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Conserved domains on  [gi|1046872995|ref|XP_017446439|]
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spliceosome-associated protein CWC27 homolog isoform X1 [Rattus norvegicus]

Protein Classification

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) ...
 8-177 1.78e-118

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: 343.95  E-value: 1.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|
gi 1046872995 168 FNPFDDIIPR 177
Cdd:cd01925   161 ENPFDDIVPR 170
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 376-427 8.78e-16

C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also called antigen NY-CO-10, or probable inactive peptidyl-prolyl cis-trans isomerase CWC27, or PPIase CWC27, or serologically defined colon cancer antigen 10, is part of the spliceosome and plays a role in pre-mRNA splicing. It is a probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. This model corresponds to the C-terminal domain of CWC27, which interacts with CWC22 MIF4G domain.


:

Pssm-ID: 412084 [Multi-domain]  Cd Length: 56  Bit Score: 71.18  E-value: 8.78e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046872995 376 KKGTSREDQTLALLSQFKSKLTQAITEMPEN----CAEAEVEDDEGWMSHVLQFED 427
Cdd:cd22288     1 KKGASREEQTLALLEKFKSKLHSAKESTPEEeeskAEEDEDEDDDGWMSHKLHFED 56
PTZ00121 super family cl31754
MAEBL; Provisional
 278-467 1.35e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  278 EEDEKNLMRERIAKRLKKDASANVKSAGDGEK-KPASRSEELRKEARQLKRELLAAKQKKESATKAEKGSEEEEAVPDGP 356
Cdd:PTZ00121  1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  357 VAEYRREKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQAITEMPENCAEAEVEDDEGWMSHVLQFEDKTRKVKDAS 436
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1046872995  437 MQDSDTFEIYDPRNPVNKRRREESKKLLREK 467
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-177 1.78e-118

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: 343.95  E-value: 1.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|
gi 1046872995 168 FNPFDDIIPR 177
Cdd:cd01925   161 ENPFDDIVPR 170
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 2.02e-50

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: 168.20  E-value: 2.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046872995 100 AMANAG--PHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMLRLTEvdidDEERPRNPHRIKSCEV 166
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLEKIEKVPT----DGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 3.35e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 160.34  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGEsvyGAPFKDEFH 88
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  89 SRLRfNRRGLVAMANA-GPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLTEVDIDDEERPRNPHRIKSCE 165
Cdd:COG0652    80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                  ..
gi 1046872995 166 VL 167
Cdd:COG0652   156 IV 157
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 10-164 8.37e-27

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 106.46  E-value: 8.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  10 PTNGKVLLKTT-----AGDIDIELWSKEAPKACRNFIQLCLEAY--------YDNTIFHRVVPGFIVQGGDPTGTGTGG- 75
Cdd:PLN03149   16 PKNPVVFFDVTiggipAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGc 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  76 ESVYGAPFKDE-FHSRlrFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEER 154
Cdd:PLN03149   96 VSIYGSKFEDEnFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNR 173

                         170
                  ....*....|
gi 1046872995 155 PRNPHRIKSC 164
Cdd:PLN03149  174 PKLACVISEC 183
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 376-427 8.78e-16

C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also called antigen NY-CO-10, or probable inactive peptidyl-prolyl cis-trans isomerase CWC27, or PPIase CWC27, or serologically defined colon cancer antigen 10, is part of the spliceosome and plays a role in pre-mRNA splicing. It is a probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. This model corresponds to the C-terminal domain of CWC27, which interacts with CWC22 MIF4G domain.


Pssm-ID: 412084 [Multi-domain]  Cd Length: 56  Bit Score: 71.18  E-value: 8.78e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046872995 376 KKGTSREDQTLALLSQFKSKLTQAITEMPEN----CAEAEVEDDEGWMSHVLQFED 427
Cdd:cd22288     1 KKGASREEQTLALLEKFKSKLHSAKESTPEEeeskAEEDEDEDDDGWMSHKLHFED 56
PTZ00121 PTZ00121
MAEBL; Provisional
 278-467 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  278 EEDEKNLMRERIAKRLKKDASANVKSAGDGEK-KPASRSEELRKEARQLKRELLAAKQKKESATKAEKGSEEEEAVPDGP 356
Cdd:PTZ00121  1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  357 VAEYRREKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQAITEMPENCAEAEVEDDEGWMSHVLQFEDKTRKVKDAS 436
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1046872995  437 MQDSDTFEIYDPRNPVNKRRREESKKLLREK 467
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-177 1.78e-118

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: 343.95  E-value: 1.78e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEF 87
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVL 167
Cdd:cd01925    81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                         170
                  ....*....|
gi 1046872995 168 FNPFDDIIPR 177
Cdd:cd01925   161 ENPFDDIVPR 170
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-171 1.53e-50

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: 169.13  E-value: 1.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEFHSRLRFN 94
Cdd:cd01923     2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046872995  95 RRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlTEVDIDDEERPRNPHRIKSCEVLFNPF 171
Cdd:cd01923    82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGglETLEAM---ENVPDPGTDRPKEEIKIEDTSVFVDPF 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 2.02e-50

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: 168.20  E-value: 2.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046872995 100 AMANAG--PHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMLRLTEvdidDEERPRNPHRIKSCEV 166
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLEKIEKVPT----DGDRPVKPVKILSCGV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-163 3.35e-50

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: 167.83  E-value: 3.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGeSVYGAPFKDEFHSRLRFNRR 96
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046872995  97 GLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMLRlteVDIDDEERPRNPHRIKS 163
Cdd:cd00317    81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEgmDVVDKIER---GDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 3.35e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 160.34  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGEsvyGAPFKDEFH 88
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  89 SRLRfNRRGLVAMANA-GPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLTEVDIDDEERPRNPHRIKSCE 165
Cdd:COG0652    80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                  ..
gi 1046872995 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 5.77e-47

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: 159.52  E-value: 5.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEFHSRLRFN 94
Cdd:cd01928     3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046872995  95 RRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVT-GDTVYNMLRLTEVDIDDeeRPRNPHRIK 162
Cdd:cd01928    83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIdGFETLDTLEKLPVDKKY--RPLEEIRIK 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 16-161 1.37e-44

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: 153.00  E-value: 1.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEFHSRLRFNR 95
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046872995  96 RGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLTEVDIDDEERPRNPHRI 161
Cdd:cd01927    81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVV---QRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-161 4.38e-43

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: 149.22  E-value: 4.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYGAPFKDEFHSRLRFNR 95
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046872995  96 RGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVyNMLRLTEVDiDDEERPRNPHRI 161
Cdd:cd01922    81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMK-VIENMVEVQ-TQTDRPIDEVKI 144
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 16-174 4.38e-40

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: 141.71  E-value: 4.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESVYG-------APFKDEFH 88
Cdd:cd01921     1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  89 SRLRFNRRGLVAMANAGPHDNGSQFFFTLGRA-DELNNKHTIFGKVTgDTVYNMLRLTEVDIDDEERPRNPHRIKSCEVL 167
Cdd:cd01921    81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIKHTHIL 159


                  ....*..
gi 1046872995 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 ...
 21-164 7.57e-28

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: 108.50  E-value: 7.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  21 AGDIDIELWSKEAPKACRNFIQLC--------LEAYYDNTIFHRVVPGFIVQGGD-PTGTGTGGESVYGAPFKDE-FHsr 90
Cdd:cd01926    14 AGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDfTRGNGTGGKSIYGEKFPDEnFK-- 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046872995  91 LRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVT-GdtvYNMLRLTEVDIDDEERPRNPHRIKSC 164
Cdd:cd01926    92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVeG---MDVVKKIENVGSGNGKPKKKVVIADC 163
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 10-164 8.37e-27

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 106.46  E-value: 8.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  10 PTNGKVLLKTT-----AGDIDIELWSKEAPKACRNFIQLCLEAY--------YDNTIFHRVVPGFIVQGGDPTGTGTGG- 75
Cdd:PLN03149   16 PKNPVVFFDVTiggipAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGc 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  76 ESVYGAPFKDE-FHSRlrFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLTEVDIDDEER 154
Cdd:PLN03149   96 VSIYGSKFEDEnFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNR 173

                         170
                  ....*....|
gi 1046872995 155 PRNPHRIKSC 164
Cdd:PLN03149  174 PKLACVISEC 183
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 1.82e-26

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 105.31  E-value: 1.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGD-PTGTGTGGESVYGAPFKDEfHSR 90
Cdd:PTZ00060   29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDE-NFK 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046872995  91 LRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLTEVDIDDEERPRNPHRIKSC 164
Cdd:PTZ00060  108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-135 2.83e-23

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: 95.59  E-value: 2.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESvyGAPFKDEFHSRLRfNR 95
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLS-NT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046872995  96 RGLVAMA-NAGPHDNGSQFFFTLGRADELNNK-----HTIFGKVTG 135
Cdd:cd01920    78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTE 123
PRK10903 PRK10903
peptidylprolyl isomerase A;
15-167 3.09e-21

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 91.06  E-value: 3.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESvyGAPFKDEFHSRLRfN 94
Cdd:PRK10903   31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLR-N 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  95 RRGLVAMANAGPHDNG-SQFFFTLGRADELNNKHTIFG-KVTGDTVYNML---RLTEVDIDD----EERPRNPHRIKSCE 165
Cdd:PRK10903  108 TRGTIAMARTADKDSAtSQFFINVADNAFLDHGQRDFGyAVFGKVVKGMDvadKISQVPTHDvgpyQNVPSKPVVILSAK 187


                  ..
gi 1046872995 166 VL 167
Cdd:PRK10903  188 VL 189
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 376-427 8.78e-16

C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also called antigen NY-CO-10, or probable inactive peptidyl-prolyl cis-trans isomerase CWC27, or PPIase CWC27, or serologically defined colon cancer antigen 10, is part of the spliceosome and plays a role in pre-mRNA splicing. It is a probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. This model corresponds to the C-terminal domain of CWC27, which interacts with CWC22 MIF4G domain.


Pssm-ID: 412084 [Multi-domain]  Cd Length: 56  Bit Score: 71.18  E-value: 8.78e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046872995 376 KKGTSREDQTLALLSQFKSKLTQAITEMPEN----CAEAEVEDDEGWMSHVLQFED 427
Cdd:cd22288     1 KKGASREEQTLALLEKFKSKLHSAKESTPEEeeskAEEDEDEDDDGWMSHKLHFED 56
PRK10791 PRK10791
peptidylprolyl isomerase B;
15-124 9.00e-16

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 74.88  E-value: 9.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGTGGESvyGAPFKDEFHSRLRfN 94
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKAT--KEPIKNEANNGLK-N 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1046872995  95 RRGLVAMANAG-PHDNGSQFFFTLGRADELN 124
Cdd:PRK10791   79 TRGTLAMARTQaPHSATAQFFINVVDNDFLN 109
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 17-134 5.75e-09

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: 55.53  E-value: 5.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGT---------------------GG 75
Cdd:cd01924     2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPgfpdpetgksrtipleikpegQK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046872995  76 ESVYGAP------FKDEFhsRLRFNRRGLVAMANAGPHDNG--SQFFFTLG-------RADELNNKHTIFGKVT 134
Cdd:cd01924    82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVT 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 77-170 5.86e-08

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 53.72  E-value: 5.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  77 SVYGAPFKDEFHsRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTgDTVYNMLRLTEVDIDDEERPR 156
Cdd:PTZ00221  131 SSTGTPIADEGY-RHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDVGRPL 208

                          90
                  ....*....|....
gi 1046872995 157 NPHRIKSCEVLFNP 170
Cdd:PTZ00221  209 LPVTVSFCGALTGE 222
PTZ00121 PTZ00121
MAEBL; Provisional
 278-467 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  278 EEDEKNLMRERIAKRLKKDASANVKSAGDGEK-KPASRSEELRKEARQLKRELLAAKQKKESATKAEKGSEEEEAVPDGP 356
Cdd:PTZ00121  1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  357 VAEYRREKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQAITEMPENCAEAEVEDDEGWMSHVLQFEDKTRKVKDAS 436
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1046872995  437 MQDSDTFEIYDPRNPVNKRRREESKKLLREK 467
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
PTZ00121 PTZ00121
MAEBL; Provisional
 243-470 1.87e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  243 SSVPAVESEKDDATGDLEDLSQDAEDDSVEHDGSMEEDEKNLMRERIAKRLKKDASANVKSAGDGEKKP---ASRSEELR 319
Cdd:PTZ00121  1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAK 1349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  320 KEARQLKRELLAAKQKKESAtkaEKGSEEeeavpdgpvaeyrrEKQKYEALRKQQPKKGTSREDQTLALLSQFKSKLTQA 399
Cdd:PTZ00121  1350 AEAEAAADEAEAAEEKAEAA---EKKKEE--------------AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046872995  400 ITEMPENCAEAEVEDDEgwmshVLQFEDKTRKVKDASMQDSDTFEIYDPRNPVNKRRREESKKLLREKKER 470
Cdd:PTZ00121  1413 AAAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 309-396 8.74e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.78  E-value: 8.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046872995  309 KKPASRSEELRKEARQLKRELLAAKQKKESATKAEKGSEEEEAVPDGPVAEYRREK----QKYEALRKQQPKKGTSREDQ 384
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQqeleAQLEQLQEKAAETSQERKQK 217

                           90
                   ....*....|..
gi 1046872995  385 TLALLSQFKSKL 396
Cdd:PRK11448   218 RKEITDQAAKRL 229
 
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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