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Conserved domains on  [gi|1034571992|ref|XP_016872694|]
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PIH1 domain-containing protein 2 isoform X5 [Homo sapiens]

Protein Classification

alpha-crystallin domain-containing protein( domain architecture ID 129)

alpha-crystallin domain-containing protein similar to alpha-crystallin-type small heat shock proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alpha-crystallin-Hsps_p23-like super family cl00175
alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a ...
 25-160 2.39e-17

alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.; The alpha-crystallin-Hsps_p23-like superfamily includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12-43 kDa, whose common feature is this 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. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this superfamily is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


The actual alignment was detected with superfamily member pfam08190:

Pssm-ID: 469641  Cd Length: 166  Bit Score: 77.35  E-value: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571992  25 SDPEG---YEKFIQQQLKE--GKQLCAAPEPQLCLQTRIlKPKEKIlFINLCQWTRIPAPQSTT------------HPVP 87
Cdd:pfam08190   2 SDPENrkrYEEEIEQLEDErgGDVKFIHPEPGFVVKTFV-DGGGKC-FINVCQHELIGKPEEEPgtdgdngttglsWRIP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034571992  88 LTVGKPEDTTEISDA-YTVIDVAYNPDVLHAAEKDQVKKNQLIQMAMKCIEEKFQFTLSHS-YHITKFRIKGSIQ 160
Cdd:pfam08190  80 YSLGQPRFDKDKKGKpCKVYDVVFHPDTLHLATKNHNFRKFVIDTALEAIEQKFNVTLDRAnLKFLKMKYKGTPQ 154
 
Name Accession Description Interval E-value
PIH1 pfam08190
PIH1 N-terminal domain; This domain is involved in pre-rRNA processing. It has has been shown ...
 25-160 2.39e-17

PIH1 N-terminal domain; This domain is involved in pre-rRNA processing. It has has been shown to be required either for nucleolar retention or correct assembly of the box C/D snoRNP in Saccharomyces cerevisiae.


Pssm-ID: 369738  Cd Length: 166  Bit Score: 77.35  E-value: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571992  25 SDPEG---YEKFIQQQLKE--GKQLCAAPEPQLCLQTRIlKPKEKIlFINLCQWTRIPAPQSTT------------HPVP 87
Cdd:pfam08190   2 SDPENrkrYEEEIEQLEDErgGDVKFIHPEPGFVVKTFV-DGGGKC-FINVCQHELIGKPEEEPgtdgdngttglsWRIP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034571992  88 LTVGKPEDTTEISDA-YTVIDVAYNPDVLHAAEKDQVKKNQLIQMAMKCIEEKFQFTLSHS-YHITKFRIKGSIQ 160
Cdd:pfam08190  80 YSLGQPRFDKDKKGKpCKVYDVVFHPDTLHLATKNHNFRKFVIDTALEAIEQKFNVTLDRAnLKFLKMKYKGTPQ 154
 
Name Accession Description Interval E-value
PIH1 pfam08190
PIH1 N-terminal domain; This domain is involved in pre-rRNA processing. It has has been shown ...
 25-160 2.39e-17

PIH1 N-terminal domain; This domain is involved in pre-rRNA processing. It has has been shown to be required either for nucleolar retention or correct assembly of the box C/D snoRNP in Saccharomyces cerevisiae.


Pssm-ID: 369738  Cd Length: 166  Bit Score: 77.35  E-value: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034571992  25 SDPEG---YEKFIQQQLKE--GKQLCAAPEPQLCLQTRIlKPKEKIlFINLCQWTRIPAPQSTT------------HPVP 87
Cdd:pfam08190   2 SDPENrkrYEEEIEQLEDErgGDVKFIHPEPGFVVKTFV-DGGGKC-FINVCQHELIGKPEEEPgtdgdngttglsWRIP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034571992  88 LTVGKPEDTTEISDA-YTVIDVAYNPDVLHAAEKDQVKKNQLIQMAMKCIEEKFQFTLSHS-YHITKFRIKGSIQ 160
Cdd:pfam08190  80 YSLGQPRFDKDKKGKpCKVYDVVFHPDTLHLATKNHNFRKFVIDTALEAIEQKFNVTLDRAnLKFLKMKYKGTPQ 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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