CAZyme Information: EKG11838.1

Basic Information

• Species: Macrophomina phaseolina
• Lineage: Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
• CAZyme ID: EKG11838.1
• CAZy Family: AA7
• CAZyme Description: Chitin-binding type 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
689	AHHD01000467|CGC3	74868.16	4.8414

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MphaseolinaMS6	14712	1126212	906	13806

• Gene Location: location=AHHD01000467:915774-918013(-)

Full Sequence      

MSSLFGNCCSKNGFCGATAEYCGDGCQLEFGICEKTEGTVSQDGTCGGALGYTCEGSKFG
ECCSQYGYCGSTGAYCDDGCRADHGKCNAGLQARQEYAAPSLATSSAVAQPSSPPANGKP
TPGQGGSTCSAKRSTSLLASRTDSCVRCEGQPGDDQFCGYDIHTDYYKHVPKTCRTVEYT
LEITNQTIAPDGIPRIALLVNGQMPGPTIEANWGDTVKVTVINKMQDNGTTIHFHGIRHH
LTNQYDGVPSVTQCPIPPGESMTYVFVAESYGSSWYHSHFAIQTWEGVFGPVVIHGPSSP
ERQYDVDAGHIMLQDWSHWTVDSQFHLAQDATPGHNGGARVMDNGLINGKNTWGRDGSYN
QTGERFKMTVIKGKSYLLRVINVSIQSTFKFHIDGHSFTVISTDFTPIVPYDTKILNINI
GERYDIIVHADQEVGDYWMRSDNQNTCAGVKQALDIKGIFSYEGSRGGTPATVSQTYTTE
CTDENHSLHVPIVPFDVSEPDVQFYGDVTVEQPDNIFRWYISGNTFNAHWDDPTVLGILD
NGEPPNYSGDLLINAPNEGEWVYVVVESDIALPHPLHLHGHDFFILATGTGRYDASVPLR
LQNPSRRDTVLMPGAGFVVGAFKAENPGAWLMHCHIGWHSAMGFAAQVVELVDQIPQTWD
DGGCELKDMCAAWSAWADARGLVAGDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	164	481	2.2e-125	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	2.05e-68	175	295	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.
259968	CuRO_3_MaLCC_like	4.03e-67	497	649	1	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.
177843	PLN02191	3.37e-65	177	666	24	563	L-ascorbate oxidase
274555	ascorbase	4.84e-65	176	656	1	532	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.
274556	laccase	7.52e-63	174	650	1	520	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	2.44e-227	1	689	43	933
CBX91631.1|AA1_3|CBM18	1.84e-222	40	689	42	732
QDS72137.1|AA1_3	3.07e-190	198	689	1	510
QIX01866.1|AA1_3	1.15e-180	145	689	916	1460
AAY33971.2|AA1_3|1.10.3.2	1.73e-178	196	682	1	487

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.32e-153	159	677	6	529	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.36e-153	159	677	7	530	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.25e-153	159	677	34	557	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3V9E_A	5.25e-134	127	689	27	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.25e-134	127	689	27	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12570|LAC1_BOTFU	1.11e-139	160	689	50	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	1.70e-137	127	689	24	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.25e-135	136	689	27	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q96UM2|LAC3_BOTFU	4.36e-117	205	647	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.57e-112	139	689	20	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 OTHER

Other	SP_Sec_SPI	CS Position
0.999158	0.000878

TMHMM  Annotations     

There is no transmembrane helices in EKG11838.1.