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Conserved domains on  [gi|162312530|ref|NP_594502|]
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cyclophilin family peptidyl-prolyl cis-trans isomerase Cyp8 [Schizosaccharomyces pombe]

Protein Classification

PPIL2 family peptidylprolyl isomerase( domain architecture ID 11616204)

PPIL2 family cyclophilin-type peptidylprolyl isomerase containing a Ubox domain, may act as an E3 ubiquitin protein ligase and may catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins; similar to peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2)

CATH:  3.30.40.10|2.40.100.10
EC:  2.3.2.27|5.2.1.8
Gene Ontology:  GO:0004842|GO:0016567|GO:0006457|GO:0003755
PubMed:  15189447|12627222|10704423|11435423|14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 277-433 4.01e-106

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: 313.58  E-value: 4.01e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 277 YARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKH 356
Cdd:cd01923    1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530 357 DDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIIIFVDPF 433
Cdd:cd01923   81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVFVDPF 157
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 41-117 2.38e-37

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


:

Pssm-ID: 438325  Cd Length: 73  Bit Score: 131.92  E-value: 2.38e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530  41 PFNYCSLSLQPFNHPCClvdeTKQAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEYCDPVTMKSF 117
Cdd:cd16663    1 PFDCCALSLQPFENPVC----TPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLNFHKNAEGEYHCPVTFKVF 73
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 108-166 6.33e-06

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16662:

Pssm-ID: 473075  Cd Length: 68  Bit Score: 43.82  E-value: 6.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312530 108 YCDPVTMKSFTRFSHIVAIRSTGNCFSWDTIERLnIKPKhWRDLVNEEQFTRDDIITIQ 166
Cdd:cd16662    2 YMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKL-IKKD-MIDPVTGKKLKEKDIIPLQ 58
 
Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 277-433 4.01e-106

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: 313.58  E-value: 4.01e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 277 YARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKH 356
Cdd:cd01923    1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530 357 DDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIIIFVDPF 433
Cdd:cd01923   81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVFVDPF 157
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 277-428 1.79e-69

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 219.27  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 277 YARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQsiwGKPFKDEFCNPLKH 356
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKH 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312530 357 dDRGIISMAN-RGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIII 428
Cdd:COG0652   85 -KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 280-426 3.17e-58

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: 189.77  E-value: 3.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530  280 IVTN-HGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIwgKPFKDEFCNPLKHDD 358
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530  359 RGIISMANRG--KNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTnSNDHPKLPIKLEDI 426
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT-DGDRPVKPVKILSC 147
PTZ00060 PTZ00060
cyclophilin; Provisional
 283-425 1.76e-38

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 138.82  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 283 NHGEINIELHTDYAPHAVYNFVQL---------AKQGYYRNTIFHRNIARFMIQGGD-PSGTGRGGQSIWGKPFKDEFCN 352
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312530 353 pLKHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNdHPKLPIKLED 425
Cdd:PTZ00060 108 -LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPKKPVVVTD 178
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 41-117 2.38e-37

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 438325  Cd Length: 73  Bit Score: 131.92  E-value: 2.38e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530  41 PFNYCSLSLQPFNHPCClvdeTKQAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEYCDPVTMKSF 117
Cdd:cd16663    1 PFDCCALSLQPFENPVC----TPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLNFHKNAEGEYHCPVTFKVF 73
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 45-108 3.66e-12

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 61.48  E-value: 3.66e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312530    45 CSLSLQPFNHPCCLVDetkqAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEY 108
Cdd:smart00504   4 CPISLEVMKDPVILPS----GQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
 108-166 6.33e-06

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain.


Pssm-ID: 438324  Cd Length: 68  Bit Score: 43.82  E-value: 6.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312530 108 YCDPVTMKSFTRFSHIVAIRSTGNCFSWDTIERLnIKPKhWRDLVNEEQFTRDDIITIQ 166
Cdd:cd16662    2 YMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKL-IKKD-MIDPVTGKKLKEKDIIPLQ 58
 
Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 277-433 4.01e-106

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: 313.58  E-value: 4.01e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 277 YARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKH 356
Cdd:cd01923    1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530 357 DDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIIIFVDPF 433
Cdd:cd01923   81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVFVDPF 157
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 277-428 1.79e-69

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 219.27  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 277 YARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQsiwGKPFKDEFCNPLKH 356
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKH 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312530 357 dDRGIISMAN-RGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIII 428
Cdd:COG0652   85 -KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 279-428 1.39e-67

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: 214.22  E-value: 1.39e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 279 RIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKHDD 358
Cdd:cd01928    4 TLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHDS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 359 RGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIII 428
Cdd:cd01928   84 RGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKDVTI 153
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 280-425 2.50e-64

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: 205.58  E-value: 2.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGqSIWGKPFKDEFCNPLKHDDR 359
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312530 360 GIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLED 425
Cdd:cd00317   81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 280-426 3.17e-60

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: 194.99  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKHDDR 359
Cdd:cd01927    2 IHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDRP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530 360 GIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDI 426
Cdd:cd01927   82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 280-426 3.17e-58

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: 189.77  E-value: 3.17e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530  280 IVTN-HGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIwgKPFKDEFCNPLKHDD 358
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530  359 RGIISMANRG--KNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTnSNDHPKLPIKLEDI 426
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT-DGDRPVKPVKILSC 147
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 275-433 2.00e-57

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: 188.71  E-value: 2.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 275 KGYARIVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPL 354
Cdd:cd01925    5 TGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 355 KHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGG--LNVLdALEKVPTNSNDHPKLPIKLEDIIIFVDP 432
Cdd:cd01925   85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDtiYNLL-KLAEVETDKDERPVYPPKITSVEVLENP 163


                 .
gi 162312530 433 F 433
Cdd:cd01925  164 F 164
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 280-423 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: 185.05  E-value: 1.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRGGQSIWGKPFKDEFCNPLKHDDR 359
Cdd:cd01922    2 LETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTGA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312530 360 GIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNsNDHPKLPIKL 423
Cdd:cd01922   82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKI 144
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 285-425 3.78e-45

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: 155.88  E-value: 3.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 285 GEINIELHTDYAPHAVYNFVQLA--------KQGYYRNTIFHRNIARFMIQGGD-PSGTGRGGQSIWGKPFKDE-FcnPL 354
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDfTRGNGTGGKSIYGEKFPDEnF--KL 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312530 355 KHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTnSNDHPKLPIKLED 425
Cdd:cd01926   93 KHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKKVVIAD 162
PTZ00060 PTZ00060
cyclophilin; Provisional
 283-425 1.76e-38

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 138.82  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 283 NHGEINIELHTDYAPHAVYNFVQL---------AKQGYYRNTIFHRNIARFMIQGGD-PSGTGRGGQSIWGKPFKDEFCN 352
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162312530 353 pLKHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNdHPKLPIKLED 425
Cdd:PTZ00060 108 -LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPKKPVVVTD 178
RING-Ubox_PPIL2 cd16663
U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 ...
 41-117 2.38e-37

U-box domain, a modified RING finger, found in peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and similar proteins; PPIL2 (EC 5.2.1.8), also known as PPIase, CYC4, cyclophilin-60 (Cyp60), cyclophilin-like protein Cyp-60, or Rotamase PPIL2, is a nuclear-specific cyclophilin which interacts with the proteinase inhibitor eglin c and regulates gene expression. PPIL2 belongs to the cyclophilin family of peptidylprolyl isomerases and catalyzes cis-trans isomerization of proline-peptide bonds, which is often a rate-limiting step in protein folding. It positively regulates beta-site amyloid precursor protein cleaving enzyme (BACE1) expression and beta-secretase activity. Moreover, PPIL2 plays an important role in the translocation of CD147 to the cell surface, and thus may present a novel target for therapeutic interventions in diseases where CD147 functions as a pathogenic factor in cancer, human immunodeficiency virus infection, or rheumatoid arthritis. PPIL2 contains an N-terminal RING-like U-box domain and a C-terminal cyclophilin (Cyp)-like chaperone domain.


Pssm-ID: 438325  Cd Length: 73  Bit Score: 131.92  E-value: 2.38e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312530  41 PFNYCSLSLQPFNHPCClvdeTKQAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEYCDPVTMKSF 117
Cdd:cd16663    1 PFDCCALSLQPFENPVC----TPDGIVFDLLNIVPYLKKYGKNPVTGEPLEAKDLIKLNFHKNAEGEYHCPVTFKVF 73
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 280-433 4.31e-37

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: 134.39  E-value: 4.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHrNIAR-FMIQGGDPSGTGRGGQSIWGKP-------FKDEFC 351
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFY-NVQKdFIAQTGDPTGTGAGGESIYSQLygrqarfFEPEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 352 NPLKHDDRGIISMANRGKNTNGSQFFILYGPA-KHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPIKLEDIIIFV 430
Cdd:cd01921   81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRIKHTHILD 160


                 ...
gi 162312530 431 DPF 433
Cdd:cd01921  161 DPF 163
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 285-423 4.61e-35

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 129.57  E-value: 4.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 285 GEINIELHTDYAPHAVYNFVQLA-----KQGY---YRNTIFHRNIARFMIQGGD-PSGTGRGGQSIWGKPFKDE-FCNpl 354
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDEnFIA-- 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 355 KHDDRGIISMANRGKNTNGSQFFILYGPAKHLDNKHTIFGRVVG-GLNVLDALEKVPTNSNDHPKLPIKL 423
Cdd:PLN03149 111 KHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGdGLLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 282-428 3.11e-29

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: 112.54  E-value: 3.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 282 TNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGdpsG-TGRGGQSIWGKPFKDEFCNPLKhDDRG 360
Cdd:cd01920    4 TSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGG---GfTPDLAQKETLKPIKNEAGNGLS-NTRG 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312530 361 IISMANRGKNTNG-SQFFILYGPAKHLDNK-----HTIFGRVVGGLNVLDALEKVPT-NSNDHPKLPikLEDIII 428
Cdd:cd01920   80 TIAMARTNAPDSAtSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETySFGSYQDVP--VQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
280-422 4.46e-23

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 96.45  E-value: 4.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGdpSGTGRGGQSIWGKPFKDEFCNPLKhDDR 359
Cdd:PRK10903  33 LTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGG--GFTEQMQQKKPNPPIKNEADNGLR-NTR 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 360 GIISMANRG-KNTNGSQFFILYGPAKHLDN-----KHTIFGRVVGGLNVLDALEKVPT-NSNDHPKLPIK 422
Cdd:PRK10903 110 GTIAMARTAdKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPThDVGPYQNVPSK 179
PRK10791 PRK10791
peptidylprolyl isomerase B;
282-428 8.49e-17

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 77.96  E-value: 8.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 282 TNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGG--DPSGTGRGGQSiwgkPFKDEFCNPLKhDDR 359
Cdd:PRK10791   6 TNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEPGMKQKATKE----PIKNEANNGLK-NTR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162312530 360 GIISMA-NRGKNTNGSQFFILYGPAKHLDNK--------HTIFGRVVGGLNVLDALEKVPTN-SNDHPKLPIklEDIII 428
Cdd:PRK10791  81 GTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGrSGMHQDVPK--EDVII 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 280-407 1.03e-14

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: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 280 IVTNHGEINIELHTDYAPHAVYNFVQLAKQGYYRNTIFHRNIARFMIQGGDPSGTGRG---------------------G 338
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 339 QSIWGKP------FKDEFcnPLKHDDRGIISMANRGKNTNG--SQFFILYG-------PAKHLDNKHTIFGRVVGGLNVL 403
Cdd:cd01924   82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVTDGLDIL 159


                 ....
gi 162312530 404 DALE 407
Cdd:cd01924  160 RELK 163
PTZ00221 PTZ00221
cyclophilin; Provisional
 228-421 1.84e-14

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 73.36  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 228 MPIHRASHTTGYAAASLTSTSFTPVTKN--ERAIIAEEDYMLNHTRIKHKGYARIVTN-------HGEINIELHTDYAPH 298
Cdd:PTZ00221   1 MPFRKLKPRRDAPQALPDPPSREQVYNDieERRLKEWENYQKSHRMKEEQNSCRAFLDisigdvlAGRLVFELFEDVVPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312530 299 AVYNFVQL------------AKQGYYRNTIFHRNIARFMIQGGDPSGTGrggQSIWGKPFKDEFCNpLKHDDRGIISMAN 366
Cdd:PTZ00221  81 TVENFRALitgscgidtntgVKLDYLYTPVHHVDRNNNIIVLGELDSFN---VSSTGTPIADEGYR-HRHTERGLLTMIS 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312530 367 RGKNTNGSQFFILYGPAKHLDNKHTIFGRVVGGLNVLDALEKVPTNSNDHPKLPI 421
Cdd:PTZ00221 157 EGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPV 211
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 45-108 3.66e-12

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 61.48  E-value: 3.66e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312530    45 CSLSLQPFNHPCCLVDetkqAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLKFAKNSAEEY 108
Cdd:smart00504   4 CPISLEVMKDPVILPS----GQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox2_NOSIP cd16662
U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein ...
 108-166 6.33e-06

U-box domain 2, a modified RING finger, found in nitric oxide synthase-interacting protein (NOSIP) and similar proteins; NOSIP, also known as endothelial NO synthase (eNOS)-interacting protein, p33RUL, is an E3 ubiquitin-protein ligase implicated in the control of airway and vascular diameter, mucosal secretion, NO synthesis in ciliated epithelium, and, therefore, of mucociliary and bronchial function. The loss of NOSIP may cause holoprosencephaly and facial anomalies including cleft lip/palate, cyclopia and facial midline clefting. NOSIP interacts with neuronal nitric oxide synthase (nNOS) and eNOS by inhibiting nitric oxide (NO) production. It acts as a novel type of modulator that promotes translocation of eNOS from the plasma membrane to intracellular sites, thereby uncoupling eNOS from plasma membrane caveolae and inhibiting NO synthesis. NOSIP also interacts with protein phosphatase PP2A and mediates the monoubiquitination of the PP2A catalytic subunit. Thus, it is a critical modulator of brain and craniofacial development in mice and a candidate gene for holoprosencephaly in humans. Moreover, NOSIP associates with the erythropoietin (Epo) receptor (EpoR), mediates ubiquitination of EpoR, and plays an essential role in erythropoietin-induced proliferation. NOSIP contains an atypical N-terminal RING-like U-box domain that is split into two parts by an interjacent stretch of 104 amino acid residues, as well as a C-terminal RING-like U-box domain. This model corresponds to the second U-box domain.


Pssm-ID: 438324  Cd Length: 68  Bit Score: 43.82  E-value: 6.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312530 108 YCDPVTMKSFTRFSHIVAIRSTGNCFSWDTIERLnIKPKhWRDLVNEEQFTRDDIITIQ 166
Cdd:cd16662    2 YMCAVTKDVLTNSVPCAVLRPSGDVVTMECVEKL-IKKD-MIDPVTGKKLKEKDIIPLQ 58
RING-Ubox_PRP19 cd16656
U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and ...
 45-99 2.33e-05

U-box domain, a modified RING finger, found in pre-mRNA-processing factor 19 (Prp19) and similar proteins; Prp19, also known as nuclear matrix protein 200 (NMP200), senescence evasion factor (SNEV), or DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signaling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex. Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerization and is essential for its auto-ubiquitination activity in vitro or when overexpressed, a coiled-coil Prp19 homology region that mediates its tetramerization and interaction with CDC5L and SPF27, and a C-terminal seven-bladed WD40 beta-propeller type of leucine-rich architectural repeats that form an asymmetrical barrel-shaped structure important for substrate recognition and recruitment.


Pssm-ID: 438318  Cd Length: 54  Bit Score: 41.78  E-value: 2.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312530  45 CSLSLQPFNHPcclVDETKQAIIFDFRFIVPWLRKHGTNPINGQKASMSDLIKLK 99
Cdd:cd16656    3 CAISGEVPEEP---VVSPKSGHVFEKRLIEKYIAENGTDPVTGEPLTEEDLIEIK 54
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 45-89 5.61e-05

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 40.62  E-value: 5.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 162312530  45 CSLSLQPFNHPCClvdeTKQAIIFDFRFIVPWLRKHGTNPINGQK 89
Cdd:cd16453    3 CPISGELMKDPVI----TPSGITYDRSAIERWLLSDNTDPFTREP 43
 
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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