CAZyme Information: RL4_JR_00181-RA-p1

Basic Information

• Species: Raffaelea lauricola
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
• CAZyme ID: RL4_JR_00181-RA-p1
• CAZy Family: AA1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1470	JACBXF010000169|CGC16	161430.70	5.0978

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RlauricolaRL4	10461	N/A	146	10315

• Gene Location: location=JACBXF010000169:613589-619948(-)

Full Sequence      

MVDVSLDLDLAARRELPQSLAAHDTVSQRKRVAVELDWDQIAVIAVAVVKGYTKPFFLRI
APLGASITYGYLSSDGNGYRKYLRDELRLNGWPVNMVGSVKNGTMNDNDNEGHPGWTIQQ
VTSFALPNIVKDQPNLVLINVGTNNAIQDNSVSTASDLYIQLLDKLWDDIPNATVILSTL
LRNEESATDTRVEQINKQIRSAVKSHYRSKKLLVADMDDGFITKADLKDGTHPTDEGYKK
MAAVWWDAIRKTDSAGWLSAPPDTGTSDNATTSGTGSFTCPKVYGSGDGNYQIQKGSGTD
DGNYVYKATTDGSYRWVNSYGASSASIDHYGQLFFAQLVNKGGNPVRGGEVDEIIWRSAQ
TGKWHFWINNNNDQFDKNDQVFDPGYTCQPANSRFADLNNDGLDDFLCIDADGNLWASIN
QGGNPPKFKAAGIIGAAPDFWSDGYTADRVHIADIDGDGRADWCILLHSGDISCHRNGGQ
GDVPTPSQGGYWQDFQSGGSGWTTVFPSQHKGNAAGVHLVDINGDFKADWVFVHEEGRAD
IFINNRGTGVGLVPHWRQASGPENNFGPSTIHGSQRVKFGRMYGTGRRDYIWLGENKNTD
DNRWHIAIEIFKNLGKGATTLKGDGTHYCDMNGDGKDDYIWVGPNGEIDIYLNTDNRPYW
DNHMGVITQGVPRKTIHVADLDGDGKCDLLSVDRATGAVRMWLNRWDGKKKKFSFADHGV
ISGSAGCKQGYGVIENDLGVRFADLTGDGKSDYLCIETNGRVTGFLNQGMTSAGKITFKD
VGQIKKATQYDRQNVRFNDVNGDGRADLIWVNKYNGHATVWYNGGQIPTDGSAFQWNNQG
VLYKGWDRGANMHFGALGGQHRADMIQVLPATNQAYISYNKCPGGKGGDDANWGDPKLPQ
YSTSSNTTCPLGQVCAQSAPHFVDDSCSAEQQAIIRQELDHALNMAIAAQGDSLTGKYYQ
KFFPDVLRDRSDFEETTRKRYENMQAMLSADGTAEYDFQKNREGKCAPEVAEKNADTYMF
VAAGIYFSQQCGGEIRFPGESVKRDVAVGTRQDDGESCPSVPNFRQPVTFDGSLGTYVHF
GDSFAAGMGTGTTGGAPCRIGSNNFGKLLSGHLNQTYTGPPVPFELRPCSGASLTGLTKQ
VDAWDSGPSTSFATLSIGGNDVNFTNLVKDCILVPNWFTSVDQDRANCVEDQNKAYAHMA
DTSTSGLRHRLKEAYLDIVRKAGTYFFTLYVTGYPHFFNAETHDCNFTAFNYWRGDYFPH
RANNPGSLVLLTESLRAEMNTLVQTLNSVIQGAVEDALQEVPWQVKYVDIALRFTGGRHH
WCENPNAEFHEPYRNRKETWFFLSSWPDVPIEGAADVTDTEEAAAVAAIIDNGSFSLPDA
ATCSSSLGTDPDPYAVALCDLAINVEKSPDGDEAQNYAQALQDVANRNSSSEFIRAALPM
RYAKTFHPRSPGMAAYRDAILEAMNEMGQL

Enzyme Prediction     

No EC number prediction in RL4_JR_00181-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE3	58	249	2.8e-60	0.9948453608247423

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238871	XynB_like	2.02e-41	58	249	1	157	SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
238861	SEST_like	1.50e-29	1077	1325	3	224	SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.
238141	SGNH_hydrolase	1.62e-17	60	248	1	187	SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
404371	Lipase_GDSL_2	2.85e-17	63	240	2	176	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
239945	SGNH_hydrolase_like_4	1.14e-09	59	249	2	183	Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDD56943.1|CE0	3.26e-208	54	912	52	874
ABA65775.1|CE0	5.09e-187	58	1439	59	1527
AAD34550.1|CE0	5.09e-187	58	1439	59	1527
CCT73237.1|CE3|GH43_30	2.38e-178	56	903	77	902
AEO70515.1|CE3	2.90e-170	54	874	99	883

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4HYQ_A	3.62e-14	1073	1316	1	195	Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 [Streptomyces albidoflavus]
2VPT_A	8.14e-14	58	246	6	192	Chain A, LIPOLYTIC ENZYME [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9RLB8|CESA_RUMFL	5.10e-13	58	249	44	260	Multidomain esterase OS=Ruminococcus flavefaciens OX=1265 GN=cesA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000074	0.000002

TMHMM  Annotations     

There is no transmembrane helices in RL4_JR_00181-RA-p1.