General Information |
MoonProt ID | 436 |
First appeared in release | 3.0 |
Name(s) | Heat shock protein SSA2, |
UniProt ID | P46587 |
GO terms | GO:0000166 nucleotide binding
GO:0005524 ATP binding
GO:0005576 extracellular region
GO:0005618 cell wall
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosolGO:0005886 plasma membrane
GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation
GO:0006986 response to unfolded protein
GO:0009277 fungal-type cell wall
GO:0009636 response to toxic substance
GO:0009986 cell surface
GO:0015833 peptide transport
GO:0016020 membrane
GO:0016192 vesicle-mediated transport
GO:0016887 ATPase activity
GO:0019730 antimicrobial humoral response
GO:0030446 hyphal cell wall
GO:0031072 heat shock protein binding
GO:0034620 cellular response to unfolded protein
GO:0042026 protein refolding
GO:0042277 peptide binding
GO:0044183 protein folding chaperone
GO:0051082 unfolded protein binding
GO:0051085 chaperone cofactor-dependent protein refolding
GO:0051787 misfolded protein binding
GO:0062040 fungal biofilm matrix |
Organisms for which functions have been demonstrated | Candida albicans (yeast, a fungi) |
Sequence length | 645 amino acids |
FASTA sequence | >sp|P46587|HSP72_CANAL Heat shock protein SSA2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=SSA2 PE=1 SV=4
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRKFDDHEVQGDIKHFPFKVVDKASKPMIQVEYKGETKTFSPEEISSMILGKMKETAEGFLGTTVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKKSEAEKNVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNFFIQEFKRKNKKDISTNQRALRRLRTACERAKRTLSSSAQTSIEIDSLYEGIDFYTSITRARFEELCADLFRSTLEPVDKVLSDAKIDKSKVDEIVLVGGSTRIPKVQKLVSDYFNGKEPNRSINPDEAVAYGAAVQAAILSGDTSSKTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSETFSTYADNQPGVLIQVFEGERAQTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIEKMVSEAEKFKEEDEKEASRVQAKNQLESYAYSLKNTLGEEQFKSKLDASEIEEVTKAADETISWLDANQTATQEEFADQQKELESKANPIMTKAYQAGATPSGAAGAAPGGFPGGAAPEPSNDGPTVEEVD |
Structure Information |
PDB ID | NA |
Quaternary structure | NA |
SCOP | NA |
CATH | NA |
TM Helix Prediction | no TM helices |
DisProt Annotation | Not in DisProt |
Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
moonID_436_uniID_P46587 is 645 residues long, with 157 residues (24.34%) predicted as disordered.The protein has 0 short (< 30 residues) disorder segments and 1 long (>= 30 residues) disorder segment.
Segment 1 - Long (>= 30 residues) disordered segment Segment is located between positions 489 and 645 in the sequence. The segment is 157 residues long (24.34 % of the total sequence length). |
Connections to Disease |
OMIM ID | |
Function 1 |
Function description | Chaperone; helps adapt to temperature variations |
References for function | Cuellar-Cruz, M.; Gutierrez-Sanchez, G.; Lopez-Romero, E.; Ruiz-Baca, E.; Villagomez-Castro, J.C.; Rodriguez-Sifuentes, L. Identification of Candida albicans heat shock proteins and Candida glabrata and Candida krusei enolases involved in the response to oxidative stress. Cent. Eur. J. Biol. 2013, 8, 337–345. |
E.C. number | NA |
Location of functional site(s) | NA |
Cellular location of function | NA |
Comments | NA |
Function 2 |
Function description | Binds HTN3/histatin-5, a peptide from human saliva |
References for function | NA |
E.C. number | NA |
Location of functional site(s) | NA |
Cellular location of function | cell surface |
Comments | |