CAZyme Information: XP_001904140.1

Basic Information

• Species: Podospora anserina
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
• CAZyme ID: XP_001904140.1
• CAZy Family: AA5
• CAZyme Description: Amb_all domain-containing protein [Source:UniProtKB/TrEMBL;Acc:B2AEQ1]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
331	CU633457|CGC5	34920.19	8.1277

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

• Gene Location: location=CU633457:402637-403763(+)

Full Sequence      

MKLLGLSVFLALAQATPTPTLPEENTVRLEKRASMSEAATLGFASLNGGTTGGAGGTVTT
VSTLPEFTAAVGEKNTAPTIVVIRGVITGNEKVRIGSNKSIIGLPGSGLRGIGLHFRRQN
NLIVRNIVSSFVVASTAEDALKIEGSTNVWVDHCEFHSTLNSDKDFYDGAVDSSHGSDFI
TVSHTYFHDHWKTSLVGHSDNNGSQDKGKLRITYANNYWKNVNSRAPLLRFGTAHIYNSF
YENMSSAVNTRMGAQALVQSNVFRNVTAAVVSQDSKEVGFAVLEGNELGGGLANAPAGNL
GSSSIPYSFSLLGAGAVPSRVPAEAGAILKF

Enzyme Prediction     

EC	4.2.2.2:5

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	82	263	1.4e-87	0.994475138121547

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214765	Amb_all	4.14e-62	95	266	14	189	Amb_all domain.
226384	PelB	4.82e-56	1	327	1	341	Pectate lyase [Carbohydrate transport and metabolism].
366158	Pec_lyase_C	5.77e-43	92	263	29	211	Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.
240339	PTZ00265	7.60e-04	67	182	66	178	multidrug resistance protein (mdr1); Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAP61917.1|PL1_7	1.45e-232	1	331	1	331
CDP28992.1|PL1_7	1.45e-232	1	331	1	331
VBB80716.1|PL1_7	5.92e-232	1	331	1	331
AEO54996.1|PL1_7	3.23e-169	1	331	1	330
AUT30983.1|PL1_7	1.31e-138	7	331	9	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VMV_A	5.62e-44	42	326	6	321	Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
1PCL_A	4.24e-33	36	241	4	246	Chain A, PECTATE LYASE E [Dickeya chrysanthemi]
5AMV_A	5.49e-28	90	327	116	395	Structural insights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]
1BN8_A	7.12e-28	90	327	137	416	Bacillus Subtilis Pectate Lyase [Bacillus subtilis]
3ZSC_A	1.16e-27	41	263	7	226	Catalytic function and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q00645|PLYB_EMENI	4.77e-87	1	326	1	323	Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1
sp|B0XT32|PLYA_ASPFC	2.99e-84	12	331	15	321	Probable pectate lyase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyA PE=3 SV=1
sp|A1CYB8|PLYA_NEOFI	4.23e-84	12	331	15	321	Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1
sp|Q4WIT0|PLYA_ASPFU	4.23e-84	12	331	15	321	Probable pectate lyase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyA PE=3 SV=1
sp|Q0CBV0|PLYB_ASPTN	6.78e-84	1	326	1	322	Probable pectate lyase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000323	0.999626	CS pos: 15-16. Pr: 0.9728

TMHMM  Annotations     

There is no transmembrane helices in XP_001904140.1.