Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  72 TLNINDEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVT 151
Cdd:cd06526    1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEEREDEHGYVSREFTRRYQLPEGVDPDSVTSSLSSDGVLTIE 80

                 ...
gi 822092484 152 APM 154
Cdd:cd06526   81 APK 83

Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  72 TLNINDEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVT 151
Cdd:cd06526    1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEEREDEHGYVSREFTRRYQLPEGVDPDSVTSSLSSDGVLTIE 80

                 ...
gi 822092484 152 APM 154
Cdd:cd06526   81 APK 83

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  76 NDEKFEVILDVQQFSPNEISVKVTDKFVIVEA--KHEEKQDEHGFVLR-----QFTRRYMLPSDVNPDSVTSSLsSDGLL 148
Cdd:COG0071    7 TDDAYVITADLPGVDKEDIDVTVEGNVLTISGerKEEEEEEGENYLRRerrygSFERSFTLPDDVDVDKIEASY-ENGVL 85

                         90       100
                 ....*....|....*....|.
gi 822092484 149 TVTAPMKklpPPATERVVPIS 169
Cdd:COG0071   86 TITLPKA---EEAKPRKIEIK 103

Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  72 TLNINDEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVT 151
Cdd:cd06526    1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEEREDEHGYVSREFTRRYQLPEGVDPDSVTSSLSSDGVLTIE 80

                 ...
gi 822092484 152 APM 154
Cdd:cd06526   81 APK 83

Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. HspB4 does not belong to this group. HspB5 shows increased synthesis in response to stress. HspB5 is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. Its functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  73 LNINDEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTA 152
Cdd:cd06498    2 MRLEKDKFSVNLDVKHFSPEELKVKVLGDFIEIHGKHEERQDEHGFISREFQRKYRIPADVDPLTITSSLSPDGVLTVCG 81

                 ...
gi 822092484 153 PMK 155
Cdd:cd06498   82 PRK 84

Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822092484  78 EKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTAP 153
Cdd:cd06497   10 DKFTIYLDVKHFSPEDLTVKVLDDYVEIHGKHSERQDDHGYISREFHRRYRLPSNVDQSAITCSLSADGMLTFSGP 85

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB2/heat shock 27kDa protein 2 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB2 is preferentially and constitutively expressed in skeletal muscle and heart. HspB2 shows homooligomeric activity and forms aggregates in muscle cytosol. Although its expression is not induced by heat shock, it redistributes to the insoluble fraction in response to heat shock. In the mouse heart, HspB2 plays a role in maintaining energetic balance, by protecting cardiac energetics during ischemia/reperfusion, and allowing for increased work during acute inotropic challenge. hHspB2 [previously also known as myotonic dystrophy protein kinase (DMPK) binding protein (MKBP)] is selectively up-regulated in skeletal muscles from myotonic dystrophy patients. The ACD of hHspB2 binds the DMPK kinase domain. In vitro, hHspB2 enhances the kinase activity of DMPK and confers thermoresistance. The hHspB2 gene lies less than 1kb from the 5 prime end of the related alphaB (HspB4)-crystallin gene, with the opposite transcription direction. These two genes may share regulatory elements for their expression.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092484  77 DEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTAP 153
Cdd:cd06476    6 DDKYQVFLDVCHFTPDEITVRTVDNLLEVSARHPQRMDRHGFVSREFTRTYILPMDVDPLLVRASLSHDGILCIQAP 82

Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) HspB8, also denoted as Hsp22 in humans, and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. A chaperone complex formed of HspB8 and Bag3 stimulates degradation of protein complexes by macroautophagy. HspB8 also forms complexes with Hsp27 (HspB1), MKBP (HspB2), HspB3, alphaB-crystallin (HspB5), Hsp20 (HspB6), and cvHsp (HspB7). These latter interactions may depend on phosphorylation of the respective partner sHsp. HspB8 may participate in the regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis. Point mutations in HspB8 have been correlated with the development of several congenital neurological diseases, including Charcot Marie tooth disease and distal motor neuropathy type II.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092484  77 DEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTAPM 154
Cdd:cd06480   14 SEPWKVCVNVHSFKPEELTVKTKDGFVEVSGKHEEQQKEGGIVSKNFTKKIQLPPEVDPVTVFASLSPEGLLIIEAPQ 91

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB9 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Human (h) HspB9 is expressed exclusively in the normal testis and in various tumor samples and is a cancer/testis antigen. hHspB9 interacts with TCTEL1 (T-complex testis expressed protein -1), a subunit of dynein. hHspB9 and TCTEL1 are co-expressed in similar cells within the testis and in tumor cells. Included in this group is Xenopus Hsp30, a developmentally-regulated heat-inducible molecular chaperone.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  78 EKFEVILDVQQFSPNEISVKVTDKFVIVEAKHEEKQ-DEHGFV---LRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTAP 153
Cdd:cd06481    7 EGFSLKLDVRGFSPEDLSVRVDGRKLVVTGKREKKNeDEKGSFsyeYQEFVREAQLPEHVDPEAVTCSLSPSGHLHIRAP 86

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092484  78 EKFEVILDVQQFSPNEISVKVTDKFVIVeakHEEKQDEHGFVLRQFTRRYMLPSDVNPDSVTSSLSSDGLLTVTA 152
Cdd:cd06479    8 DTYQFAVDVSDFSPEDIIVTTSNNQIEV---HAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKA 79

Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to Lactobacillus plantarum (Lp) small heat shock proteins (sHsp) HSP 18.5, HSP 18.55 and HSP 19.3. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Transcription of the genes encoding Lp HSP 18.5, 18.55 and 19.3 is regulated by a variety of stresses including heat, cold and ethanol. Early growing L. plantarum cells contain elevated levels of these mRNAs which rapidly fall of as the cells enter stationary phase. Also belonging to this group is Bifidobacterium breve (Bb) HSP20 and Oenococcus oenis (syn. Leuconostoc oenos) (Oo) HSP18. Transcription of the gene encoding BbHSP20 is strongly induced following heat or osmotic shock, and that of the gene encoding OoHSP18 following heat, ethanol or acid shock. OoHSP18 is peripherally associated with the cytoplasmic membrane.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  76 NDEKFEVILDVQQFSPNEISVKVTDKFVIVEAKHE---EKQDEHGFVLRQ------FTRRYMLPsDVNPDSVTSSLsSDG 146
Cdd:cd06471    8 TDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRDeskDEKDKKGNYIRReryygsFSRSFYLP-NVDEEEIKAKY-ENG 85

                 ....*..
gi 822092484 147 LLTVTAP 153
Cdd:cd06471   86 VLKITLP 92

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092484  85 DVQQFSPNEISVKVTDKFVIV---EAKHEEKQD----------EHGFVlrqftRRYMLPSDVNPDSVTSSLsSDGLLTVT 151
Cdd:cd06472   16 DVPGVKKEDVKVEVEDGRVLRisgERKKEEEKKgddwhrversSGRFV-----RRFRLPENADADEVKAFL-ENGVLTVT 89

                 ..
gi 822092484 152 AP 153
Cdd:cd06472   90 VP 91