CAZyme Information: ALNC14_087880:RNA-p1

Basic Information

• Species: Albugo laibachii
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
• CAZyme ID: ALNC14_087880:RNA-p1
• CAZy Family: GH5
• CAZyme Description: glycoside hydrolase putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
873		97456.75	8.5932

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlaibachiiNc14	14629	890382	180	14449

• Gene Location: location=FR824207:22777-25625(+)

Full Sequence      

MTEEVKGIQVFIPAALNRPTHTLYNIFTLVQPVEQEWMVNRRYSQFLQLRQDLCACLTEH
QKCPRCPVVLSQILKFTFPHKTLFRTNRIVRKRVKLLQEFLHLLLQLIYLDNTPKCSTCN
HSIRNIIRPFLIRGAQPVGSSELIEIQSALSLPSYDVATRSAKTSAVPLNLEASYSSTIE
SDDPDQKGDQWDSSREEEKAGFFRSRNYGDERCYDPVLPLEEAIKEVVVAEGLPCSKEDV
VARLSTMWRAYEGTPIEKSRLSMNPKSRFKFIVASFGSGLEYSPNLLLAFPFFYEHCGNL
KRTRLIMLPRALSLLSLGLCIWQVGGQVAAPIIVRGNKLYNAKTKERFVIIGMTYEYAVS
DTYYIKYSKEILKTKLAGLKYNTLRLYDVNPEETYDIFMKDMAEINVYVIISVSPDNNPY
YGKYRYSTIDRTLPANGKDLTKTCYPALLLEYGKKIIKKFAVHDNLLAILIGNEILQVNL
KAAACVKQYAADLKNWMRVNGKKIRLIPLAYAAADSSYAGLIEDADKYHLLKIQGLLCGD
RMSNGMMVKSIDIYLINEYRFCPGSTFEEAYERFLTLAKGIPIVIALGEYGCKLSKGEPR
TWEMIPYLYDPPSKTQGFSEVFSGGLAYSYGEAKLSSASLFPMFTGGSSEITGKPSDKPS
KDFSNLKEALSKHKPFSDKAAWTKDTICKWTPPLKYKIDPKSGIASKGFILPTCNAPELK
PKKDDTWVTQSREGVICTDRGAPCDVVIHGKVGTTQESICGEYEVESGGGTCSSSNDCGS
NGQCAITKGVGTCHCLACYTGADCSIKDTSSCLELTSSPTAPKFIFMGVGIFLVFMLFIF
VALGILAKKKASVLSELRTEIKSRSTGQNTAGM

Enzyme Prediction     

No EC number prediction in ALNC14_087880:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH72	329	671	8.2e-75	0.9775641025641025

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397351	Glyco_hydro_72	4.27e-32	331	672	11	313	Glucanosyltransferase. This is a family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases. The active site residues in the Aspergillus fumigatus example are the two glutamate residues at 160 and 261.
132810	PX_RUN	1.64e-04	8	84	1	66	The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.
132768	PX_domain	6.24e-04	20	95	16	79	The Phox Homology domain, a phosphoinositide binding module. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.
132807	PX_SNARE	8.64e-04	9	54	2	46	The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.
395635	PX	0.002	34	95	6	56	PX domain. PX domains bind to phosphoinositides.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA22645.1|GH72	0.0	1	873	1	873
CCA15473.1|GH72	1.22e-236	315	865	8	557
UIZ26083.1|GH72	8.47e-226	328	871	27	580
CCA14303.1|GH72	3.12e-159	332	767	60	505
AIG55862.1|GH72	9.86e-144	330	806	20	500

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W62_A	4.01e-16	336	750	40	405	Saccharomyces cerevisiae Gas2p in complex with laminaripentaose [Saccharomyces cerevisiae],2W63_A Saccharomyces Cerevisiae Gas2p In Complex With Laminaritriose And Laminaritetraose [Saccharomyces cerevisiae],5O9O_A Crystal structure of ScGas2 in complex with compound 7. [Saccharomyces cerevisiae S288C],5O9P_A Crystal structure of Gas2 in complex with compound 10 [Saccharomyces cerevisiae S288C],5O9Q_A Crystal structure of ScGas2 in complex with compound 6 [Saccharomyces cerevisiae S288C],5O9R_A Crystal structure of ScGas2 in complex with compound 9 [Saccharomyces cerevisiae S288C],5O9Y_A Crystal structure of ScGas2 in complex with compound 11 [Saccharomyces cerevisiae S288C],5OA2_A Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_B Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_C Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA6_A Crystal structure of ScGas2 in complex with compound 12 [Saccharomyces cerevisiae S288C]
2W61_A	9.27e-16	336	750	40	405	Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) [Saccharomyces cerevisiae]
5FIH_A	9.27e-16	336	750	40	405	SACCHAROMYCES CEREVISIAE GAS2P (E176Q MUTANT) IN COMPLEX WITH LAMINARITETRAOSE AND LAMINARIPENTAOSE [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q08193|GAS5_YEAST	1.73e-18	307	672	1	329	1,3-beta-glucanosyltransferase GAS5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAS5 PE=1 SV=1
sp|Q9Y7Y7|GAS4_SCHPO	1.06e-17	313	630	9	298	1,3-beta-glucanosyltransferase gas4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas4 PE=1 SV=1
sp|O13692|GAS5_SCHPO	1.46e-17	313	632	10	304	1,3-beta-glucanosyltransferase gas5 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas5 PE=1 SV=1
sp|Q08271|GAS4_YEAST	6.50e-17	368	632	71	302	1,3-beta-glucanosyltransferase GAS4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAS4 PE=1 SV=1
sp|P0C954|GEL2_ASPFU	6.65e-17	307	630	1	296	1,3-beta-glucanosyltransferase gel2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gel2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000003

TMHMM  Annotations     

Start	End
824	846