dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: OTA24539.1

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Basic Information help

Species

Hortaea werneckii

Lineage

Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii

CAZyme ID

OTA24539.1

CAZy Family

CE5

CAZyme Description

PPIase cyclophilin-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1Z5SUP9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
527	MUNK01000240\|CGC1	58422.79	4.1919

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in OTA24539.1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE16	201	511	2.9e-67	0.9925093632958801

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238907	cyclophilin_ABH_like	2.70e-64	7	184	1	161	cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.
238194	cyclophilin	3.88e-54	10	183	1	144	cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.
240249	PTZ00060	4.31e-52	6	183	15	176	cyclophilin; Provisional
238882	fatty_acyltransferase_like	6.09e-52	200	514	1	270	Fatty acyltransferase-like subfamily of the SGNH hydrolases, 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. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.
178694	PLN03149	3.81e-51	3	184	15	181	peptidyl-prolyl isomerase H (cyclophilin H); Provisional

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
2.82e-239	1	523	1	604
7.55e-237	1	523	1	604
1.10e-158	193	525	38	366
1.30e-153	186	526	28	369
1.84e-152	186	526	44	385

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.06e-43	7	185	11	173	Crystal structure of a U4/U6 snRNP complex between human spliceosomal cyclophilin H and a U4/U6-60K peptide [Homo sapiens],1QOI_A U4/U6 snRNP-specific cyclophilin SnuCyp-20 [Homo sapiens],5O9Z_M Cryo-EM structure of a pre-catalytic human spliceosome primed for activation (B complex) [Homo sapiens],6AHD_W Chain W, Peptidyl-prolyl cis-trans isomerase H [Homo sapiens]
1.58e-42	4	183	24	190	Chain A, Peptidyl-prolyl cis-trans isomerase G [Homo sapiens]
6.54e-42	4	183	7	173	Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in complex with cyclosporin A. [Homo sapiens]
9.10e-42	4	183	7	173	Atomic resolution crystal structure of the PPIase domain of human cyclophilin G [Homo sapiens]
9.17e-40	2	210	11	204	Bovine Cyclophilin 40, monoclinic form [Bos taurus],1IIP_A Bovine Cyclophilin 40, Tetragonal Form [Bos taurus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.48e-89	198	525	27	345	Acetylesterase OS=Hypocrea jecorina OX=51453 GN=aes1 PE=1 SV=1
1.20e-43	6	184	12	174	Peptidyl-prolyl cis-trans isomerase H OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CYP3 PE=3 SV=1
1.20e-43	6	184	12	174	Peptidyl-prolyl cis-trans isomerase H OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CYP3 PE=3 SV=1
3.12e-42	7	185	11	173	Peptidyl-prolyl cis-trans isomerase H OS=Bos taurus OX=9913 GN=PPIH PE=2 SV=1
3.12e-42	7	185	11	173	Peptidyl-prolyl cis-trans isomerase H OS=Homo sapiens OX=9606 GN=PPIH PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000048	0.000000

TMHMM Annotations help

There is no transmembrane helices in OTA24539.1.