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Conserved domains on  [gi|663070907|ref|NP_001284573|]
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spliceosome-associated protein CWC27 homolog isoform 2 [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112476)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413
SCOP:  4000390

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 1.75e-134

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


:

Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 381.70  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070907 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
PTZ00121 super family cl31754
MAEBL; Provisional
 249-377 5.33e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  249 ESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMR-ERIAKKLKKDTSANVKSAGEGEVEKK---SVSRSEELRKEARQLK 324
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELK 1708

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 663070907  325 RELLAAKQKkvenaAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKK 377
Cdd:PTZ00121 1709 KKEAEEKKK-----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 1.75e-134

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


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 381.70  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070907 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 6.20e-61

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: 193.63  E-value: 6.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663070907  100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 9.42e-60

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.77  E-value: 9.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 663070907 166 VL 167
Cdd:COG0652  156 IV 157
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 9.77e-35

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 126.50  E-value: 9.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060  29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070907  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060 108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
PTZ00121 PTZ00121
MAEBL; Provisional
 249-377 5.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  249 ESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMR-ERIAKKLKKDTSANVKSAGEGEVEKK---SVSRSEELRKEARQLK 324
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELK 1708

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 663070907  325 RELLAAKQKkvenaAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKK 377
Cdd:PTZ00121 1709 KKEAEEKKK-----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 263-374 6.49e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  263 EDESAEHDEYIDGDEknLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEArqLKRELLAAKQKKVE--NAAK 340
Cdd:pfam17380 441 EEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMIEeeRKRK 516

                          90       100       110
                  ....*....|....*....|....*....|....
gi 663070907  341 QAEKRSEEEEAppdgAVAEYRREKQKYEALRKQQ 374
Cdd:pfam17380 517 LLEKEMEERQK----AIYEEERRREAEEERRKQQ 546
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 239-377 1.91e-03

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


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 40.44  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907 239 DPHLSSVPVVESEKGDAPDLVDDGEDESAEHD--EYIDGDEKNLMRERI----AKKLK-KDTSANVKSAGEgeveKKSVS 311
Cdd:COG5163  457 DPRASLMTMEETQRHSEEDLVNRFEDVRYEHVagEEDDDDDEELQAQKEleleAQGIKySETSEADKDVNK----SKNKK 532

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663070907 312 RSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSEEEEappdgavAEYRREKQKYEALRKQQSKK 377
Cdd:COG5163  533 RKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEEQA-------ENLKKKKKQIAKQKKLDSKK 591
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 1.75e-134

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


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 381.70  E-value: 1.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070907 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-171 3.22e-64

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


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 202.26  E-value: 3.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070907  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKSCEVLFNPF 171
Cdd:cd01923   82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGglETLEAM---ENVPDPGTDRPKEEIKIEDTSVFVDPF 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-163 4.13e-61

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 193.63  E-value: 4.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGeSIYGAPFKDEFHSRLRFNRR 96
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070907  97 GLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKS 163
Cdd:cd00317   81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEgmDVVDKI---ERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 6.20e-61

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: 193.63  E-value: 6.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663070907  100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 9.42e-60

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.77  E-value: 9.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 663070907 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 2.35e-58

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


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 186.87  E-value: 2.35e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070907  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT-GDTVYNMLRLSEVDIDDdeRPHNPHKIK 162
Cdd:cd01928   83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIdGFETLDTLEKLPVDKKY--RPLEEIRIK 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 16-161 8.05e-57

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


Pssm-ID: 238908 [Multi-domain]  Cd Length: 148  Bit Score: 183.05  E-value: 8.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663070907  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKI 161
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVV---QRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-155 4.97e-56

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


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 180.81  E-value: 4.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVyNMLRLSEVDIDDDeRP 155
Cdd:cd01922   81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMK-VIENMVEVQTQTD-RP 138
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 16-174 4.04e-49

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


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 163.67  E-value: 4.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYG-------APFKDEFH 88
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  89 SRLRFNRRGLVAMANAGSHDNGSQFFFTLGRA-DELNNKHTIFGKVTgDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01921   81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIKHTHIL 159


                 ....*..
gi 663070907 168 FNPFDDI 174
Cdd:cd01921  160 DDPFPDP 166
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 21-134 1.27e-37

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 133.54  E-value: 1.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  21 AGDIDIELWSKEAPKACRNFIQLC--------LEAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDE-FHsr 90
Cdd:cd01926   14 AGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDEnFK-- 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663070907  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT 134
Cdd:cd01926   92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV 135
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 9.77e-35

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 126.50  E-value: 9.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060  29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070907  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060 108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 10-164 8.30e-34

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 124.18  E-value: 8.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  10 PTNGKVLLKTT-----AGDIDIELWSKEAPKACRNFIQLCLEAY--------YDNTIFHRVVPGFIVQGGD-PTGTGSGG 75
Cdd:PLN03149  16 PKNPVVFFDVTiggipAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  76 ESIYGAPFKDE-FHSRlrFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDER 154
Cdd:PLN03149  96 VSIYGSKFEDEnFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNR 173

                        170
                 ....*....|
gi 663070907 155 PHNPHKIKSC 164
Cdd:PLN03149 174 PKLACVISEC 183
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-135 6.36e-25

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


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 99.44  E-value: 6.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESiyGAPFKDEFHSRLRfNR 95
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLS-NT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663070907  96 RGLVAMA-NAGSHDNGSQFFFTLGRADELNNK-----HTIFGKVTG 135
Cdd:cd01920   78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTE 123
PRK10903 PRK10903
peptidylprolyl isomerase A;
15-167 2.08e-24

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 99.15  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSggESIYGAPFKDEFHSRLRfN 94
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQ--QKKPNPPIKNEADNGLR-N 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  95 RRGLVAMANAGSHDNG-SQFFFTLGRADELNNKHTIFG-KVTGDTVYNML---RLSEVDIDD----DERPHNPHKIKSCE 165
Cdd:PRK10903 108 TRGTIAMARTADKDSAtSQFFINVADNAFLDHGQRDFGyAVFGKVVKGMDvadKISQVPTHDvgpyQNVPSKPVVILSAK 187


                 ..
gi 663070907 166 VL 167
Cdd:PRK10903 188 VL 189
PRK10791 PRK10791
peptidylprolyl isomerase B;
15-124 3.23e-16

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 75.65  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGdptGTGSG-GESIYGAPFKDEFHSRLRf 93
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGmKQKATKEPIKNEANNGLK- 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663070907  94 NRRGLVAMANAGS-HDNGSQFFFTLGRADELN 124
Cdd:PRK10791  78 NTRGTLAMARTQApHSATAQFFINVVDNDFLN 109
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 17-134 1.07e-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: 71.71  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSG---------------------G 75
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070907  76 ESIYGAP------FKDEFhsRLRFNRRGLVAMANAGSHDNG--SQFFFTLG-------RADELNNKHTIFGKVT 134
Cdd:cd01924   82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVT 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 73-170 3.66e-07

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 51.02  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  73 SGGESIYGAPFKDEFHsRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTgDTVYNMLRLSEVDIDDD 152
Cdd:PTZ00221 127 SFNVSSTGTPIADEGY-RHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDV 204

                         90
                 ....*....|....*...
gi 663070907 153 ERPHNPHKIKSCEVLFNP 170
Cdd:PTZ00221 205 GRPLLPVTVSFCGALTGE 222
PTZ00121 PTZ00121
MAEBL; Provisional
 249-377 5.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  249 ESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMR-ERIAKKLKKDTSANVKSAGEGEVEKK---SVSRSEELRKEARQLK 324
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELK 1708

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 663070907  325 RELLAAKQKkvenaAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKK 377
Cdd:PTZ00121 1709 KKEAEEKKK-----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 263-374 6.49e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  263 EDESAEHDEYIDGDEknLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEArqLKRELLAAKQKKVE--NAAK 340
Cdd:pfam17380 441 EEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--LEKELEERKQAMIEeeRKRK 516

                          90       100       110
                  ....*....|....*....|....*....|....
gi 663070907  341 QAEKRSEEEEAppdgAVAEYRREKQKYEALRKQQ 374
Cdd:pfam17380 517 LLEKEMEERQK----AIYEEERRREAEEERRKQQ 546
PTZ00121 PTZ00121
MAEBL; Provisional
 264-382 6.55e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  264 DESAEHDEYIDGDEKNLMRERiAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEARQLKREL-----LAAKQKKVENA 338
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelkkAAAAKKKADEA 1423

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 663070907  339 AKQAEKRSEEEEAPPDGAVAEYRRE-KQKYEALRKQQSKKGTSRE 382
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEE 1468
NOP7 COG5163
Protein required for biogenesis of the 60S ribosomal subunit [Translation, ribosomal structure ...
 239-377 1.91e-03

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


Pssm-ID: 227492 [Multi-domain]  Cd Length: 591  Bit Score: 40.44  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907 239 DPHLSSVPVVESEKGDAPDLVDDGEDESAEHD--EYIDGDEKNLMRERI----AKKLK-KDTSANVKSAGEgeveKKSVS 311
Cdd:COG5163  457 DPRASLMTMEETQRHSEEDLVNRFEDVRYEHVagEEDDDDDEELQAQKEleleAQGIKySETSEADKDVNK----SKNKK 532

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663070907 312 RSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSEEEEappdgavAEYRREKQKYEALRKQQSKK 377
Cdd:COG5163  533 RKVDEEEEEKKLKMIMMSNKQKKLYKKMKYSNAKKEEQA-------ENLKKKKKQIAKQKKLDSKK 591
PTZ00121 PTZ00121
MAEBL; Provisional
 286-382 2.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  286 AKKLKKDTSANvKSAGEGEVEKKSVSRSEELRKEARQLKRELLAAKQ----KKVENAAKQAE--------KRSEEEEAPP 353
Cdd:PTZ00121 1407 ADELKKAAAAK-KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeaKKAEEAKKKAEeakkadeaKKKAEEAKKA 1485

                          90       100
                  ....*....|....*....|....*....
gi 663070907  354 DGAVAEYRREKQKYEALRKQQSKKGTSRE 382
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
PTZ00121 PTZ00121
MAEBL; Provisional
 226-377 2.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  226 KGKSKSSHDLLKDDPHLSSVPVVESEKGDAPDLVDDGEDESAEHDEYIDGDEKNLMRERIAKKLKKdTSANVKSAGEGEV 305
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKAEEAKK 1464

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663070907  306 EKKSVSRSEELRKEARQLKRELLAakQKKVENAAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKK 377
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 306-384 6.13e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 38.78  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907 306 EKKsvsRSEE--LRKEARQ--LKREllaaKQKKVENAAKQAEKRSEEEEAPPDGAVAeyrREKQKYEALRKQQSKKGTSR 381
Cdd:PRK05035 444 EKK---KAEEakARFEARQarLERE----KAAREARHKKAAEARAAKDKDAVAAALA---RVKAKKAAATQPIVIKAGAR 513


                 ...
gi 663070907 382 EDQ 384
Cdd:PRK05035 514 PDN 516
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 277-385 6.41e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  277 EKNLMRERIAKKLKKDTSANVKSAGEGEVEKKSVSRSEELRKEARQLKRELLAAKQKKVENAAKQAEKRSEEEEAppdgA 356
Cdd:pfam13868  99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA----E 174

                          90       100       110
                  ....*....|....*....|....*....|
gi 663070907  357 VAEYRREKQK-YEALRKQQSKKGTSREDQD 385
Cdd:pfam13868 175 REEIEEEKEReIARLRAQQEKAQDEKAERD 204
PTZ00121 PTZ00121
MAEBL; Provisional
 249-379 6.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070907  249 ESEKGDAPDLVDDGEDESAEHDEYIDGDEKnlmrERIAKKLKKDTSANVKSAGE-GEVEKKSVSRSEELRKEARQLKREL 327
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEAKKEAEEDKKKA 1746

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 663070907  328 LAAK-----QKKVENAAKQAEKRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKKGT 379
Cdd:PTZ00121 1747 EEAKkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 306-377 7.92e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.56  E-value: 7.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070907  306 EKKSVSRSEELRKEARQLKRELLAAKQKKVENAAKQAE--KRSEEEEAPPDGAVAEYRREKQKYEALRKQQSKK 377
Cdd:pfam05672  31 EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEerRREEEERQRKAEEEAEEREQREQEEQERLQKQKE 104
 
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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