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Conserved domains on  [gi|270288729|ref|NP_001161834|]
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protocadherin-11 X-linked isoform g precursor [Homo sapiens]

Protein Classification

protocadherin( domain architecture ID 13228258)

protocadherin is a transmembrane protein belonging to the cadherin superfamily and may be a calcium-dependent cell-adhesion protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Protocadherin pfam08374
Protocadherin; The structure of protocadherins is similar to that of classic cadherins ...
 775-976 3.38e-82

Protocadherin; The structure of protocadherins is similar to that of classic cadherins (pfam00028), but particularly on the cytoplasmic domains they also have some unique features. They are expressed in a variety of organizms and are found in high concentrations in the brain where they seem to be localized mainly at cell-cell contact sites. Their expression seems to be developmentally regulated.


:

Pssm-ID: 462451  Cd Length: 217  Bit Score: 268.15  E-value: 3.38e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   775 SVTNATLINELVRKSTEAPVTPNT-EIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVR-CRQA--PHLKAAQKnkQ 850
Cdd:pfam08374    1 SLANATLVEELVRRSLETPLDRDIaGDPDYSSLGKDYLKILIAILAGAMTVILVIFIVVLVRyCRQKekPGYKAGKK--Q 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   851 NSEWATPNPENRQMIMMKKK---KKKKKHSPKNLLLNFVTIEETKADDVDSDGNRVTLDLPIdleeqtmgkynwvTTPTT 927
Cdd:pfam08374   79 NSDWVTPNPENKQMKGKKKKkkkRPKPAKLPKSLLLNLVTIEESKPDDVENEGDSPRIDLPI-------------TLPTT 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 270288729   928 FKPDSPDLARHYKSASPQPAFQIQPETPLN-SKHHIIQELPLDNTFV-ACD 976
Cdd:pfam08374  146 FKPDSPDLARHYKSNSPLPAFQLQPESPSAsKKHQAVQELPLDNTFVgTGD 196
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 253-351 5.44e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  253 EIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDG 332
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77

                          90       100
                  ....*....|....*....|.
gi 270288729  333 GLMP--ARAMVLVNVTDVNDN 351
Cdd:cd11304    78 GGPPlsSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 574-669 5.99e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  574 EYNFYVPENLPRHGTVGLITVTDPDYGDNSAVTLSILDENDD--FTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRV 651
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 270288729  652 SRSSSAKVTINVVDVNDN 669
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 472-566 4.21e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 117.80  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  472 TVSIPENNSPGIQLTKVSAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPL 550
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPL 82

                          90
                  ....*....|....*.
gi 270288729  551 TSNVTVFVSIIDQNDN 566
Cdd:cd11304    83 SSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 143-245 9.86e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 88.14  E-value: 9.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  143 VINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIkSQNIFGLDVIETPEGDkmpqLIVQKELDREEKDTYVMKVKVE 222
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV-SGNEDGLFSIDPSTGE----ITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|...
gi 270288729  223 DGGFPQRSSTAILQVSVTDTNDN 245
Cdd:cd11304    76 DGGGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 681-772 2.71e-20

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 86.98  E-value: 2.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  681 SYELVLP-STNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQP 759
Cdd:cd11304     1 SYEVSVPeNAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|...
gi 270288729  760 dSLFSVVIVNLFV 772
Cdd:cd11304    81 -PLSSTATVTITV 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 384-464 3.03e-12

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


:

Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 63.52  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    384 TVTDKDADHNGRVTCF---TDHEIPFRLRPvfsNQFLLETAAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDEN 460
Cdd:smart00112    1 SATDADSGENGKVTYSilsGNDDGLFSIDP---ETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77


                    ....
gi 270288729    461 DNAP 464
Cdd:smart00112   78 DNAP 81
Cadherin_2 super family cl29227
Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.
 28-102 3.50e-06

Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.


The actual alignment was detected with superfamily member pfam08266:

Pssm-ID: 462413  Cd Length: 83  Bit Score: 46.37  E-value: 3.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270288729    28 YTIREEMPENVLIGDLLKDLNLSLipnKSLtTAMQFKLVYKtGDVPLIRIEEDTGEIFTTGaRIDREKLCAGIPR 102
Cdd:pfam08266    4 YSVPEETERGSFVGNLAKDLGLEV---GEL-AARGARVVSK-GNKQYFQLNPETGDLLLNE-KLDREELCGSTEP 72
FAM47 super family cl25915
FAM47 family; The function of this Chordate family of proteins is not known.
 1149-1217 9.49e-05

FAM47 family; The function of this Chordate family of proteins is not known.


The actual alignment was detected with superfamily member pfam14642:

Pssm-ID: 405345 [Multi-domain]  Cd Length: 257  Bit Score: 45.64  E-value: 9.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270288729  1149 SPRVTQTIALC--HSPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASALCYSPPLAQAAA 1217
Cdd:pfam14642  187 SPRPPETRVSClpPEPPKTPVSSLRPEPPETGVSHLRPQPPKTQVSSLHLEPPETGVSHLRPEPPKTQVSS 257
 
Name Accession Description Interval E-value
Protocadherin pfam08374
Protocadherin; The structure of protocadherins is similar to that of classic cadherins ...
 775-976 3.38e-82

Protocadherin; The structure of protocadherins is similar to that of classic cadherins (pfam00028), but particularly on the cytoplasmic domains they also have some unique features. They are expressed in a variety of organizms and are found in high concentrations in the brain where they seem to be localized mainly at cell-cell contact sites. Their expression seems to be developmentally regulated.


Pssm-ID: 462451  Cd Length: 217  Bit Score: 268.15  E-value: 3.38e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   775 SVTNATLINELVRKSTEAPVTPNT-EIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVR-CRQA--PHLKAAQKnkQ 850
Cdd:pfam08374    1 SLANATLVEELVRRSLETPLDRDIaGDPDYSSLGKDYLKILIAILAGAMTVILVIFIVVLVRyCRQKekPGYKAGKK--Q 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   851 NSEWATPNPENRQMIMMKKK---KKKKKHSPKNLLLNFVTIEETKADDVDSDGNRVTLDLPIdleeqtmgkynwvTTPTT 927
Cdd:pfam08374   79 NSDWVTPNPENKQMKGKKKKkkkRPKPAKLPKSLLLNLVTIEESKPDDVENEGDSPRIDLPI-------------TLPTT 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 270288729   928 FKPDSPDLARHYKSASPQPAFQIQPETPLN-SKHHIIQELPLDNTFV-ACD 976
Cdd:pfam08374  146 FKPDSPDLARHYKSNSPLPAFQLQPESPSAsKKHQAVQELPLDNTFVgTGD 196
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 253-351 5.44e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  253 EIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDG 332
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77

                          90       100
                  ....*....|....*....|.
gi 270288729  333 GLMP--ARAMVLVNVTDVNDN 351
Cdd:cd11304    78 GGPPlsSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 574-669 5.99e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  574 EYNFYVPENLPRHGTVGLITVTDPDYGDNSAVTLSILDENDD--FTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRV 651
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 270288729  652 SRSSSAKVTINVVDVNDN 669
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 472-566 4.21e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 117.80  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  472 TVSIPENNSPGIQLTKVSAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPL 550
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPL 82

                          90
                  ....*....|....*.
gi 270288729  551 TSNVTVFVSIIDQNDN 566
Cdd:cd11304    83 SSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 489-568 6.78e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 96.65  E-value: 6.78e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    489 SAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPLTSNVTVFVSIIDQNDNS 567
Cdd:smart00112    1 SATDADSGENGKVTYsILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 270288729    568 P 568
Cdd:smart00112   81 P 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 593-671 1.92e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 95.11  E-value: 1.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    593 TVTDPDYGDNSAVTLSILDENDD--FTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTINVVDVNDNK 670
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 270288729    671 P 671
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
254-346 6.92e-22

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.21  E-value: 6.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   254 IEVSIPENAPVGTSVTQLHATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDGG 333
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYS---ILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77

                           90
                   ....*....|....*
gi 270288729   334 LMP--ARAMVLVNVT 346
Cdd:pfam00028   78 GPPlsSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 272-353 2.17e-21

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 89.33  E-value: 2.17e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    272 HATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDGGLMP--ARAMVLVNVTDVN 349
Cdd:smart00112    1 SATDADSGENGKVTYS---ILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPlsSTATVTITVLDVN 77


                    ....
gi 270288729    350 DNVP 353
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
575-663 6.30e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 88.51  E-value: 6.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   575 YNFYVPENLPRHGTVGLITVTDPDYGDNSAVTLSIL--DENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVS 652
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILggGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|.
gi 270288729   653 RSSSAKVTINV 663
Cdd:pfam00028   81 LSSTATVTITV 91
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 143-245 9.86e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 88.14  E-value: 9.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  143 VINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIkSQNIFGLDVIETPEGDkmpqLIVQKELDREEKDTYVMKVKVE 222
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV-SGNEDGLFSIDPSTGE----ITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|...
gi 270288729  223 DGGFPQRSSTAILQVSVTDTNDN 245
Cdd:cd11304    76 DGGGPPLSSTATVTITVLDVNDN 98
Cadherin pfam00028
Cadherin domain;
472-561 1.85e-20

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 86.97  E-value: 1.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   472 TVSIPENNSPGIQLTKVSAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPL 550
Cdd:pfam00028    2 SASVPENAPVGTEVLTVTATDPDLGPNGRIFYsILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPPL 81

                           90
                   ....*....|.
gi 270288729   551 TSNVTVFVSII 561
Cdd:pfam00028   82 SSTATVTITVL 92
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 681-772 2.71e-20

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 86.98  E-value: 2.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  681 SYELVLP-STNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQP 759
Cdd:cd11304     1 SYEVSVPeNAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|...
gi 270288729  760 dSLFSVVIVNLFV 772
Cdd:cd11304    81 -PLSSTATVTITV 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 163-247 3.04e-16

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 74.69  E-value: 3.04e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    163 AVDPDVGINGVQNYElIKSQNIFGLDVIETPEGdkmpQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242
Cdd:smart00112    2 ATDADSGENGKVTYS-ILSGNDDGLFSIDPETG----EITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDV 76


                    ....*
gi 270288729    243 NDNHP 247
Cdd:smart00112   77 NDNAP 81
Cadherin pfam00028
Cadherin domain;
691-772 6.37e-14

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 68.48  E-value: 6.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   691 PGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPdSLFSVVIVNL 770
Cdd:pfam00028   11 VGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP-PLSSTATVTI 89


                   ..
gi 270288729   771 FV 772
Cdd:pfam00028   90 TV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 384-464 3.03e-12

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 63.52  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    384 TVTDKDADHNGRVTCF---TDHEIPFRLRPvfsNQFLLETAAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDEN 460
Cdd:smart00112    1 SATDADSGENGKVTYSilsGNDDGLFSIDP---ETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77


                    ....
gi 270288729    461 DNAP 464
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
144-240 1.65e-11

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 61.55  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   144 INISIPENSAINSKYTLPAAVDPDVGINGVQNYeLIKSQNIFGLDVIETPEGDkmpqLIVQKELDREEKDTYVMKVKVED 223
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFY-SILGGGPGGNFRIDPDTGD----ISTTKPLDRESIGEYELTVEATD 75

                           90
                   ....*....|....*..
gi 270288729   224 GGFPQRSSTAILQVSVT 240
Cdd:pfam00028   76 SGGPPLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 700-772 1.75e-11

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 61.21  E-value: 1.75e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 270288729    700 AVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPdSLFSVVIVNLFV 772
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGP-PLSSTATVTITV 73
Cadherin pfam00028
Cadherin domain;
367-456 1.52e-09

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 56.15  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   367 TVVLSENIPLNTKIALITVTDKDADHNGRVTcftdHEIpfrLRPVFSNQF-------LLETAAYLDYESTKEYAIKLLAA 439
Cdd:pfam00028    2 SASVPENAPVGTEVLTVTATDPDLGPNGRIF----YSI---LGGGPGGNFridpdtgDISTTKPLDRESIGEYELTVEAT 74

                           90
                   ....*....|....*..
gi 270288729   440 DAGKPPLNQSAMLFIKV 456
Cdd:pfam00028   75 DSGGPPLSSTATVTITV 91
Cadherin_2 pfam08266
Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.
 28-102 3.50e-06

Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.


Pssm-ID: 462413  Cd Length: 83  Bit Score: 46.37  E-value: 3.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270288729    28 YTIREEMPENVLIGDLLKDLNLSLipnKSLtTAMQFKLVYKtGDVPLIRIEEDTGEIFTTGaRIDREKLCAGIPR 102
Cdd:pfam08266    4 YSVPEETERGSFVGNLAKDLGLEV---GEL-AARGARVVSK-GNKQYFQLNPETGDLLLNE-KLDREELCGSTEP 72
FAM47 pfam14642
FAM47 family; The function of this Chordate family of proteins is not known.
 1149-1217 9.49e-05

FAM47 family; The function of this Chordate family of proteins is not known.


Pssm-ID: 405345 [Multi-domain]  Cd Length: 257  Bit Score: 45.64  E-value: 9.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270288729  1149 SPRVTQTIALC--HSPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASALCYSPPLAQAAA 1217
Cdd:pfam14642  187 SPRPPETRVSClpPEPPKTPVSSLRPEPPETGVSHLRPQPPKTQVSSLHLEPPETGVSHLRPEPPKTQVSS 257
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
 1134-1243 1.68e-03

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 41.46  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729 1134 LC----HSPPLSQASTQHHSPRVTQTIALCHSPPVTQTIALCHSPPPIQ---VSALHHspplvqaTAlhHSPPSAQASAL 1206
Cdd:cd21974    56 LCmtppYSPPFFEASHSPSVASLHPPSAASSQPPPEPESSEPPAASPQRaqaTSVIRH-------TA--DPVPVSPPPVL 126

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 270288729 1207 CYSPPLAQAAAISHSSPLPQVIALHRSQAQSSVSLQQ 1243
Cdd:cd21974   127 CQMLPVSSSSGVIVAFLKAPQQPSPQPQKPALPQPQV 163
CopL_fam NF033807
CopL family metal-binding regulatory protein; The founding member of this family was shown to ...
 1143-1228 3.32e-03

CopL family metal-binding regulatory protein; The founding member of this family was shown to be involved in the copper-responsive expression of a multicopper oxidase copA encoded downstream. The regulatory function likely involves copper-binding, but activity as a DNA-binding transcriptional regulator was not demonstrated directly.


Pssm-ID: 468190 [Multi-domain]  Cd Length: 129  Bit Score: 39.24  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729 1143 ASTQHHSPRVTQTIALCHSPPVTQTIALCH----SPPPIQVSALHHSPPL-------------VQATALHHSPPSAQASA 1205
Cdd:NF033807   21 ASVRMAMPHMAAAAAAAAAAAAAAAAAPCHgdapAAAAAAPPAADHDPHAddccksgscdcacAQHCSAALPTLPALPAH 100

                          90       100
                  ....*....|....*....|....
gi 270288729 1206 LCYSPPLAQAAAISHSSP-LPQVI 1228
Cdd:NF033807  101 LPGSLAVAAPLLSGHPSPaLPHLF 124
 
Name Accession Description Interval E-value
Protocadherin pfam08374
Protocadherin; The structure of protocadherins is similar to that of classic cadherins ...
 775-976 3.38e-82

Protocadherin; The structure of protocadherins is similar to that of classic cadherins (pfam00028), but particularly on the cytoplasmic domains they also have some unique features. They are expressed in a variety of organizms and are found in high concentrations in the brain where they seem to be localized mainly at cell-cell contact sites. Their expression seems to be developmentally regulated.


Pssm-ID: 462451  Cd Length: 217  Bit Score: 268.15  E-value: 3.38e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   775 SVTNATLINELVRKSTEAPVTPNT-EIADVSSPTSDYVKILVAAVAGTITVVVVIFITAVVR-CRQA--PHLKAAQKnkQ 850
Cdd:pfam08374    1 SLANATLVEELVRRSLETPLDRDIaGDPDYSSLGKDYLKILIAILAGAMTVILVIFIVVLVRyCRQKekPGYKAGKK--Q 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   851 NSEWATPNPENRQMIMMKKK---KKKKKHSPKNLLLNFVTIEETKADDVDSDGNRVTLDLPIdleeqtmgkynwvTTPTT 927
Cdd:pfam08374   79 NSDWVTPNPENKQMKGKKKKkkkRPKPAKLPKSLLLNLVTIEESKPDDVENEGDSPRIDLPI-------------TLPTT 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 270288729   928 FKPDSPDLARHYKSASPQPAFQIQPETPLN-SKHHIIQELPLDNTFV-ACD 976
Cdd:pfam08374  146 FKPDSPDLARHYKSNSPLPAFQLQPESPSAsKKHQAVQELPLDNTFVgTGD 196
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 253-351 5.44e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  253 EIEVSIPENAPVGTSVTQLHATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDG 332
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77

                          90       100
                  ....*....|....*....|.
gi 270288729  333 GLMP--ARAMVLVNVTDVNDN 351
Cdd:cd11304    78 GGPPlsSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 574-669 5.99e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 123.19  E-value: 5.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  574 EYNFYVPENLPRHGTVGLITVTDPDYGDNSAVTLSILDENDD--FTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRV 651
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 270288729  652 SRSSSAKVTINVVDVNDN 669
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 472-566 4.21e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 117.80  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  472 TVSIPENNSPGIQLTKVSAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPL 550
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPPL 82

                          90
                  ....*....|....*.
gi 270288729  551 TSNVTVFVSIIDQNDN 566
Cdd:cd11304    83 SSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 489-568 6.78e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 96.65  E-value: 6.78e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    489 SAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPLTSNVTVFVSIIDQNDNS 567
Cdd:smart00112    1 SATDADSGENGKVTYsILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 270288729    568 P 568
Cdd:smart00112   81 P 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 593-671 1.92e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 95.11  E-value: 1.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    593 TVTDPDYGDNSAVTLSILDENDD--FTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVSRSSSAKVTINVVDVNDNK 670
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 270288729    671 P 671
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
254-346 6.92e-22

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.21  E-value: 6.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   254 IEVSIPENAPVGTSVTQLHATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDGG 333
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYS---ILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77

                           90
                   ....*....|....*
gi 270288729   334 LMP--ARAMVLVNVT 346
Cdd:pfam00028   78 GPPlsSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 272-353 2.17e-21

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 89.33  E-value: 2.17e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    272 HATDADIGENAKIHFSfsnLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLASDGGLMP--ARAMVLVNVTDVN 349
Cdd:smart00112    1 SATDADSGENGKVTYS---ILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPlsSTATVTITVLDVN 77


                    ....
gi 270288729    350 DNVP 353
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
575-663 6.30e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 88.51  E-value: 6.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   575 YNFYVPENLPRHGTVGLITVTDPDYGDNSAVTLSIL--DENDDFTIDSQTGVIRPNISFDREKQESYTFYVKAEDGGRVS 652
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILggGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|.
gi 270288729   653 RSSSAKVTINV 663
Cdd:pfam00028   81 LSSTATVTITV 91
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 143-245 9.86e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 88.14  E-value: 9.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  143 VINISIPENSAINSKYTLPAAVDPDVGINGVQNYELIkSQNIFGLDVIETPEGDkmpqLIVQKELDREEKDTYVMKVKVE 222
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV-SGNEDGLFSIDPSTGE----ITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|...
gi 270288729  223 DGGFPQRSSTAILQVSVTDTNDN 245
Cdd:cd11304    76 DGGGPPLSSTATVTITVLDVNDN 98
Cadherin pfam00028
Cadherin domain;
472-561 1.85e-20

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 86.97  E-value: 1.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   472 TVSIPENNSPGIQLTKVSAMDADSGPNAKINY-LLGPDAPPEFSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPPL 550
Cdd:pfam00028    2 SASVPENAPVGTEVLTVTATDPDLGPNGRIFYsILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPPL 81

                           90
                   ....*....|.
gi 270288729   551 TSNVTVFVSII 561
Cdd:pfam00028   82 SSTATVTITVL 92
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 681-772 2.71e-20

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 86.98  E-value: 2.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  681 SYELVLP-STNPGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQP 759
Cdd:cd11304     1 SYEVSVPeNAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|...
gi 270288729  760 dSLFSVVIVNLFV 772
Cdd:cd11304    81 -PLSSTATVTITV 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 163-247 3.04e-16

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 74.69  E-value: 3.04e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    163 AVDPDVGINGVQNYElIKSQNIFGLDVIETPEGdkmpQLIVQKELDREEKDTYVMKVKVEDGGFPQRSSTAILQVSVTDT 242
Cdd:smart00112    2 ATDADSGENGKVTYS-ILSGNDDGLFSIDPETG----EITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDV 76


                    ....*
gi 270288729    243 NDNHP 247
Cdd:smart00112   77 NDNAP 81
Cadherin pfam00028
Cadherin domain;
691-772 6.37e-14

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 68.48  E-value: 6.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   691 PGTVVFQVIAVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPdSLFSVVIVNL 770
Cdd:pfam00028   11 VGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP-PLSSTATVTI 89


                   ..
gi 270288729   771 FV 772
Cdd:pfam00028   90 TV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 384-464 3.03e-12

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 63.52  E-value: 3.03e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729    384 TVTDKDADHNGRVTCF---TDHEIPFRLRPvfsNQFLLETAAYLDYESTKEYAIKLLAADAGKPPLNQSAMLFIKVKDEN 460
Cdd:smart00112    1 SATDADSGENGKVTYSilsGNDDGLFSIDP---ETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77


                    ....
gi 270288729    461 DNAP 464
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
144-240 1.65e-11

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 61.55  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   144 INISIPENSAINSKYTLPAAVDPDVGINGVQNYeLIKSQNIFGLDVIETPEGDkmpqLIVQKELDREEKDTYVMKVKVED 223
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFY-SILGGGPGGNFRIDPDTGD----ISTTKPLDRESIGEYELTVEATD 75

                           90
                   ....*....|....*..
gi 270288729   224 GGFPQRSSTAILQVSVT 240
Cdd:pfam00028   76 SGGPPLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 700-772 1.75e-11

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 61.21  E-value: 1.75e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 270288729    700 AVDNDTGMNAEVRYSIVGGNTRDLFAIDQETGNITLMEKCDVTDLGLHRVLVKANDLGQPdSLFSVVIVNLFV 772
Cdd:smart00112    2 ATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGP-PLSSTATVTITV 73
Cadherin pfam00028
Cadherin domain;
367-456 1.52e-09

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 56.15  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729   367 TVVLSENIPLNTKIALITVTDKDADHNGRVTcftdHEIpfrLRPVFSNQF-------LLETAAYLDYESTKEYAIKLLAA 439
Cdd:pfam00028    2 SASVPENAPVGTEVLTVTATDPDLGPNGRIF----YSI---LGGGPGGNFridpdtgDISTTKPLDRESIGEYELTVEAT 74

                           90
                   ....*....|....*..
gi 270288729   440 DAGKPPLNQSAMLFIKV 456
Cdd:pfam00028   75 DSGGPPLSSTATVTITV 91
Cadherin_2 pfam08266
Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.
 28-102 3.50e-06

Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.


Pssm-ID: 462413  Cd Length: 83  Bit Score: 46.37  E-value: 3.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270288729    28 YTIREEMPENVLIGDLLKDLNLSLipnKSLtTAMQFKLVYKtGDVPLIRIEEDTGEIFTTGaRIDREKLCAGIPR 102
Cdd:pfam08266    4 YSVPEETERGSFVGNLAKDLGLEV---GEL-AARGARVVSK-GNKQYFQLNPETGDLLLNE-KLDREELCGSTEP 72
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 254-351 6.22e-05

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 43.10  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  254 IEVSIPENAPVGTSVTQLhatDADIGENAKIHFSFSNLVSNIARRLFHLNATTGLITIKEPLDREETPNHKLLVLA-SDG 332
Cdd:cd00031     2 PDGSAVEGRSRGSFRVSI---PTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLEKLDREDKGVHYISVSAaSLG 78

                          90       100
                  ....*....|....*....|
gi 270288729  333 GLMPARAMVLV-NVTDVNDN 351
Cdd:cd00031    79 ANVPQTSSVFSiEVYDENDN 98
FAM47 pfam14642
FAM47 family; The function of this Chordate family of proteins is not known.
 1149-1217 9.49e-05

FAM47 family; The function of this Chordate family of proteins is not known.


Pssm-ID: 405345 [Multi-domain]  Cd Length: 257  Bit Score: 45.64  E-value: 9.49e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270288729  1149 SPRVTQTIALC--HSPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASALCYSPPLAQAAA 1217
Cdd:pfam14642  187 SPRPPETRVSClpPEPPKTPVSSLRPEPPETGVSHLRPQPPKTQVSSLHLEPPETGVSHLRPEPPKTQVSS 257
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 472-566 1.07e-04

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 42.72  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729  472 TVSIPENNSPGIQLTKV-SAMDADSGPNAKINYLlGPDAPPE-FSLDCRTGMLTVVKKLDREKEDKYLFTILAKDNGVPP 549
Cdd:cd00031     3 DGSAVEGRSRGSFRVSIpTDLIASSGEIIKISAA-GKEALPSwLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANV 81

                          90
                  ....*....|....*..
gi 270288729  550 LTSNVTVFVSIIDQNDN 566
Cdd:cd00031    82 PQTSSVFSIEVYDENDN 98
Cadherin_2 pfam08266
Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.
 254-319 2.47e-04

Cadherin-like; This cadherin domain is usually the most N-terminal copy of the domain.


Pssm-ID: 462413  Cd Length: 83  Bit Score: 40.97  E-value: 2.47e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270288729   254 IEVSIPENAPVGTSVTQLhATD--ADIGE----NAKIhfsfsnlVSNIARRLFHLNATTGLITIKEPLDREE 319
Cdd:pfam08266    2 IRYSVPEETERGSFVGNL-AKDlgLEVGElaarGARV-------VSKGNKQYFQLNPETGDLLLNEKLDREE 65
FAM47 pfam14642
FAM47 family; The function of this Chordate family of proteins is not known.
 1162-1225 4.53e-04

FAM47 family; The function of this Chordate family of proteins is not known.


Pssm-ID: 405345 [Multi-domain]  Cd Length: 257  Bit Score: 43.71  E-value: 4.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 270288729  1162 PPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASALCYSPPlaqAAAISHSSPLP 1225
Cdd:pfam14642  190 PPETRVSCLPPEPPKTPVSSLRPEPPETGVSHLRPQPPKTQVSSLHLEPP---ETGVSHLRPEP 250
FAM47 pfam14642
FAM47 family; The function of this Chordate family of proteins is not known.
 1138-1205 5.37e-04

FAM47 family; The function of this Chordate family of proteins is not known.


Pssm-ID: 405345 [Multi-domain]  Cd Length: 257  Bit Score: 43.33  E-value: 5.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270288729  1138 PPLSQASTQHHSPRVTQTIALCHSPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSPPSAQASA 1205
Cdd:pfam14642  190 PPETRVSCLPPEPPKTPVSSLRPEPPETGVSHLRPQPPKTQVSSLHLEPPETGVSHLRPEPPKTQVSS 257
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
 1134-1243 1.68e-03

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 41.46  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729 1134 LC----HSPPLSQASTQHHSPRVTQTIALCHSPPVTQTIALCHSPPPIQ---VSALHHspplvqaTAlhHSPPSAQASAL 1206
Cdd:cd21974    56 LCmtppYSPPFFEASHSPSVASLHPPSAASSQPPPEPESSEPPAASPQRaqaTSVIRH-------TA--DPVPVSPPPVL 126

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 270288729 1207 CYSPPLAQAAAISHSSPLPQVIALHRSQAQSSVSLQQ 1243
Cdd:cd21974   127 CQMLPVSSSSGVIVAFLKAPQQPSPQPQKPALPQPQV 163
CopL_fam NF033807
CopL family metal-binding regulatory protein; The founding member of this family was shown to ...
 1143-1228 3.32e-03

CopL family metal-binding regulatory protein; The founding member of this family was shown to be involved in the copper-responsive expression of a multicopper oxidase copA encoded downstream. The regulatory function likely involves copper-binding, but activity as a DNA-binding transcriptional regulator was not demonstrated directly.


Pssm-ID: 468190 [Multi-domain]  Cd Length: 129  Bit Score: 39.24  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729 1143 ASTQHHSPRVTQTIALCHSPPVTQTIALCH----SPPPIQVSALHHSPPL-------------VQATALHHSPPSAQASA 1205
Cdd:NF033807   21 ASVRMAMPHMAAAAAAAAAAAAAAAAAPCHgdapAAAAAAPPAADHDPHAddccksgscdcacAQHCSAALPTLPALPAH 100

                          90       100
                  ....*....|....*....|....
gi 270288729 1206 LCYSPPLAQAAAISHSSP-LPQVI 1228
Cdd:NF033807  101 LPGSLAVAAPLLSGHPSPaLPHLF 124
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 1136-1237 4.42e-03

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 39.08  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270288729 1136 HSPPLsqasTQHHSPRVTQTIA--LCHSPPVTQTIALCHSPPPIQVSALHHSPPLVQATALHHSP----------PSAQA 1203
Cdd:cd22541     4 HELPL----TPPAEPSFHQSLAysFELSPVKMLPTPAPAPAASAPPHPSPVSSPTQQPQQLPPNPaddipwwsiqQSNPA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 270288729 1204 SALCYSPPLAQAAAISHSS---PLPQVIALHRSQAQS 1237
Cdd:cd22541    80 HPPSTSTPLGHPTFAGYQPqiaALLQTKSPAASLSTT 116
 
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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