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Conserved domains on  [gi|688573424|ref|XP_009303436|]
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spliceosome-associated protein CWC27 homolog isoform X1 [Danio rerio]

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) ...
 8-178 4.50e-119

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: 345.49  E-value: 4.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   8 EPPTNGKVLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLADVACDGDERPLNPHKIRSTEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 688573424 168 HSPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 370-425 1.34e-18

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: 79.27  E-value: 1.34e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688573424 370 KKGSGREAQTLALLESFKSKLSSAISETPSAPEEDVEELAEDDDKGWMAHVLHFDE 425
Cdd:cd22288    1 KKGASREEQTLALLEKFKSKLHSAKESTPEEEESKAEEDEDEDDDGWMSHKLHFED 56
PTZ00121 super family cl31754
MAEBL; Provisional
 272-467 3.65e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLKKDKTDEEKSSQDLVK----KTS----RSDELRKEARQLKKELLAIKQRKEDGVKKEEDVSEGD 343
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEeakkKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  344 SKQNSEAVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKSKLSSAISETPSApeEDVEELAEDDDKGWMAHVlHF 423
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA--DEAKKKAEEAKKADEAKK-KA 1492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 688573424  424 DEQSRKVKDANMQDEDTFEIYDPRNPVNKRRREESKKLLKDKKA 467
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 4.50e-119

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: 345.49  E-value: 4.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   8 EPPTNGKVLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLADVACDGDERPLNPHKIRSTEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 688573424 168 HSPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 7.37e-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: 167.05  E-value: 7.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   20 SAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYgrPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688573424  100 AMANAG--PHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLADVACDGDeRPLNPHKIRSTEV 166
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 7.64e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 7.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   9 PPTNGKVLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGEsiyGRPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  89 SRLRfNRRGLVAMANA-GPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLADVACDGDERPLNPHKIRSTE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 688573424 166 VL 167
Cdd:COG0652  156 IV 157
PTZ00060 PTZ00060
cyclophilin; Provisional
 20-133 8.60e-28

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 109.16  E-value: 8.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  20 SAGDIDIELWSKETPKACRNFVQLCM------EG---YYDGTIFHRMVPEFIVQGGD-PTGTGTGGESIYGRPFKDEfHS 89
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCIgdkvgsSGknlHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDE-NF 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 688573424  90 RLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKV 133
Cdd:PTZ00060 107 KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKV 150
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 370-425 1.34e-18

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: 79.27  E-value: 1.34e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688573424 370 KKGSGREAQTLALLESFKSKLSSAISETPSAPEEDVEELAEDDDKGWMAHVLHFDE 425
Cdd:cd22288    1 KKGASREEQTLALLEKFKSKLHSAKESTPEEEESKAEEDEDEDDDGWMSHKLHFED 56
PTZ00121 PTZ00121
MAEBL; Provisional
 272-467 3.65e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLKKDKTDEEKSSQDLVK----KTS----RSDELRKEARQLKKELLAIKQRKEDGVKKEEDVSEGD 343
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEeakkKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  344 SKQNSEAVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKSKLSSAISETPSApeEDVEELAEDDDKGWMAHVlHF 423
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA--DEAKKKAEEAKKADEAKK-KA 1492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 688573424  424 DEQSRKVKDANMQDEDTFEIYDPRNPVNKRRREESKKLLKDKKA 467
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 4.50e-119

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: 345.49  E-value: 4.50e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   8 EPPTNGKVLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  88 HSRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLADVACDGDERPLNPHKIRSTEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 688573424 168 HSPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-171 2.99e-52

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: 173.37  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  15 VLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEFHSRLRFN 94
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688573424  95 RRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlADVACDGDERPLNPHKIRSTEVLHSPF 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 7.37e-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: 167.05  E-value: 7.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   20 SAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYgrPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688573424  100 AMANAG--PHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLADVACDGDeRPLNPHKIRSTEV 166
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-163 3.23e-49

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: 165.13  E-value: 3.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  17 LKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGeSIYGRPFKDEFHSRLRFNRR 96
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688573424  97 GLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlADVACDGDERPLNPHKIRS 163
Cdd:cd00317   81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEgmDVVDKI---ERGDTDENGRPIKPVTISD 146
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 15-161 5.11e-48

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: 162.22  E-value: 5.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  15 VLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEFHSRLRFN 94
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688573424  95 RRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVT-GDTVYNMLRLADVacDGDERPLNPHKI 161
Cdd:cd01928   83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIdGFETLDTLEKLPV--DKKYRPLEEIRI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 7.64e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 7.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424   9 PPTNGKVLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGEsiyGRPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  89 SRLRfNRRGLVAMANA-GPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLADVACDGDERPLNPHKIRSTE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 688573424 166 VL 167
Cdd:COG0652  156 IV 157
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 16-161 1.00e-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: 153.39  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  16 LLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEFHSRLRFNR 95
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688573424  96 RGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLADVACDGDERPLNPHKI 161
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVV---QRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-161 1.18e-44

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: 153.07  E-value: 1.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  16 LLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYGRPFKDEFHSRLRFNR 95
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688573424  96 RGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVyNMLRLADVACDGDeRPLNPHKI 161
Cdd:cd01922   81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMK-VIENMVEVQTQTD-RPIDEVKI 144
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 16-174 6.99e-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: 141.32  E-value: 6.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  16 LLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESIYG-------RPFKDEFH 88
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  89 SRLRFNRRGLVAMANAGPHDNGSQFFFTLGRA-DELNNKHTIFGKVTgDTVYNMLRLADVACDGDERPLNPHKIRSTEVL 167
Cdd:cd01921   81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIKHTHIL 159


                 ....*..
gi 688573424 168 HSPFDDI 174
Cdd:cd01921  160 DDPFPDP 166
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 19-134 1.37e-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: 110.81  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  19 TSAGDIDIELWSKETPKACRNFVQLCmEG---------YYDGTIFHRMVPEFIVQGGD-PTGTGTGGESIYGRPFKDE-F 87
Cdd:cd01926   12 EPAGRIVMELFADVVPKTAENFRALC-TGekgkggkpfGYKGSTFHRVIPDFMIQGGDfTRGNGTGGKSIYGEKFPDEnF 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 688573424  88 HsrLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVT 134
Cdd:cd01926   91 K--LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV 135
PTZ00060 PTZ00060
cyclophilin; Provisional
 20-133 8.60e-28

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 109.16  E-value: 8.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  20 SAGDIDIELWSKETPKACRNFVQLCM------EG---YYDGTIFHRMVPEFIVQGGD-PTGTGTGGESIYGRPFKDEfHS 89
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCIgdkvgsSGknlHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDE-NF 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 688573424  90 RLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKV 133
Cdd:PTZ00060 107 KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKV 150
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 20-161 8.06e-26

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 103.76  E-value: 8.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  20 SAGDIDIELWSKETPKACRNFVQLCMEGY--------YDGTIFHRMVPEFIVQGGDPTGTGTGG-ESIYGRPFKDE-FHS 89
Cdd:PLN03149  31 PAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGcVSIYGSKFEDEnFIA 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688573424  90 RlrFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLADVACDGDERPLNPHKI 161
Cdd:PLN03149 111 K--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-163 1.93e-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: 95.97  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  16 LLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESiyGRPFKDEFHSRLRfNR 95
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLS-NT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688573424  96 RGLVAMA-NAGPHDNGSQFFFTLGRADELNNK-----HTIFGKVTG--DTVYNMLRLAdVACDG--DERPLNPHKIRS 163
Cdd:cd01920   78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEgmDVVDKIAGVE-TYSFGsyQDVPVQDVIIES 154
PRK10903 PRK10903
peptidylprolyl isomerase A;
15-133 4.59e-19

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 84.89  E-value: 4.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  15 VLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESiyGRPFKDEFHSRLRfN 94
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLR-N 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 688573424  95 RRGLVAMANAGPHDNG-SQFFFTLGRADELNN-----KHTIFGKV 133
Cdd:PRK10903 108 TRGTIAMARTADKDSAtSQFFINVADNAFLDHgqrdfGYAVFGKV 152
CWC27_CTD cd22288
C-terminal domain of spliceosome-associated protein CWC27 and similar proteins; CWC27, also ...
 370-425 1.34e-18

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: 79.27  E-value: 1.34e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688573424 370 KKGSGREAQTLALLESFKSKLSSAISETPSAPEEDVEELAEDDDKGWMAHVLHFDE 425
Cdd:cd22288    1 KKGASREEQTLALLEKFKSKLHSAKESTPEEEESKAEEDEDEDDDGWMSHKLHFED 56
PRK10791 PRK10791
peptidylprolyl isomerase B;
15-124 2.40e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 64.86  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  15 VLLKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGTGGESiyGRPFKDEFHSRLRfN 94
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKAT--KEPIKNEANNGLK-N 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 688573424  95 RRGLVAMANAG-PHDNGSQFFFTLGRADELN 124
Cdd:PRK10791  79 TRGTLAMARTQaPHSATAQFFINVVDNDFLN 109
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 17-147 8.75e-10

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: 57.84  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  17 LKTSAGDIDIELWSKETPKACRNFVQLCMEGYYDGTIFHRMVPEFIVQGGDPTGTGT---------------------GG 75
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPgfpdpetgksrtipleikpegQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  76 ESIYGRP------FKDEFhsRLRFNRRGLVAMANAGPHDNG--SQFFFTLG-------RADELNNKHTIFGKVT-GDTVY 139
Cdd:cd01924   82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVTdGLDIL 159


                 ....*...
gi 688573424 140 NMLRLADV 147
Cdd:cd01924  160 RELKVGDK 167
PTZ00221 PTZ00221
cyclophilin; Provisional
 77-158 4.16e-07

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 51.02  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  77 SIYGRPFKDEFHsRLRFNRRGLVAMANAGPHDNGSQFFFTLGRADELNNKHTIFGKVTgDTVYNMLRLADVACDGDERPL 156
Cdd:PTZ00221 131 SSTGTPIADEGY-RHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDVGRPL 208


                 ..
gi 688573424 157 NP 158
Cdd:PTZ00221 209 LP 210
PTZ00121 PTZ00121
MAEBL; Provisional
 272-467 3.65e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLKKDKTDEEKSSQDLVK----KTS----RSDELRKEARQLKKELLAIKQRKEDGVKKEEDVSEGD 343
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEeakkKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  344 SKQNSEAVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKSKLSSAISETPSApeEDVEELAEDDDKGWMAHVlHF 423
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA--DEAKKKAEEAKKADEAKK-KA 1492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 688573424  424 DEQSRKVKDANMQDEDTFEIYDPRNPVNKRRREESKKLLKDKKA 467
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
PTZ00121 PTZ00121
MAEBL; Provisional
 178-467 2.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  178 EIKGKKEKNK-DEAKKSQSKatknfsllsfgeeaeedeEMVNQVSQtmKGKSKSSHDLLKDDPKLSSVPVVDRNQGQGDF 256
Cdd:PTZ00121 1282 ELKKAEEKKKaDEAKKAEEK------------------KKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  257 EDSDDDEDDAEDDSDREAEKAKVRENIAKKlkkdKTDEEKSSQDLVKKTS----RSDELRKEARQLKKELLAIKQRKEDG 332
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEK----KKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAAK 1417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  333 VKKEEDVSEGDSKQNSEAVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKSKLSSAISETPSApeEDVEELAEDD 412
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEA 1495

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 688573424  413 DKgwMAHVLHFDEQSRKVKDANMQDEDTFEIYDPRNPVNKRRREESKKLLKDKKA 467
Cdd:PTZ00121 1496 KK--KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
PTZ00121 PTZ00121
MAEBL; Provisional
 272-469 2.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLK--KDKTDEEKSSQDLVKKTSRSDELRKEARQLKKELLAIKQRKEDGVKKEEDVSEGDSKQNSE 349
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  350 AVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKSKLSSAISETPSAPEED----VEELAEDDDKGWMAHVLHFDE 425
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkAEEAKKAEEAKIKAEELKKAE 1629

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 688573424  426 QSRKVKDANMQDEDTfeiyDPRNPVNKRRREESKKLLKDKKARR 469
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAE----EKKKAEELKKAEEENKIKAAEEAKK 1669
PTZ00121 PTZ00121
MAEBL; Provisional
 272-466 2.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLKKDKTDEEKSSQDLVKKTS---RSDELRKEARQLKKELLAIKQRKEDGVKKEE----------D 338
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakaeaeaaaD 1357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  339 VSEGDSKQNSEAVTEYLESRKKYDDMRKQKLKKGSGREAQTLALLESFKS-KLSSAISETPSApeEDVEELAEDDDKGwm 417
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdELKKAAAAKKKA--DEAKKKAEEKKKA-- 1433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 688573424  418 ahvlhfDEQSRKVKDANMQDEDTFEIYDPRNPVN-KRRREESKKLLKDKK 466
Cdd:PTZ00121 1434 ------DEAKKKAEEAKKADEAKKKAEEAKKAEEaKKKAEEAKKADEAKK 1477
PTZ00121 PTZ00121
MAEBL; Provisional
 272-466 1.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  272 REAEKAKVRENIAKKLKKDKTDEEKSSQDLVKKTSRSDELRK--EARQLKKELLAIKQRKEDGVKKEEDVSEGDSKQNSE 349
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688573424  350 AVTEYLESRKKYDDMRKQKLKKGSGREaQTLALLESFKSKLSSAISETPSAPEEDVEELAEDDDKGWMAHVLHFDEQsrk 429
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK--- 1768

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 688573424  430 vKDANMQDEDTFEIYDPRNPVNKRRREESKKLLKDKK 466
Cdd:PTZ00121 1769 -KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
 
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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