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Conserved domains on  [gi|1406928173|ref|NP_001351407|]
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spliceosome-associated protein CWC27 homolog isoform 5 [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112476)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413
PubMed:  14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 2.68e-134

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


:

Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 379.77  E-value: 2.68e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|.
gi 1406928173 168 FNPFDDIIPRE 178
Cdd:cd01925   161 ENPFDDIVPRI 171
NOP7 super family cl34924
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 239-348 3.30e-03

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5163:

Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 39.29  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173 239 DPHLSSVPVVESEKGDAPDLVDDGEDESAEHD--EYIDGDEKNLMRERI----AKKLK-KDTSANVKSAGEgeveKKSVS 311
Cdd:COG5163   457 DPRASLMTMEETQRHSEEDLVNRFEDVRYEHVagEEDDDDDEELQAQKEleleAQGIKySETSEADKDVNK----SKNKK 532

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1406928173 312 RSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSED 348
Cdd:COG5163   533 RKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEE 569
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 2.68e-134

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 379.77  E-value: 2.68e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|.
gi 1406928173 168 FNPFDDIIPRE 178
Cdd:cd01925   161 ENPFDDIVPRI 171
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 1.36e-60

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 191.31  E-value: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1406928173 100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 3.31e-60

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.77  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652    80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                  ..
gi 1406928173 166 VL 167
Cdd:COG0652   156 IV 157
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 1.22e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 125.34  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060   29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1406928173  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060  108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 239-348 3.30e-03

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 39.29  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173 239 DPHLSSVPVVESEKGDAPDLVDDGEDESAEHD--EYIDGDEKNLMRERI----AKKLK-KDTSANVKSAGEgeveKKSVS 311
Cdd:COG5163   457 DPRASLMTMEETQRHSEEDLVNRFEDVRYEHVagEEDDDDDEELQAQKEleleAQGIKySETSEADKDVNK----SKNKK 532

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1406928173 312 RSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSED 348
Cdd:COG5163   533 RKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEE 569
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 281-345 7.09e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 37.93  E-value: 7.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1406928173 281 MRERIAKKLKKDTSanvksagEGEVEKKSVSRSEELRKEARQLKRELLAAKQKKVEnaAKQAEKR 345
Cdd:pfam07946 265 TREEEIEKIKKAAE-------EERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYE--EKERKKE 320
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 2.68e-134

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 379.77  E-value: 2.68e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|.
gi 1406928173 168 FNPFDDIIPRE 178
Cdd:cd01925   161 ENPFDDIVPRI 171
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-171 3.38e-64

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 201.10  E-value: 3.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01923     2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1406928173  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKSCEVLFNPF 171
Cdd:cd01923    82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGglETLEAM---ENVPDPGTDRPKEEIKIEDTSVFVDPF 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-163 8.97e-61

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.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 191.71  E-value: 8.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGeSIYGAPFKDEFHSRLRFNRR 96
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1406928173  97 GLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKS 163
Cdd:cd00317    81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEgmDVVDKI---ERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 1.36e-60

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 191.31  E-value: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1406928173 100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 3.31e-60

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.77  E-value: 3.31e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652    80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                  ..
gi 1406928173 166 VL 167
Cdd:COG0652   156 IV 157
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 15-162 3.03e-58

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 185.72  E-value: 3.03e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01928     3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1406928173  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT-GDTVYNMLRLSEVDIDDdeRPHNPHKIK 162
Cdd:cd01928    83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIdGFETLDTLEKLPVDKKY--RPLEEIRIK 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 16-161 6.61e-57

cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known.


Pssm-ID: 238908 [Multi-domain]  Cd Length: 148  Bit Score: 181.89  E-value: 6.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1406928173  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKI 161
Cdd:cd01927    81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVV---QRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-155 1.81e-56

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 180.81  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVyNMLRLSEVDIDDDeRP 155
Cdd:cd01922    81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMK-VIENMVEVQTQTD-RP 138
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 16-174 5.13e-49

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 162.13  E-value: 5.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYG-------APFKDEFH 88
Cdd:cd01921     1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  89 SRLRFNRRGLVAMANAGSHDNGSQFFFTLGRA-DELNNKHTIFGKVTgDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01921    81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIKHTHIL 159


                  ....*..
gi 1406928173 168 FNPFDDI 174
Cdd:cd01921   160 DDPFPDP 166
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 21-134 1.67e-37

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.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 132.38  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  21 AGDIDIELWSKEAPKACRNFIQLC--------LEAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDE-FHsr 90
Cdd:cd01926    14 AGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDEnFK-- 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1406928173  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT 134
Cdd:cd01926    92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV 135
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 1.22e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 125.34  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060   29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1406928173  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060  108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 10-164 4.43e-34

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 124.18  E-value: 4.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  10 PTNGKVLLKTT-----AGDIDIELWSKEAPKACRNFIQLCLEAY--------YDNTIFHRVVPGFIVQGGD-PTGTGSGG 75
Cdd:PLN03149   16 PKNPVVFFDVTiggipAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  76 ESIYGAPFKDE-FHSRlrFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDER 154
Cdd:PLN03149   96 VSIYGSKFEDEnFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNR 173

                         170
                  ....*....|
gi 1406928173 155 PHNPHKIKSC 164
Cdd:PLN03149  174 PKLACVISEC 183
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-135 3.80e-25

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 99.44  E-value: 3.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESiyGAPFKDEFHSRLRfNR 95
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLS-NT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1406928173  96 RGLVAMA-NAGSHDNGSQFFFTLGRADELNNK-----HTIFGKVTG 135
Cdd:cd01920    78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTE 123
PRK10903 PRK10903
peptidylprolyl isomerase A;
15-167 1.07e-24

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 99.15  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSggESIYGAPFKDEFHSRLRfN 94
Cdd:PRK10903   31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQ--QKKPNPPIKNEADNGLR-N 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  95 RRGLVAMANAGSHDNG-SQFFFTLGRADELNNKHTIFG-KVTGDTVYNML---RLSEVDIDD----DERPHNPHKIKSCE 165
Cdd:PRK10903  108 TRGTIAMARTADKDSAtSQFFINVADNAFLDHGQRDFGyAVFGKVVKGMDvadKISQVPTHDvgpyQNVPSKPVVILSAK 187


                  ..
gi 1406928173 166 VL 167
Cdd:PRK10903  188 VL 189
PRK10791 PRK10791
peptidylprolyl isomerase B;
15-124 3.41e-16

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 75.26  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGdptGTGSG-GESIYGAPFKDEFHSRLRf 93
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGmKQKATKEPIKNEANNGLK- 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1406928173  94 NRRGLVAMANAGS-HDNGSQFFFTLGRADELN 124
Cdd:PRK10791   78 NTRGTLAMARTQApHSATAQFFINVVDNDFLN 109
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 17-134 5.53e-15

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 72.09  E-value: 5.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSG---------------------G 75
Cdd:cd01924     2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1406928173  76 ESIYGAP------FKDEFhsRLRFNRRGLVAMANAGSHDNG--SQFFFTLG-------RADELNNKHTIFGKVT 134
Cdd:cd01924    82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVT 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 73-170 2.23e-07

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 51.41  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173  73 SGGESIYGAPFKDEFHsRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTgDTVYNMLRLSEVDIDDD 152
Cdd:PTZ00221  127 SFNVSSTGTPIADEGY-RHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDV 204

                          90
                  ....*....|....*...
gi 1406928173 153 ERPHNPHKIKSCEVLFNP 170
Cdd:PTZ00221  205 GRPLLPVTVSFCGALTGE 222
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 239-348 3.30e-03

Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 39.29  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406928173 239 DPHLSSVPVVESEKGDAPDLVDDGEDESAEHD--EYIDGDEKNLMRERI----AKKLK-KDTSANVKSAGEgeveKKSVS 311
Cdd:COG5163   457 DPRASLMTMEETQRHSEEDLVNRFEDVRYEHVagEEDDDDDEELQAQKEleleAQGIKySETSEADKDVNK----SKNKK 532

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1406928173 312 RSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSED 348
Cdd:COG5163   533 RKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEE 569
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 281-345 7.09e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 37.93  E-value: 7.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1406928173 281 MRERIAKKLKKDTSanvksagEGEVEKKSVSRSEELRKEARQLKRELLAAKQKKVEnaAKQAEKR 345
Cdd:pfam07946 265 TREEEIEKIKKAAE-------EERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYE--EKERKKE 320
 
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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