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Conserved domains on  [gi|568948734|ref|XP_006541365|]
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neuron navigator 2 isoform X21 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 18-80 1.56e-39

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).


The actual alignment was detected with superfamily member cd21285:

Pssm-ID: 469584  Cd Length: 121  Bit Score: 143.57  E-value: 1.56e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 80
Cdd:cd21285    53 ANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1996-2233 5.63e-08

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: 57.86  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1996 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2070
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2071 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2121
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2122 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2198
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568948734 2199 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2233
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1547-1623 2.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568948734 1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1623
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1766-1821 7.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568948734 1766 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1821
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 225-619 7.96e-04

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: 44.91  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   225 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 303
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   304 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 383
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   384 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 462
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   463 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 526
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   527 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 606
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 568948734   607 NVTAESSSAGVSM 619
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1547-1819 3.14e-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: 42.70  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1626
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1627 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1695
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1696 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1761
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1762 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1819
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 867-1218 7.59e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  867 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 946
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  947 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1025
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1026 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1104
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1105 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1178
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568948734 1179 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1218
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 18-80 1.56e-39

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: 143.57  E-value: 1.56e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 80
Cdd:cd21285    53 ANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1996-2233 5.63e-08

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1996 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2070
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2071 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2121
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2122 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2198
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568948734 2199 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2233
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
AAA_22 pfam13401
AAA domain;
2007-2100 2.08e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  2007 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2072
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80

                           90       100
                   ....*....|....*....|....*...
gi 568948734  2073 SENNAVdmplVIILDNLHHVSslGEIFN 2100
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1547-1623 2.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568948734 1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1623
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2010-2118 5.43e-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: 42.75  E-value: 5.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   2010 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2083
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568948734   2084 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2118
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1766-1821 7.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568948734 1766 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1821
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 225-619 7.96e-04

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: 44.91  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   225 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 303
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   304 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 383
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   384 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 462
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   463 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 526
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   527 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 606
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 568948734   607 NVTAESSSAGVSM 619
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1758-1816 9.29e-04

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: 40.24  E-value: 9.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568948734 1758 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1816
Cdd:cd22887     7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 29-79 9.60e-04

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: 40.73  E-value: 9.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568948734    29 PKNRSQMIENIDACLNFLAAK-GINTQGLSAEEIRNGNLKAILGLFFSLSRY 79
Cdd:pfam00307   55 NKSEFDKLENINLALDVAEKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRR 106
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1547-1819 3.14e-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: 42.70  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1626
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1627 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1695
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1696 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1761
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1762 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1819
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 867-1218 7.59e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  867 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 946
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  947 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1025
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1026 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1104
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1105 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1178
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568948734 1179 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1218
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
PHA03247 PHA03247
large tegument protein UL36; Provisional
 176-623 8.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  176 PGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPgmseNVPAPLENSPS 255
Cdd:PHA03247 2571 PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA----NEPDPHPPPTV 2646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  256 VPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP-------------AGPEAPRPTPEamkPAPNNQKSMLEkl 322
Cdd:PHA03247 2647 PPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsltslADPPPPPPTPE---PAPHALVSATP-- 2720

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  323 klfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKG 402
Cdd:PHA03247 2721 ----LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  403 NEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVTEMPKKSSKIASFIPKGGKL----------- 471
Cdd:PHA03247 2797 SLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrpp 2867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  472 -NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLPPQKAQLDSRHSSSSSSLASSEGKGPGGTSL 550
Cdd:PHA03247 2868 sRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTT 2947

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734  551 NPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRSQTDTEGNVTAESSSAGVSMEPSH 623
Cdd:PHA03247 2948 DPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDP 3019
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 922-1210 9.42e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   922 KMEPGSKWRRNPSDMSDESDKSVSGKKN---------PVLSQTGSW--------------RRGMTAEVGITMPRTKPSAP 978
Cdd:pfam17823   32 KMWNGAGKQNASGDAVPRADNKSSEQ*NfcaataapaPVTLTKGTSaahlnstevtaehtPHGTDLSEPATREGAADGAA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   979 TGTLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTVNANSFGFKKQSGSAAGLAMITA 1058
Cdd:pfam17823  112 SRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1059 SGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSN 1138
Cdd:pfam17823  192 SSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN 271

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568948734  1139 MSSKSAGLPVPKLREPSKASLGSSLPGLVNQTdkekgisSDSESVASCNSVKVNPATQPVSSSAQATLQPGT 1210
Cdd:pfam17823  272 MGDPHARRLSPAKHMPSDTMARNPAAPMGAQA-------QGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNT 336
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 18-80 1.56e-39

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: 143.57  E-value: 1.56e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 80
Cdd:cd21285    53 ANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 18-80 1.07e-33

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: 126.30  E-value: 1.07e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 80
Cdd:cd21286    43 ANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 105
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 18-80 6.27e-30

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: 115.37  E-value: 6.27e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 80
Cdd:cd21212    43 AGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 18-80 1.37e-10

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: 60.39  E-value: 1.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL-SRYK 80
Cdd:cd21213    43 AGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALaAHFK 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 29-76 2.25e-08

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: 53.94  E-value: 2.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568948734   29 PKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21215    56 PKMRVQKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTL 103
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1996-2233 5.63e-08

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1996 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2070
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2071 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2121
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2122 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2198
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 568948734 2199 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2233
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 29-76 8.01e-08

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: 52.39  E-value: 8.01e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568948734   29 PKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21214    56 GKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 6-76 8.31e-08

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: 52.29  E-value: 8.31e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568948734    6 GTKLLLCVSAGSANdKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21227    34 GVKLIALVEILQGR-KLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHL 103
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 29-78 5.05e-06

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: 47.53  E-value: 5.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568948734   29 PKNRSQMIENIDACLNFLAAK-GINTQGLSAEEIRNGNLKAILGLFFSLSR 78
Cdd:cd21225    58 PKNRIQMIQNLHLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 18-78 1.17e-05

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: 46.18  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734   18 ANDKIEDINGCPKNRSQMIENIDACLNFLAAKGI-NTQGLSAEEI-RNGNLKAILGLFFSLSR 78
Cdd:cd00014    41 SPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
AAA_22 pfam13401
AAA domain;
2007-2100 2.08e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  2007 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2072
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80

                           90       100
                   ....*....|....*....|....*...
gi 568948734  2073 SENNAVdmplVIILDNLHHVSslGEIFN 2100
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 29-76 3.49e-05

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: 44.78  E-value: 3.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568948734   29 PKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21183    57 PAFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTL 104
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 29-79 4.69e-05

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: 44.89  E-value: 4.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568948734   29 PKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL-SRY 79
Cdd:cd21222    70 PSTDDEKLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLfSKY 121
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 6-76 8.17e-05

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: 44.02  E-value: 8.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568948734    6 GTKLLLCVSAGSANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21228    34 GLRLIALLEVLSQKRMYKKYNKRPTFRQMKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTL 104
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 4-76 1.23e-04

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: 43.98  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568948734    4 SLGTKLLLCVSAGSANdKIEDINGCPKNRSQMIENIDACLNFLAA-KGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21311    43 SDGLRLIALVEVLSGK-KFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTL 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1547-1623 2.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568948734 1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1623
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2010-2118 5.43e-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: 42.75  E-value: 5.43e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   2010 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2083
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 568948734   2084 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2118
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 32-72 5.48e-04

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: 41.90  E-value: 5.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568948734   32 RSQMIENIDACLNFLAAKgINTQGLSAEEIRNGNLKAILGL 72
Cdd:cd21193    70 RVQKIENVNKALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1766-1821 7.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568948734 1766 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1821
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 225-619 7.96e-04

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: 44.91  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   225 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 303
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   304 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 383
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   384 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 462
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   463 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 526
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   527 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 606
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 568948734   607 NVTAESSSAGVSM 619
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1758-1816 9.29e-04

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: 40.24  E-value: 9.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568948734 1758 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1816
Cdd:cd22887     7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 29-79 9.60e-04

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: 40.73  E-value: 9.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568948734    29 PKNRSQMIENIDACLNFLAAK-GINTQGLSAEEIRNGNLKAILGLFFSLSRY 79
Cdd:pfam00307   55 NKSEFDKLENINLALDVAEKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 30-76 1.00e-03

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: 40.85  E-value: 1.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568948734   30 KNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 76
Cdd:cd21188    54 RMRFHRLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTI 100
AAA_18 pfam13238
AAA domain;
2013-2090 1.72e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.49  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  2013 IILSGPSGTGKTYLANRLSEyvVLREGRELTD-----GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILD 2087
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSK--RLGFGDNVRDlalenGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLIID 78


                   ...
gi 568948734  2088 NLH 2090
Cdd:pfam13238   79 GHL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1547-1819 3.14e-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: 42.70  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1547 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1626
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1627 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1695
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1696 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1761
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1762 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1819
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
AAA_28 pfam13521
AAA domain;
2012-2044 5.71e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 5.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 568948734  2012 RIILSGPSGTGKTYLANRLSE---YVVLRE-GRELTD 2044
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAArfgYPVVPEaAREILE 37
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 2007-2093 5.92e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.93  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 2007 LTEHRRII-LSGPSGTGKTYLANRL-----SEYVVLR------EGRELTDGVIATFNVDHKSS------KELRQYLSNLA 2068
Cdd:COG3267    39 LAQGGGFVvLTGEVGTGKTTLLRRLlerlpDDVKVAYipnpqlSPAELLRAIADELGLEPKGAskadllRQLQEFLLELA 118

                          90       100
                  ....*....|....*....|....*
gi 568948734 2069 DQcnsennavDMPLVIILDNLHHVS 2093
Cdd:COG3267   119 AA--------GRRVVLIIDEAQNLP 135
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1550-1622 6.07e-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: 6.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734 1550 QSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQ 1622
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 867-1218 7.59e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  867 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 946
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  947 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1025
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1026 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1104
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1105 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1178
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 568948734 1179 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1218
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
PHA03247 PHA03247
large tegument protein UL36; Provisional
 176-623 8.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  176 PGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPgmseNVPAPLENSPS 255
Cdd:PHA03247 2571 PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAA----NEPDPHPPPTV 2646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  256 VPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP-------------AGPEAPRPTPEamkPAPNNQKSMLEkl 322
Cdd:PHA03247 2647 PPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsltslADPPPPPPTPE---PAPHALVSATP-- 2720

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  323 klfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGPASSSPKIALKGIAQRTFSRALTNKKSSPKG 402
Cdd:PHA03247 2721 ----LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  403 NEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVTEMPKKSSKIASFIPKGGKL----------- 471
Cdd:PHA03247 2797 SLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrpp 2867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  472 -NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLPPQKAQLDSRHSSSSSSLASSEGKGPGGTSL 550
Cdd:PHA03247 2868 sRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTT 2947

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568948734  551 NPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRSQTDTEGNVTAESSSAGVSMEPSH 623
Cdd:PHA03247 2948 DPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDP 3019
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 911-1165 9.29e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  911 KKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSGK----KNPVLSQTGSWRRGMTAEVGITMPRTKPSAPTGTLKT-P 985
Cdd:PHA03307  190 PAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRsaadDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTrI 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  986 GTGKTDDAKVSEKGRLSPkasqvkrSPSDAGRSSgdeskKTLPSSSRTPTVNANSFGFKKQSGSA-AGLAMITASGATVT 1064
Cdd:PHA03307  270 WEASGWNGPSSRPGPASS-------SSSPRERSP-----SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSR 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734 1065 SRSATLGKIPKSSALVGRP----TGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMS 1140
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPpppaDPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPL 417

                         250       260
                  ....*....|....*....|....*
gi 568948734 1141 SKSAGLPVPKLREPSKASLGSSLPG 1165
Cdd:PHA03307  418 DAGAASGAFYARYPLLTPSGEPWPG 442
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 922-1210 9.42e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   922 KMEPGSKWRRNPSDMSDESDKSVSGKKN---------PVLSQTGSW--------------RRGMTAEVGITMPRTKPSAP 978
Cdd:pfam17823   32 KMWNGAGKQNASGDAVPRADNKSSEQ*NfcaataapaPVTLTKGTSaahlnstevtaehtPHGTDLSEPATREGAADGAA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734   979 TGTLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTVNANSFGFKKQSGSAAGLAMITA 1058
Cdd:pfam17823  112 SRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948734  1059 SGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSN 1138
Cdd:pfam17823  192 SSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN 271

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568948734  1139 MSSKSAGLPVPKLREPSKASLGSSLPGLVNQTdkekgisSDSESVASCNSVKVNPATQPVSSSAQATLQPGT 1210
Cdd:pfam17823  272 MGDPHARRLSPAKHMPSDTMARNPAAPMGAQA-------QGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNT 336
 
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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