CAZyme Information: QRC99159.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRC99159.1
• CAZy Family: GH154
• CAZyme Description: Chitin-binding type-1 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2F5L2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
933		100177.07	6.1966

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069031:949056-951906(-)

Full Sequence      

MSLLRRAFVCALAVSALVVAHDRPAKELSVSSDGTCGNGMSCVGSPFGGCCSKDGRCGST
SDYCGSGCQMAFGFCQDTKGKVSPDGTCAGSTGYTCAGSTFGSCCSEYHFCGSTSDHCQK
ETCLPGFGDCGINSNHSSSSNQTIHDKTPTHLPTTHGNDEKNHVKSRAAGMACPNSNNTV
HKTHSGAEFQVECGIDHVGGDISWSGNGFITKCLEECIDACARWPGCVDVSWVDQYRPGG
ACYLKDRIGDKTDAGHVAGARLVKKCDGDCPITTPALNKPPFAAPISTGFISVSKSSSPT
GVALVLKDSIASGPTQSISQSTAVHPAPTALSQADSNLAPTIITPTLIASSANATASSLV
SATASASACAHSFTKRADNAVFKRQEIDPDCVPCEGQSGALPYCGADHTTDNYKFTPKTC
RTVYYNFDVTNTTLAPDGIPRIVLAVNGQVPGPLLEANWGDNVVVTVNNKLQDNGTSIHF
HGIRQINNAAHDGVPAITQCPIAPGDSFTYKWTATNYGTSWYHSHYAIQAWEGVAGPMVI
HGPTSASWDVDAGTIMLQDWAHQTVDSMYSMEQDAINGGPRTMDNGLINGMNTWGVEGTR
NQTGKRFELDTKFEAGKTYLLRIINSAMQGTMKFHIDNHELEVINMDFTNIVPYKTNILN
INIGQRYMVLVKANQEPGNYWMRADNQEACAANHQSNDVKGIIRYTGVTKSDVAPSSTAY
EYIGECVDEPLASLVPTAHVNAFSKDKSFTQDISVGANSDNLFKWYLSGDSFYSKYEDPT
LVRVLANNTAPTYSGNLILDLPKMGEWIYIIVESAIPLNHPIHLHGHDFLILGTGSGTYT
DQPLNLQNPPRRDTANMPAAGWLVIAFETDNPGAWLMHCHIGWHTSMGFALQILEGQSMI
KDTVKDTCEMYGTCANWNKWVASRGFKQHDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	410	726	3.6e-126	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.90e-73	746	894	5	157	The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555	ascorbase	2.12e-73	422	896	1	524	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259923	CuRO_1_MaLCC_like	2.71e-70	421	541	2	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
177843	PLN02191	2.82e-70	423	925	24	572	L-ascorbate oxidase
274556	laccase	6.11e-69	420	891	1	515	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC99159.1|AA1_3|CBM18	0.0	1	933	1	933
CBX91631.1|AA1_3|CBM18	1.20e-314	379	933	178	732
AID53024.1|AA1_3	1.04e-204	464	823	1	360
QDS72137.1|AA1_3	1.78e-190	444	933	1	510
QIX01866.1|AA1_3	1.22e-180	388	924	913	1453

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	2.86e-146	387	920	16	562	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	9.09e-146	402	920	3	534	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	9.39e-146	402	920	4	535	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3SQR_A	2.94e-139	384	933	32	580	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	2.94e-139	384	933	32	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J5JH35|OPS5_BEAB2	3.05e-149	358	933	15	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.86e-148	409	933	53	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96WM9|LAC2_BOTFU	4.72e-141	384	933	32	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q96UM2|LAC3_BOTFU	7.98e-118	451	892	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.54e-104	421	933	56	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000356	0.999646	CS pos: 20-21. Pr: 0.9772

TMHMM  Annotations     

There is no transmembrane helices in QRC99159.1.