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Conserved domains on  [gi|2462528517|ref|XP_054226365|]
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neuron navigator 2 isoform X20 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 5-118 1.07e-75

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409134  Cd Length: 121  Bit Score: 246.80  E-value: 1.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    5 LWRWEQNNTTMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21285      1 GKSWEAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1919-2303 7.34e-09

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.94  E-value: 7.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1919 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1998
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1999 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 2070
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2071 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2138
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2139 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2196
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2197 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2273
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528517 2274 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2303
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 237-666 2.26e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.91  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  237 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 316
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  317 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 395
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  396 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 474
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  475 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 552
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  553 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 629
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528517  630 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 666
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1615-1691 6.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 6.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1691
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1834-1889 1.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528517 1834 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1889
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1615-1887 1.93e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1694
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1695 QAAINGVIN-TPELNCK---GNGTAQSADLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1763
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1764 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNSHSNSLISECMDSEA------------- 1829
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1830 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1887
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 894-1195 6.45e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  894 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 973
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  974 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1052
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1053 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1127
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528517 1128 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1195
Cdd:PHA03307   375 PSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPG 442
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 5-118 1.07e-75

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 246.80  E-value: 1.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    5 LWRWEQNNTTMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21285      1 GKSWEAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 20-118 1.01e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   20 TDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINgCPKNRSQMIENIDACLNFLAAK-GINIQGLSAE 98
Cdd:pfam00307    8 LRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLIEPE 86

                           90       100
                   ....*....|....*....|
gi 2462528517   99 EIRNGNLKAILGLFFSLSRY 118
Cdd:pfam00307   87 DLVEGDNKSVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-118 4.83e-11

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 61.56  E-value: 4.83e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    18 IYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINIQGLS 96
Cdd:smart00033    2 TLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 2462528517    97 AEEIRNGNlKAILGLFFSLSRY 118
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-116 5.25e-09

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 61.50  E-value: 5.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    1 MSVMLWRWEQNNTtmkliYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDA 80
Cdd:COG5069      1 MEAKKWQKVQKKT-----FTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462528517   81 CLNFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLS 116
Cdd:COG5069     75 RLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1919-2303 7.34e-09

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.94  E-value: 7.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1919 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1998
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1999 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 2070
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2071 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2138
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2139 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2196
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2197 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2273
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528517 2274 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2303
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 237-666 2.26e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.91  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  237 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 316
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  317 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 395
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  396 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 474
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  475 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 552
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  553 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 629
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528517  630 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 666
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
AAA_22 pfam13401
AAA domain;
2081-2168 2.81e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.80  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2081 IILSGPSGTGKTYLANRLSE----------YIVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVd 2147
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLLALAVAV- 86

                           90       100
                   ....*....|....*....|.
gi 2462528517 2148 mplVIILDNLHHVSslGEIFN 2168
Cdd:pfam13401   87 ---VLIIDEAQHLS--LEALE 102
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2078-2186 2.35e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 2.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  2078 HRRIILSGPSGTGKTYLANRLSEYIVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2151
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462528517  2152 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2186
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1615-1691 6.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 6.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1691
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1834-1889 1.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528517 1834 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1889
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1826-1884 1.62e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.86  E-value: 1.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528517 1826 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1884
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1615-1887 1.93e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1694
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1695 QAAINGVIN-TPELNCK---GNGTAQSADLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1763
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1764 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNSHSNSLISECMDSEA------------- 1829
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1830 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1887
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 894-1195 6.45e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  894 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 973
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  974 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1052
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1053 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1127
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528517 1128 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1195
Cdd:PHA03307   375 PSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPG 442
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2081-2161 6.84e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.44  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2081 IILSGPSGTGKTYLANRLSEYIVLREGR--ELTdgvIATFNVDHKSSKELRQYLSNLAdqcnSENNAVDMPLVIILDNLH 2158
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPflYLN---ASDLLEGLVVAELFGHFLVRLL----FELAEKAKPGVLFIDEID 94


                   ...
gi 2462528517 2159 HVS 2161
Cdd:cd00009     95 SLS 97
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 5-118 1.07e-75

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 246.80  E-value: 1.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    5 LWRWEQNNTTMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21285      1 GKSWEAENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 18-118 5.02e-62

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 207.19  E-value: 5.02e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   18 IYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGLSA 97
Cdd:cd21286      4 IYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 83

                           90       100
                   ....*....|....*....|.
gi 2462528517   98 EEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21286     84 EEIRNGNLKAILGLFFSLSRY 104
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 16-118 1.52e-56

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 191.64  E-value: 1.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21212      2 IEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGI 81

                           90       100
                   ....*....|....*....|...
gi 2462528517   96 SAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21212     82 TAEDIVDGNLKAILGLFFSLSRY 104
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 19-115 1.62e-26

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 105.84  E-value: 1.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   19 YTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGLSAE 98
Cdd:cd21213      5 YVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSAK 84

                           90
                   ....*....|....*..
gi 2462528517   99 EIRNGNLKAILGLFFSL 115
Cdd:cd21213     85 DIVDGNLKAIMRLILAL 101
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 6-115 1.34e-20

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 89.00  E-value: 1.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFL 85
Cdd:cd21215      1 WVDVQKKT-----FTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFI 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462528517   86 AAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21215     74 KSRGVKLTNIGAEDIVDGNLKLILGLLWTL 103
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 8-115 1.28e-18

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 83.21  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    8 WEQnntTMKLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcPKNRSQMIENIDACLNFLAA 87
Cdd:cd21214      2 WEK---QQRKTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIAS 75

                           90       100
                   ....*....|....*....|....*...
gi 2462528517   88 KGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21214     76 KGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 10-115 2.11e-17

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 80.02  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   10 QNNTtmkliYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKG 89
Cdd:cd21227      5 QKNT-----FTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDG 77

                           90       100
                   ....*....|....*....|....*.
gi 2462528517   90 INIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21227     78 IKLVNIGNEDIVNGNLKLILGLIWHL 103
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 19-117 4.40e-16

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 75.84  E-value: 4.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   19 YTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINI-QGLSA 97
Cdd:cd00014      4 LLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPElDLFEP 82

                           90       100
                   ....*....|....*....|.
gi 2462528517   98 EEI-RNGNLKAILGLFFSLSR 117
Cdd:cd00014     83 EDLyEKGNLKKVLGTLWALAL 103
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 6-115 6.81e-16

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 75.95  E-value: 6.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFL 85
Cdd:cd21311     12 WKRIQQNT-----FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFL 84

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   86 AA-KGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21311     85 EEdEGIKIVNIDSSDIVDGKLKLILGLIWTL 115
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 8-117 7.49e-15

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 72.56  E-value: 7.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    8 WEqnnTTMKLIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLA 86
Cdd:cd21225      1 WE---KVQIKAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFpKKFDLEPKNRIQMIQNLHLAMLFIE 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528517   87 AK-GINIQGLSAEEIRNGNLKAILGLFFSLSR 117
Cdd:cd21225     77 EDlKIRVQGIGAEDFVDNNKKLILGLLWTLYR 108
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 20-118 1.01e-14

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   20 TDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINgCPKNRSQMIENIDACLNFLAAK-GINIQGLSAE 98
Cdd:pfam00307    8 LRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLIEPE 86

                           90       100
                   ....*....|....*....|
gi 2462528517   99 EIRNGNLKAILGLFFSLSRY 118
Cdd:pfam00307   87 DLVEGDNKSVLTYLASLFRR 106
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 16-111 2.29e-14

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 71.56  E-value: 2.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GcpKNRSQMIENIDACLNFLAAKgINIQG 94
Cdd:cd21193     18 KKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNrG--RLRVQKIENVNKALAFLKTK-VRLEN 92

                           90
                   ....*....|....*..
gi 2462528517   95 LSAEEIRNGNLKAILGL 111
Cdd:cd21193     93 IGAEDIVDGNPRLILGL 109
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 6-115 5.85e-14

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 69.82  E-value: 5.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21228      1 WKKIQQNT-----FTRWCNEHL-KCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEF 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21228     74 LERESIKLVSIDSSAIVDGNLKLILGLIWTL 104
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 12-115 5.67e-13

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 67.04  E-value: 5.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   12 NTTMKLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCpkNRSQMIENIDACLNFLAAKGIN 91
Cdd:cd21188      1 DAVQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRKIK 76

                           90       100
                   ....*....|....*....|....
gi 2462528517   92 IQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21188     77 LVNIRAEDIVDGNPKLTLGLIWTI 100
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 6-115 1.72e-12

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 65.97  E-value: 1.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIE-DINGCPKNRSQMIENIDACLNF 84
Cdd:cd21183      1 WKRIQANT-----FTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKF 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21183     74 IEADHIKLVNIGSGDIVNGNIKLILGLIWTL 104
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 6-115 5.70e-12

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 65.05  E-value: 5.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21310     13 WKKIQQNT-----FTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEF 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21310     86 LDREHIKLVSIDSKAIVDGNLKLILGLIWTL 116
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 14-118 2.06e-11

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 62.97  E-value: 2.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   14 TMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQ 93
Cdd:cd21190      5 VQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLV 84

                           90       100
                   ....*....|....*....|....*
gi 2462528517   94 GLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21190     85 NINSTDIVDGKPSIVLGLIWTIILY 109
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 16-111 4.12e-11

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 62.00  E-value: 4.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GcpKNRSQMIENIDACLNFLAAKGINIQG 94
Cdd:cd21246     18 KKTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTkG--KMRIHCLENVDKALQFLKEQRVHLEN 93

                           90
                   ....*....|....*..
gi 2462528517   95 LSAEEIRNGNLKAILGL 111
Cdd:cd21246     94 MGSHDIVDGNHRLTLGL 110
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-118 4.83e-11

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 61.56  E-value: 4.83e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    18 IYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINIQGLS 96
Cdd:smart00033    2 TLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLFE 80

                            90       100
                    ....*....|....*....|..
gi 2462528517    97 AEEIRNGNlKAILGLFFSLSRY 118
Cdd:smart00033   81 PEDLVEGP-KLILGVIWTLISL 101
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 6-115 1.26e-10

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 61.26  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21308     17 WKKIQQNT-----FTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEF 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21308     90 LDRESIKLVSIDSKAIVDGNLKLILGLIWTL 120
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 6-115 2.97e-10

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 60.09  E-value: 2.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    6 WRWEQNNTtmkliYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNF 84
Cdd:cd21309     14 WKKIQQNT-----FTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEF 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   85 LAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21309     87 LDRESIKLVSIDSKAIVDGNLKLILGLVWTL 117
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 16-118 4.18e-10

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 59.31  E-value: 4.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21241      7 KKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKLVNI 86

                           90       100
                   ....*....|....*....|...
gi 2462528517   96 SAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21241     87 NPTDIVDGKPSIVLGLIWTIILY 109
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 9-115 1.10e-09

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 58.88  E-value: 1.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIedingcPK-NRSQM----IENIDACLN 83
Cdd:cd21318     33 DEREAVQKKTFTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLLEVLSGEQL------PKpTRGRMrihsLENVDKALQ 104

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528517   84 FLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21318    105 FLKEQRVHLENVGSHDIVDGNHRLTLGLIWTI 136
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
1-116 5.25e-09

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 61.50  E-value: 5.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    1 MSVMLWRWEQNNTtmkliYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDA 80
Cdd:COG5069      1 MEAKKWQKVQKKT-----FTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSG 74

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462528517   81 CLNFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLS 116
Cdd:COG5069     75 RLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1919-2303 7.34e-09

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.94  E-value: 7.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1919 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1998
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1999 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 2070
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2071 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2138
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2139 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2196
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2197 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2273
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528517 2274 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2303
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 9-115 3.03e-08

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 54.67  E-value: 3.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIedingcPKN-----RSQMIENIDACLN 83
Cdd:cd21317     26 DEREAVQKKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQL------PKPtkgrmRIHCLENVDKALQ 97

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528517   84 FLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21317     98 FLKEQKVHLENMGSHDIVDGNHRLTLGLIWTI 129
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 14-118 4.83e-08

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409070  Cd Length: 106  Bit Score: 53.05  E-value: 4.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   14 TMKLIYTDWANHYLAKsghKRLI-KDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQM--IENIDACLNFLAAKGI 90
Cdd:cd21221      1 ELVRVLTEWINEELAD---DRIVvRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKqkLAVVLACVNFLLGLEE 77

                           90       100
                   ....*....|....*....|....*...
gi 2462528517   91 NIQGLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21221     78 DEARWTVDGIYNKDLVSILHLLVALAHH 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 19-111 9.06e-08

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 52.58  E-value: 9.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   19 YTDWANHYLAKSGH--KRLIKDLQQD-----VTDGVLLAQIIQVVANEKIED--INGC-PKNRSQMIENIDACLNflAAK 88
Cdd:cd21217      6 FVEHINSLLADDPDlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVPGTIDErkLNKKkPKNIFEATENLNLALN--AAK 83

                           90       100
                   ....*....|....*....|....*
gi 2462528517   89 --GINIQGLSAEEIRNGNLKAILGL 111
Cdd:cd21217     84 kiGCKVVNIGPQDILDGNPHLVLGL 108
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 9-115 1.08e-07

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 53.51  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGcpKNRSQMIENIDACLNFLAA 87
Cdd:cd21316     48 DEREAVQKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRIHCLENVDKALQFLKE 123

                           90       100
                   ....*....|....*....|....*...
gi 2462528517   88 KGINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21316    124 QRVHLENMGSHDIVDGNHRLTLGLIWTI 151
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 9-115 1.41e-07

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 51.76  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTtMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAK 88
Cdd:cd21242      1 EQEQT-QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNK 77

                           90       100
                   ....*....|....*....|....*..
gi 2462528517   89 GINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21242     78 SIKLINIHVPDIIEGKPSIILGLIWTI 104
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 16-115 1.49e-07

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 51.61  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKrLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21186      4 KKTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVNI 80

                           90       100
                   ....*....|....*....|
gi 2462528517   96 SAEEIRNGNLKAILGLFFSL 115
Cdd:cd21186     81 SSNDIVDGNPKLTLGLVWSI 100
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 16-115 3.82e-07

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 50.66  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21191      7 KRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVSI 86

                           90       100
                   ....*....|....*....|
gi 2462528517   96 SAEEIRNGNLKAILGLFFSL 115
Cdd:cd21191     87 DAAEIADGNPSLVLGLIWNI 106
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 9-115 1.00e-06

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 49.64  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAK 88
Cdd:cd21235      1 DERDRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 76

                           90       100
                   ....*....|....*....|....*..
gi 2462528517   89 GINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21235     77 QVKLVNIRNDDIADGNPKLTLGLIWTI 103
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 9-115 1.11e-06

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 49.65  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAK 88
Cdd:cd21237      1 DERDRVQKKTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG--RMRFHRLQNVQIALDFLKQR 76

                           90       100
                   ....*....|....*....|....*..
gi 2462528517   89 GINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21237     77 QVKLVNIRNDDITDGNPKLTLGLIWTI 103
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 16-115 1.91e-06

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 48.77  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21231      8 KKTFTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKG--STRVHALNNVNKALQVLQKNNVDLVNI 84

                           90       100
                   ....*....|....*....|
gi 2462528517   96 SAEEIRNGNLKAILGLFFSL 115
Cdd:cd21231     85 GSADIVDGNHKLTLGLIWSI 104
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 9-111 2.20e-06

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 48.99  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEdingcPKNRSQM----IENIDACLNF 84
Cdd:cd21247     15 EQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLP-----RPSRGKMrvhfLENNSKAITF 89

                           90       100
                   ....*....|....*....|....*..
gi 2462528517   85 LAAKgINIQGLSAEEIRNGNLKAILGL 111
Cdd:cd21247     90 LKTK-VPVKLIGPENIVDGDRTLILGL 115
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 22-118 4.31e-06

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 47.66  E-value: 4.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   22 WANHYlaksGHKRLIKDLQQDVTDGVLLAQIIqvvanEKIEdiNGC----------PKNRSQMIEN----IDACLNFlaa 87
Cdd:cd21219     12 WLNSL----GLDPLINNLYEDLRDGLVLLQVL-----DKIQ--PGCvnwkkvnkpkPLNKFKKVENcnyaVDLAKKL--- 77

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   88 kGINIQGLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21219     78 -GFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 9-115 7.13e-06

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 47.67  E-value: 7.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517    9 EQNNTTMKLIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAK 88
Cdd:cd21236     12 DERDKVQKKTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHRLQNVQIALDYLKRR 87

                           90       100
                   ....*....|....*....|....*..
gi 2462528517   89 GINIQGLSAEEIRNGNLKAILGLFFSL 115
Cdd:cd21236     88 QVKLVNIRNDDITDGNPKLTLGLIWTI 114
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 237-666 2.26e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.91  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  237 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 316
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  317 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 395
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  396 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 474
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  475 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 552
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  553 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 629
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528517  630 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 666
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
AAA_22 pfam13401
AAA domain;
2081-2168 2.81e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.80  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2081 IILSGPSGTGKTYLANRLSE----------YIVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVd 2147
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLLALAVAV- 86

                           90       100
                   ....*....|....*....|.
gi 2462528517 2148 mplVIILDNLHHVSslGEIFN 2168
Cdd:pfam13401   87 ---VLIIDEAQHLS--LEALE 102
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2078-2186 2.35e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 2.35e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  2078 HRRIILSGPSGTGKTYLANRLSEYIVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2151
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462528517  2152 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2186
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 23-118 4.13e-04

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 42.19  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   23 ANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANEKI--EDINGCPKNRSQMIENIDACLNFLAAKGINIQGLSAEEI 100
Cdd:cd21222     25 VNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPEDI 102

                           90
                   ....*....|....*....
gi 2462528517  101 RNGNLKAILGLFFSL-SRY 118
Cdd:cd21222    103 VNGDLKSILRVLYSLfSKY 121
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1615-1691 6.03e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 6.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1691
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 21-118 7.81e-04

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409153  Cd Length: 107  Bit Score: 41.14  E-value: 7.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   21 DWANHYLAksGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIE-------DINGCPKNRsQMIENIDACLNFlaaKGINIQ 93
Cdd:cd21304      8 EWINDELA--EQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEvaevtqsEVGQKQKLR-TVLDKINRILNL---PRWSQQ 81

                           90       100
                   ....*....|....*....|....*
gi 2462528517   94 GLSAEEIRNGNLKAILGLFFSLSRY 118
Cdd:cd21304     82 KWSVDSIHSKNLVAILHLLVALARH 106
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 16-115 8.36e-04

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 41.15  E-value: 8.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQGL 95
Cdd:cd21232      4 KKTFTKWINARFSKSG-KPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERG--STRVHALNNVNRVLQVLHQNNVELVNI 80

                           90       100
                   ....*....|....*....|
gi 2462528517   96 SAEEIRNGNLKAILGLFFSL 115
Cdd:cd21232     81 GGTDIVDGNHKLTLGLLWSI 100
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 16-117 1.29e-03

first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409141  Cd Length: 145  Bit Score: 41.50  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   16 KLIYTDWANHYLAKSGH-KRLI------KDLQQDVTDGVLLAQIIQVVANEKIED--INGCPKNRSQMIENIDACLNFLA 86
Cdd:cd21292     26 KVAFVNWINKNLGDDPDcKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDEraINKKKLTVFTIHENLTLALNSAS 105

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2462528517   87 AKGINIQGLSAEEIRNGNLKAILGLFFSLSR 117
Cdd:cd21292    106 AIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1834-1889 1.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528517 1834 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1889
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1826-1884 1.62e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 39.86  E-value: 1.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528517 1826 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1884
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
AAA_18 pfam13238
AAA domain;
2081-2158 1.77e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.49  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2081 IILSGPSGTGKTYLANRLSEyiVLREGRELTD-----GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILD 2155
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSK--RLGFGDNVRDlalenGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLIID 78


                   ...
gi 2462528517 2156 NLH 2158
Cdd:pfam13238   79 GHL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1615-1887 1.93e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1615 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1694
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1695 QAAINGVIN-TPELNCK---GNGTAQSADLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1763
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1764 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNSHSNSLISECMDSEA------------- 1829
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1830 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1887
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 36-115 2.38e-03

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 39.88  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   36 IKDLQQDVTDGVLLAQIIQVVANekieDINGCPK------NRSQMIENIDACLNFLAAKGI----NIQGLSAEEIRNGNL 105
Cdd:cd21223     26 VTNLAVDLRDGVRLCRLVELLTG----DWSLLSKlrvpaiSRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHR 101

                           90
                   ....*....|
gi 2462528517  106 KAILGLFFSL 115
Cdd:cd21223    102 EKTLALLWRI 111
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 22-109 3.42e-03

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 39.59  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   22 WANHYLAKSGHKRL-IKDLQQDVTDGVLLAQII-QVVANEKIEDINGCPKNRSQMIENIDACLNflAAKGINI-QGLSAE 98
Cdd:cd21218     18 WVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLhSLAPELCDKELVLEVLSEEDLEKRAEKVLQ--AAEKLGCkYFLTPE 95

                           90
                   ....*....|.
gi 2462528517   99 EIRNGNLKAIL 109
Cdd:cd21218     96 DIVSGNPRLNL 106
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 894-1195 6.45e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  894 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 973
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517  974 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1052
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 1053 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1127
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528517 1128 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1195
Cdd:PHA03307   375 PSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPG 442
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 36-118 6.60e-03

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 38.87  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517   36 IKDLQQDVTDGVLLAQIIQVVANEKIE--DINGCPKNRSQMIENIDACLNFLAAKGINIQGLSAEEIRNGNLKAILGLFF 113
Cdd:cd21307     36 VKDLDSQFADGVILLLLIGQLEGFFIHlsEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLY 115


                   ....*.
gi 2462528517  114 SL-SRY 118
Cdd:cd21307    116 CLfSKY 121
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2081-2161 6.84e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.44  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528517 2081 IILSGPSGTGKTYLANRLSEYIVLREGR--ELTdgvIATFNVDHKSSKELRQYLSNLAdqcnSENNAVDMPLVIILDNLH 2158
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPflYLN---ASDLLEGLVVAELFGHFLVRLL----FELAEKAKPGVLFIDEID 94


                   ...
gi 2462528517 2159 HVS 2161
Cdd:cd00009     95 SLS 97
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1618-1690 7.01e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 7.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528517 1618 QSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQ 1690
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 15-52 9.89e-03

second calponin homology (CH) domain found in the family of plastin; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409144  Cd Length: 113  Bit Score: 38.02  E-value: 9.89e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462528517   15 MKL----IYTDWANHYLAKSGHKRLIKDLQQDVTDGV----LLAQI 52
Cdd:cd21295      9 LKLspeeILLRWVNYHLERAGCDRRIKNFSGDIKDSEaythLLKQI 54
 
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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