dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Ascosphaera apis

Lineage

Ascomycota; Eurotiomycetes; ; Ascosphaeraceae; Ascosphaera; Ascosphaera apis

CAZyme ID

KZZ92659.1

CAZy Family

GH72

CAZyme Description

Laccase TilA [Source:UniProtKB/TrEMBL;Acc:A0A167ZHC5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
838		93273.00	4.8982

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AapisARSEF7405	6442	392613	0	6442

Gene Location

Enzyme Prediction help

No EC number prediction in KZZ92659.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	56	625	1.7e-77	0.9748603351955307

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
206661	Rab1_Ypt1	4.54e-129	645	810	1	166	Rab GTPase family 1 includes the yeast homolog Ypt1. Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
206659	Rab8_Rab10_Rab13_like	2.78e-107	644	810	1	167	Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13). Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
197555	RAB	1.20e-96	647	810	1	164	Rab subfamily of small GTPases. Rab GTPases are implicated in vesicle trafficking.
395024	Ras	1.69e-94	648	809	1	162	Ras family. Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.
206640	Rab	2.85e-91	647	805	1	159	Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases). Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.40e-165	51	643	44	599
1.98e-165	51	643	44	599
3.11e-152	50	643	35	589
4.23e-149	50	643	35	589
4.23e-149	50	643	35	589

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.66e-100	633	812	3	182	Crystal structure of the GTP-bound Rab1a in complex with the coiled-coil domain of LidA from Legionella pneumophila [Homo sapiens]
1.94e-100	636	812	5	181	Crystal structure of LepB GAP domain from Legionella drancourtii in complex with Rab1-GDP and AlF3 [Homo sapiens]
1.96e-100	636	812	15	191	Crystal structure of human RAB1A in complex with GDP [Homo sapiens]
1.48e-99	640	811	1	171	EspG-Rab1 complex [Homo sapiens],4FMC_D EspG-Rab1 complex [Homo sapiens],4FMD_B EspG-Rab1 complex structure at 3.05 A [Homo sapiens],4FMD_D EspG-Rab1 complex structure at 3.05 A [Homo sapiens],4FME_B EspG-Rab1-Arf6 complex [Homo sapiens],4FME_E EspG-Rab1-Arf6 complex [Homo sapiens]
2.09e-99	633	811	3	181	Crystal structure of the GDP-bound Rab1a S25N mutant in complex with the coiled-coil domain of LidA from Legionella pneumophila [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.18e-136	51	643	36	592	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
3.46e-126	51	639	32	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
4.38e-124	60	643	62	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
3.50e-123	51	643	32	597	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
8.92e-121	51	643	37	600	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000958	0.999033	CS pos: 22-23. Pr: 0.9708

TMHMM Annotations download full data without filtering help

Start	End
2	24

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