1.
DR CDD; cd00198; vWFA; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR47763; ALPHA-PROTEIN KINASE VWKA; 1.
DR PANTHER; PTHR47763:SF1; ALPHA-PROTEIN KINASE VWKA; 1.
DR Pfam; PF01083; Cutinase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM01110; Cutinase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00089; PKD; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:EOD58249.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..444
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 450..535
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 547..636
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 628..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 74108 MW; DB85C73E476BFC96 CRC64;
MLVVFARGSG QNFTDKKSDE ADTFYEKIKE NAPGVRIARA DLGNLDGNNR VDAGEYPAVP
MTQWFGIDLK DYFDPDEDAA LDGYNRSRKT GTDELVSFLE HRNCPAETIV LGGYSQGADA
IGSALPKLSS KVLGRVGYVA LFGDPKFWTG SLASRLFGAK APWVRGDFDG YFDEGILGGR
DPYVPESLAS RTGSWCDKLD GLCTGNILQL PPTSHAHFEY PQSEVPQAAN EVAVALRKLR
PDLRSRVFPT LLPVDLRPTE KVDVAFVVDS TGSMADDIDA ARASISRVTD EIFGVAKSAR
VSLVDYKDVD DSYQARVDVP FTESKTEFID AVNGIVVDGG GDDPESIFSG LMAAYAQKWR
PGALKLTILI GDAPAKDPEP RTGYTQAQVL KAAKELDPVV INPILVGGKE ATRTSFEKLA
DGSKGQVYSS ATAADLVKAI DDAMRGFATA PVGQAGGPYK AAVGEPIHFS AAGSFDPDGS
ITKYAWDFND DGKIDETSTS PVVTHSYKKA YKGMAVVTVT GDDGRQNAAT AVVDVGAGLR
APRSPSPPLE VVASQSGPGQ VEISWQPPAS PGDASIDGYR IDRTDGVQIG VVRSEARKFA
VEGVPDETQV QFTVTAVNKF GNGAAGTSNL LRTQAPPSTS APATSAPAGV KPSASSVADV
RLWERPVFWG ISGCAAILLL LLLGIFIRSA RRRQRR
//
