CAZyme Information: KAF5673623.1

Basic Information

• Species: Fusarium circinatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum
• CAZyme ID: KAF5673623.1
• CAZy Family: GH15|CBM20
• CAZyme Description: P-type ATPase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1075		116692.55	5.9868

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FcircinatumNRRL25331	13905	N/A	0	13905

• Gene Location: location=JAAQPE010000261:39805-44705(+)

Full Sequence      

MVISKIKADAPLVHAILFKTLEHARFDVSAEDLSILVQKARARIHPETCSTQDASKTYLL
KELNRLVYNGLRLHPRVTQIVTIVDARKARNMAREYFGNCITAVDTPYLPASKNLSAVAF
AIREGVAGLTPEKLAKGDEWIQSVQAVNGLMDLAPAFDTDTLLLMQEMRRAWDTAIDPSQ
WLNARGKADSLISKMTLEEKSSMVTGTFDGTCIEYIAPIKRLGFGGLCIQDGPIGLRLGD
LVSVFPSGVTTAATWDRQLMALRGEAMAEEFKAKGAHIMLGPVAGALGRSPYGGRNWEGF
SPDPYLTGIAMDETIRAIQDTGVQATAKHLVGNEQETQRKATLINGKMVDAVSSNIDDRT
MHELYMWPFADAVHAGVSSVMCGYNRINAVAPSLDGNPVEESRANDVAKFLGLDDFFNLP
KSIIMACCAVGAYIVFRFLSMHEKLCTLYPRQNNVMRNPAQRPKSIKGAQVSILSLDGLT
CASCKSDVQDIIGSIPGVLKATVSLGLLRAQVEFNSDVVTEEEIIEAIRSSGYDAHSLPS
SESQSWASLLSMMQEPSNSQRHHVNSCQRDFLVATTASVLFFASRSINALWTTQHNYMNL
IAYFAVAMSLLAVSQLHVEALRSAWHGRRPDMATLASLGIMLALVQAATDSSQTGMNRSY
HMDSKSLEVIPILSTSVLGGRFLKAILSQRNRVFASPLSSLIPTMAMVCNKTDKHISIPI
DLLSLGDTVIVKQGEHIPCDGVVESTESALVTETWINGSLEPRVVEHGDALQCEHRSLES
VTHASFCEEWGSSPKQAILWRAVQEVEVENTHPVGRALFQESSSRLGDEQECLTSLTVSE
IKHELGRGAQAVVTLTHPGSDATTQNLAIGSRAYIESLGVSVDLSQIPVNMRTGITTTVV
LAIDGKQTAVFVLEDKVRSNAHQVIRQLKDLGLTIGMITGDNAASATSVAREVGIDSDMV
FANALPEEKSRVLAQFLQRGPAIYVGDNYNDILCFASASFSICIAGSDMTSVEDDCADAM
LMASETSPLSRIPLMICLSRRMSSIVTQNHSWAVIYNILSVAWVLGIVGSGPPSP

Enzyme Prediction     

EC	3.2.1.-:5	3.2.1.21:4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH3	218	393	5.6e-43	0.75

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225127	ZntA	2.49e-55	474	1068	6	683	Cation transport ATPase [Inorganic ion transport and metabolism].
319774	P-type_ATPase_HM	3.08e-44	573	1074	2	598	P-type heavy metal-transporting ATPase. Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
319783	P-type_ATPase_Cu-like	2.16e-39	569	1061	1	607	P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
319849	P-type_ATPase_HM_ZosA_PfeT-like	1.94e-35	799	1069	338	588	P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which transports copper, and perhaps zinc under oxidative stress, and perhaps ferrous iron. Bacillus subtilis ZosA/PfeT (previously known as YkvW) transports copper, it may also transport zinc under oxidative stress and may also be involved in ferrous iron efflux. ZosA/PfeT is expressed under the regulation of the peroxide-sensing repressor PerR. It is involved in competence development. Disruption of the zosA/pfeT gene results in low transformability. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.
319850	P-type_ATPase_Cu-like	4.46e-29	806	1067	361	600	P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase. Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD56596.1|GH3	3.59e-206	2	388	980	1474
ATQ35965.1|GH3	3.05e-95	176	391	44	259
QQK45461.1|GH3	2.77e-89	173	388	22	237
UKZ78727.1|GH3	2.58e-80	181	388	38	248
QGI97665.1|GH3	3.08e-76	181	388	62	273

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4IIB_A	1.37e-65	178	388	11	233	Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIB_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIC_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IIC_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IID_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IID_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IIE_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIE_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIF_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIF_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIG_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIG_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIH_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus],4IIH_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus]
6SZ6_A	1.07e-64	178	388	9	228	Chain A, Beta-glucosidase [Thermochaetoides thermophila]
5JU6_A	1.54e-63	171	388	23	249	Chain A, Beta-glucosidase [Rasamsonia emersonii],5JU6_B Chain B, Beta-glucosidase [Rasamsonia emersonii],5JU6_C Chain C, Beta-glucosidase [Rasamsonia emersonii],5JU6_D Chain D, Beta-glucosidase [Rasamsonia emersonii]
5FJJ_A	5.76e-63	171	388	5	234	Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_B Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_C Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_D Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae]
5FJI_A	5.90e-63	180	388	20	234	Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus fumigatus],5FJI_B Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus fumigatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q5B0F4|BGLG_EMENI	6.02e-74	181	388	66	277	Probable beta-glucosidase G OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=bglG PE=3 SV=2
sp|B8NMR5|BGLG_ASPFN	7.68e-74	181	388	65	276	Probable beta-glucosidase G OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=bglG PE=3 SV=1
sp|Q2U325|BGLG_ASPOR	7.68e-74	181	388	65	276	Probable beta-glucosidase G OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=bglG PE=3 SV=1
sp|Q0CUC1|BGLG_ASPTN	1.13e-71	181	388	65	276	Probable beta-glucosidase G OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=bglG PE=3 SV=1
sp|A1DC16|BGLG_NEOFI	1.13e-71	180	388	64	276	Probable beta-glucosidase G OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=bglG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000058	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KAF5673623.1.