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Conserved domains on  [gi|2462528555|ref|XP_054226384|]
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neuron navigator 2 isoform X36 [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 ...
 15-126 1.14e-72

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: 238.32  E-value: 1.14e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   15 PVIHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285      1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528555   93 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1831-2215 7.05e-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: 7.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1831 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1910
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1911 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 1982
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1983 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2050
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2051 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2108
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2109 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2185
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528555 2186 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2215
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
143-330 2.91e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.46  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  143 PPAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTARVSAAGSEAKTRGGSTTANNRRS 222
Cdd:PRK07003   373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAK 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  223 QsfnnydkSKPVTSPPPPPSSHEKEPLASSASSHPGMSDNAPASLESGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSVK 302
Cdd:PRK07003   453 A-------NARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAA 525

                          170       180
                   ....*....|....*....|....*...
gi 2462528555  303 hsatvsmlsvKPPGPEAPRPTPEAMKPA 330
Cdd:PRK07003   526 ----------APPAPEARPPTPAAAAPA 543
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 222-651 3.23e-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: 49.53  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  222 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 301
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  302 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 380
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  381 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 459
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  460 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 537
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  538 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 614
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528555  615 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 651
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1530-1606 8.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 8.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528555 1530 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1606
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
Atg16_CCD super family cl46300
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1738-1796 1.75e-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.


The actual alignment was detected with superfamily member cd22887:

Pssm-ID: 480640 [Multi-domain]  Cd Length: 91  Bit Score: 39.47  E-value: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555 1738 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1796
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 879-1180 6.63e-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: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  879 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 958
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  959 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1037
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1038 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1112
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528555 1113 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1180
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 ...
 15-126 1.14e-72

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: 238.32  E-value: 1.14e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   15 PVIHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285      1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528555   93 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 21-126 5.11e-16

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: 75.79  E-value: 5.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINgCPKNRSQMIENIDACLNFLAAK-GIN 99
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100
                   ....*....|....*....|....*..
gi 2462528555  100 IQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 25-126 2.22e-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: 62.33  E-value: 2.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555    25 RIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINIQGL 103
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 2462528555   104 SAEEIRNGNlKAILGLFFSLSRY 126
Cdd:smart00033   80 EPEDLVEGP-KLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-124 1.19e-09

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 63.42  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:COG5069     10 QKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                           90       100
                   ....*....|....*....|..
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSLS 124
Cdd:COG5069     89 IGPQDIVDGNPKLILGLIWSLI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1831-2215 7.05e-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: 7.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1831 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1910
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1911 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 1982
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1983 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2050
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2051 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2108
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2109 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2185
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528555 2186 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2215
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
AAA_22 pfam13401
AAA domain;
1993-2080 2.71e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.80  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1993 IILSGPSGTGKTYLANRLSE----------YIVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVd 2059
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLLALAVAV- 86

                           90       100
                   ....*....|....*....|.
gi 2462528555 2060 mplVIILDNLHHVSslGEIFN 2080
Cdd:pfam13401   87 ---VLIIDEAQHLS--LEALE 102
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
143-330 2.91e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.46  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  143 PPAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTARVSAAGSEAKTRGGSTTANNRRS 222
Cdd:PRK07003   373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAK 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  223 QsfnnydkSKPVTSPPPPPSSHEKEPLASSASSHPGMSDNAPASLESGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSVK 302
Cdd:PRK07003   453 A-------NARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAA 525

                          170       180
                   ....*....|....*....|....*...
gi 2462528555  303 hsatvsmlsvKPPGPEAPRPTPEAMKPA 330
Cdd:PRK07003   526 ----------APPAPEARPPTPAAAAPA 543
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 222-651 3.23e-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: 49.53  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  222 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 301
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  302 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 380
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  381 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 459
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  460 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 537
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  538 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 614
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528555  615 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 651
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
PHA03247 PHA03247
large tegument protein UL36; Provisional
 141-638 5.84e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  141 PLPPAvsqvagAPSqcqaGTPQQQVPvtpqapcqPHQPAPhqqskaqaemqsRLPGP--TARVSAAGSEAKTRGGSTTAN 218
Cdd:PHA03247  2554 PLPPA------APP----AAPDRSVP--------PPRPAP------------RPSEPavTSRARRPDAPPQSARPRAPVD 2603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  219 NRRSQSFNNYDKSKPVTSPPPPPSSHEKEPLASS-------ASSHPGMSDNAPAsleSGSSSTPTNCSTSSAIPQPGAAT 291
Cdd:PHA03247  2604 DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEpdphpppTVPPPERPRDDPA---PGRVSRPRRARRLGRAAQASSPP 2680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  292 KPWRSKSLSVKhSATVSMLSVKPPGPEAPRPTPEAMKPApnnqksmlekLKLFNSKGGSKAGEGPGSRDTSCERLETLPS 371
Cdd:PHA03247  2681 QRPRRRAARPT-VGSLTSLADPPPPPPTPEPAPHALVSA----------TPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  372 feESEELEAASRMLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSlkgnekEKEKQQREKDKEKSKDLAKRASVTERLD 451
Cdd:PHA03247  2750 --TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE------SRESLPSPWDPADPPAAVLAPAAALPPA 2821

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  452 LKEEPKEDPSGAAVPEMPKKSSK-IASFIPKGGKL------------NSAKKEPMAPSH---------------SGIPKP 503
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARppvrrlarpavsrstESFALP 2901

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  504 GMKSMPGKSPSAPAPSKEGERSRSGKLSSGLPQQKPQLDGRHSSSSSSLASSEGKGPGGTTLNHSIssqtVSGSVGTTQT 583
Cdd:PHA03247  2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL----VPGRVAVPRF 2977

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555  584 -TGSNTVSVQLPQPQqqyNHPNTATVAPflyrsqtdtegNVTAESSSTGVSVEPSH 638
Cdd:PHA03247  2978 rVPQPAPSREAPASS---TPPLTGHSLS-----------RVSSWASSLALHEETDP 3019
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1990-2098 2.26e-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: 2.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  1990 HRRIILSGPSGTGKTYLANRLSEYIVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2063
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462528555  2064 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2098
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1530-1606 8.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 8.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528555 1530 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1606
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1738-1796 1.75e-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: 39.47  E-value: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555 1738 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1796
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1746-1801 2.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555 1746 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1801
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 138-480 2.27e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  138 LSSPLPPAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTAR---VSAAGSEAKTRGGS 214
Cdd:pfam03154  334 LQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALkplSSLSTHHPPSAHPP 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  215 TTANNRRSQSFNNYDKSKPVTSPPP----PPSSHekePLASSASSHPGMSDNAPASLESGSSS--TPTNC---STSSAIP 285
Cdd:pfam03154  414 PLQLMPQSQQLPPPPAQPPVLTQSQslppPAASH---PPTSGLHQVPSQSPFPQHPFVPGGPPpiTPPSGpptSTSSAMP 490

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  286 --QPGAATKPWRSKSLSVKHSATVSMLSVK------PPGPEAPRPTPEAMKPAPN-----NQKSMLEKLKLFNSKGGSka 352
Cdd:pfam03154  491 giQPPSSASVSSSGPVPAAVSCPLPPVQIKeealdeAEEPESPPPPPRSPSPEPTvvntpSHASQSARFYKHLDRGYN-- 568

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  353 gegpgsrdtSCERLETLpsfeeseeleaasrmlttVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQ-QRE 431
Cdd:pfam03154  569 ---------SCARTDLY------------------FMPLAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKErERE 621

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2462528555  432 KDKEKSKDLAKRASVTERLDLKEEPKEDPSGAAVPEMPKKSSKIASFIP 480
Cdd:pfam03154  622 REREREAERAAKASSSSHEGRMGDPQLAGPAHMRPSFEPPPTTIAAVPP 670
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1993-2073 6.59e-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: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1993 IILSGPSGTGKTYLANRLSEYIVLREGR--ELTdgvIATFNVDHKSSKELRQYLSNLAdqcnSENNAVDMPLVIILDNLH 2070
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPflYLN---ASDLLEGLVVAELFGHFLVRLL----FELAEKAKPGVLFIDEID 94


                   ...
gi 2462528555 2071 HVS 2073
Cdd:cd00009     95 SLS 97
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 879-1180 6.63e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  879 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 958
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  959 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1037
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1038 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1112
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528555 1113 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1180
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 ...
 15-126 1.14e-72

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: 238.32  E-value: 1.14e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   15 PVIHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285      1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528555   93 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21285     81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRY 114
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 25-126 2.45e-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: 207.96  E-value: 2.45e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   25 RIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQGLS 104
Cdd:cd21286      3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                           90       100
                   ....*....|....*....|..
gi 2462528555  105 AEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21286     83 AEEIRNGNLKAILGLFFSLSRY 104
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 23-126 6.72e-57

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: 192.41  E-value: 6.72e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21212      1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                           90       100
                   ....*....|....*....|....
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21212     81 ITAEDIVDGNLKAILGLFFSLSRY 104
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 23-123 9.99e-27

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: 106.23  E-value: 9.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21213      1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21213     81 TSAKDIVDGNLKAIMRLILAL 101
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 23-123 2.95e-21

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: 90.54  E-value: 2.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21215      5 QKKTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTN 82

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21215     83 IGAEDIVDGNLKLILGLLWTL 103
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 23-123 3.54e-20

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: 87.44  E-value: 3.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21214      6 QRKTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIASKGVKLVS 82

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21214     83 IGAEEIVDGNLKMTLGMIWTI 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 21-123 1.25e-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: 80.41  E-value: 1.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINI 100
Cdd:cd21227      3 EIQKNTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                           90       100
                   ....*....|....*....|...
gi 2462528555  101 QGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21227     81 VNIGNEDIVNGNLKLILGLIWHL 103
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 24-125 1.34e-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: 77.38  E-value: 1.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   24 KRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINI-QG 102
Cdd:cd00014      1 EEELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPElDL 79

                           90       100
                   ....*....|....*....|....
gi 2462528555  103 LSAEEI-RNGNLKAILGLFFSLSR 125
Cdd:cd00014     80 FEPEDLyEKGNLKKVLGTLWALAL 103
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 14-119 2.23e-16

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: 76.95  E-value: 2.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   14 KPVIHGLED-----QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GcpKNRSQMIENID 87
Cdd:cd21193      3 KGRIRALQEeriniQKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNrG--RLRVQKIENVN 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528555   88 ACLNFLAAKgINIQGLSAEEIRNGNLKAILGL 119
Cdd:cd21193     79 KALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 21-126 5.11e-16

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: 75.79  E-value: 5.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINgCPKNRSQMIENIDACLNFLAAK-GIN 99
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100
                   ....*....|....*....|....*..
gi 2462528555  100 IQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 23-123 7.89e-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: 7.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAA-KGINIQ 101
Cdd:cd21311     16 QQNTFTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIV 93

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21311     94 NIDSSDIVDGKLKLILGLIWTL 115
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 23-125 2.04e-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: 74.10  E-value: 2.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLAAK-GINI 100
Cdd:cd21225      5 QIKAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFpKKFDLEPKNRIQMIQNLHLAMLFIEEDlKIRV 83

                           90       100
                   ....*....|....*....|....*
gi 2462528555  101 QGLSAEEIRNGNLKAILGLFFSLSR 125
Cdd:cd21225     84 QGIGAEDFVDNNKKLILGLLWTLYR 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 23-123 1.25e-14

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: 71.66  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCpkNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21188      4 QKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRKIKLVN 79

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21188     80 IRAEDIVDGNPKLTLGLIWTI 100
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 23-123 1.25e-13

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: 69.05  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21228      5 QQNTFTRWCNEHL-KCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLV 82

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21228     83 SIDSSAIVDGNLKLILGLIWTL 104
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 23-126 4.75e-13

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: 67.60  E-value: 4.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21190      6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85

                           90       100
                   ....*....|....*....|....
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21190     86 INSTDIVDGKPSIVLGLIWTIILY 109
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 23-119 5.07e-13

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: 67.39  E-value: 5.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GcpKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21246     17 QKKTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTkG--KMRIHCLENVDKALQFLKEQRVHLE 92

                           90
                   ....*....|....*...
gi 2462528555  102 GLSAEEIRNGNLKAILGL 119
Cdd:cd21246     93 NMGSHDIVDGNHRLTLGL 110
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 23-123 1.05e-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: 66.35  E-value: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIE-DINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21183      5 QANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADHIKLV 82

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21183     83 NIGSGDIVNGNIKLILGLIWTL 104
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 23-126 2.45e-12

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: 65.47  E-value: 2.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21241      6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKLVN 85

                           90       100
                   ....*....|....*....|....
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21241     86 INPTDIVDGKPSIVLGLIWTIILY 109
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 23-123 1.00e-11

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: 64.28  E-value: 1.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21310     17 QQNTFTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHIKLV 94

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21310     95 SIDSKAIVDGNLKLILGLIWTL 116
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 25-126 2.22e-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: 62.33  E-value: 2.22e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555    25 RIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINIQGL 103
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 2462528555   104 SAEEIRNGNlKAILGLFFSLSRY 126
Cdd:smart00033   80 EPEDLVEGP-KLILGVIWTLISL 101
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 23-123 4.99e-11

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: 62.74  E-value: 4.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIedingcPK-NRSQM----IENIDACLNFLAAKG 97
Cdd:cd21318     39 QKKTFTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLLEVLSGEQL------PKpTRGRMrihsLENVDKALQFLKEQR 110

                           90       100
                   ....*....|....*....|....*.
gi 2462528555   98 INIQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21318    111 VHLENVGSHDIVDGNHRLTLGLIWTI 136
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 23-123 1.64e-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: 60.87  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21308     21 QQNTFTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21308     99 SIDSKAIVDGNLKLILGLIWTL 120
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 23-123 4.38e-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: 59.71  E-value: 4.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21309     18 QQNTFTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLV 95

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21309     96 SIDSKAIVDGNLKLILGLVWTL 117
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 23-123 1.16e-09

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: 58.53  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIedingcPKN-----RSQMIENIDACLNFLAAKG 97
Cdd:cd21317     32 QKKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQL------PKPtkgrmRIHCLENVDKALQFLKEQK 103

                           90       100
                   ....*....|....*....|....*.
gi 2462528555   98 INIQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21317    104 VHLENMGSHDIVDGNHRLTLGLIWTI 129
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-124 1.19e-09

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 63.42  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:COG5069     10 QKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                           90       100
                   ....*....|....*....|..
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSLS 124
Cdd:COG5069     89 IGPQDIVDGNPKLILGLIWSLI 110
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 23-123 1.65e-09

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: 57.39  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21186      3 QKKTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVN 79

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21186     80 ISSNDIVDGNPKLTLGLVWSI 100
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 23-123 2.70e-09

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: 56.82  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21191      6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVS 85

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21191     86 IDAAEIADGNPSLVLGLIWNI 106
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1831-2215 7.05e-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: 7.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1831 LTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEEMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIhVD 1910
Cdd:COG1401     55 LRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEA-LE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1911 PVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTISVTVKGLAENSLDSLVFESLI--------PKPILQR 1982
Cdd:COG1401    134 RARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYlkdllrekFEETLEA 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1983 YVSLLIEHRRIILSGPSGTGKTYLANRLSEYIVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ------------ 2050
Cdd:COG1401    214 FLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyeptpgiflrf 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2051 CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQATSStpnlq 2108
Cdd:COG1401    291 CLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDDRS----- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 2109 lhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNMELVKIIDwipkvwhHLNRFLEahsSSDVTIGPRLFL 2185
Cdd:COG1401    366 -----------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLLE-------ELNEILE---KRDFQIGHRALL 418

                          410       420       430
                   ....*....|....*....|....*....|
gi 2462528555 2186 SCPIDVDGSRVWFTDLWNYSIIPYLLEAIR 2215
Cdd:COG1401    419 LLDGLLSGDLDLLLLLLLLLLELLLLLLDK 448
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 23-123 7.37e-09

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: 56.98  E-value: 7.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKI-EDINGcpKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21316     54 QKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRIHCLENVDKALQFLKEQRVHLE 129

                           90       100
                   ....*....|....*....|..
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21316    130 NMGSHDIVDGNHRLTLGLIWTI 151
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 23-123 7.42e-09

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: 55.61  E-value: 7.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21242      6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKSIKLIN 83

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21242     84 IHVPDIIEGKPSIILGLIWTI 104
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 24-126 1.94e-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: 54.20  E-value: 1.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   24 KRIYTDWANHYLAKsghKRLI-KDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQM--IENIDACLNFLAAKGINI 100
Cdd:cd21221      3 VRVLTEWINEELAD---DRIVvRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKqkLAVVLACVNFLLGLEEDE 79

                           90       100
                   ....*....|....*....|....*.
gi 2462528555  101 QGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21221     80 ARWTVDGIYNKDLVSILHLLVALAHH 105
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 22-119 4.29e-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: 53.35  E-value: 4.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   22 DQKRIYTDWANHYLAKSGH--KRLIKDLQQD-----VTDGVLLAQIIQVVANEKIED--INGC-PKNRSQMIENIDACLN 91
Cdd:cd21217      1 EEKEAFVEHINSLLADDPDlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVPGTIDErkLNKKkPKNIFEATENLNLALN 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462528555   92 flAAK--GINIQGLSAEEIRNGNLKAILGL 119
Cdd:cd21217     81 --AAKkiGCKVVNIGPQDILDGNPHLVLGL 108
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 21-123 4.33e-08

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: 53.39  E-value: 4.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 ED-QKRIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGIN 99
Cdd:cd21231      4 EDvQKKTFTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKG--STRVHALNNVNKALQVLQKNNVD 80

                           90       100
                   ....*....|....*....|....
gi 2462528555  100 IQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21231     81 LVNIGSADIVDGNHKLTLGLIWSI 104
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 23-123 5.69e-08

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: 53.10  E-value: 5.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21235      7 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVKLVN 82

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21235     83 IRNDDIADGNPKLTLGLIWTI 103
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 23-123 9.32e-08

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: 52.73  E-value: 9.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21237      7 QKKTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG--RMRFHRLQNVQIALDFLKQRQVKLVN 82

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21237     83 IRNDDITDGNPKLTLGLIWTI 103
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 23-123 3.64e-07

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: 51.14  E-value: 3.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21236     18 QKKTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHRLQNVQIALDYLKRRQVKLVN 93

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21236     94 IRNDDITDGNPKLTLGLIWTI 114
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 23-119 1.04e-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: 49.76  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIEdingcPKNRSQM----IENIDACLNFLAAKgI 98
Cdd:cd21247     21 QKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLP-----RPSRGKMrvhfLENNSKAITFLKTK-V 94

                           90       100
                   ....*....|....*....|.
gi 2462528555   99 NIQGLSAEEIRNGNLKAILGL 119
Cdd:cd21247     95 PVKLIGPENIVDGDRTLILGL 115
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 24-126 1.16e-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: 49.20  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   24 KRIYTDWANHYlaksGHKRLIKDLQQDVTDGVLLAQIIqvvanEKIEdiNGC----------PKNRSQMIEN----IDAC 89
Cdd:cd21219      6 ERAFRMWLNSL----GLDPLINNLYEDLRDGLVLLQVL-----DKIQ--PGCvnwkkvnkpkPLNKFKKVENcnyaVDLA 74

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462528555   90 LNFlaakGINIQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21219     75 KKL----GFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 23-123 2.23e-05

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: 45.39  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   23 QKRIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANEKIEDINGcpKNRSQMIENIDACLNFLAAKGINIQG 102
Cdd:cd21232      3 QKKTFTKWINARFSKSG-KPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERG--STRVHALNNVNRVLQVLHQNNVELVN 79

                           90       100
                   ....*....|....*....|.
gi 2462528555  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21232     80 IGGTDIVDGNHKLTLGLLWSI 100
AAA_22 pfam13401
AAA domain;
1993-2080 2.71e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.80  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1993 IILSGPSGTGKTYLANRLSE----------YIVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVd 2059
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLLALAVAV- 86

                           90       100
                   ....*....|....*....|.
gi 2462528555 2060 mplVIILDNLHHVSslGEIFN 2080
Cdd:pfam13401   87 ---VLIIDEAQHLS--LEALE 102
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
143-330 2.91e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.46  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  143 PPAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTARVSAAGSEAKTRGGSTTANNRRS 222
Cdd:PRK07003   373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAK 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  223 QsfnnydkSKPVTSPPPPPSSHEKEPLASSASSHPGMSDNAPASLESGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSVK 302
Cdd:PRK07003   453 A-------NARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAA 525

                          170       180
                   ....*....|....*....|....*...
gi 2462528555  303 hsatvsmlsvKPPGPEAPRPTPEAMKPA 330
Cdd:PRK07003   526 ----------APPAPEARPPTPAAAAPA 543
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 222-651 3.23e-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: 49.53  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  222 SQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSdnapasleSGSSSTPTNCSTSSAIPQPGAATKPWRSKSLSV 301
Cdd:pfam05109  431 SPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVS--------TADVTSPTPAGTTSGASPVTPSPSPRDNGTESK 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  302 KHSATVSMLSVKPPGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNS-KGGSKAGEGPGSRDTSCERLETLPSFEESEELEA 380
Cdd:pfam05109  503 APDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAvTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSA 582

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  381 asrmLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQQREKDKEKSKDLAKRASVTER-LDLKEEPKED 459
Cdd:pfam05109  583 ----VTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRpSSISETLSPS 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  460 PSGAAVPEMPkkssKIASFIPKGGKlNSAKKEPMAPSHSGIPKPGMKSMPGKSPSAPAPSKEGERSRSGK--LSSGLPQQ 537
Cdd:pfam05109  659 TSDNSTSHMP----LLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEvnVTKGTPPK 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  538 K---PQLDGRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSVGTTQTTGSNTVsvqlpqPQQQYnhpNTATVAPFLYR 614
Cdd:pfam05109  734 NatsPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTT------PRTRY---NATTYLPPSTS 804

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2462528555  615 SQTDTEGNVTAESSSTGVSVEPshFTKTGQPALEELT 651
Cdd:pfam05109  805 SKLRPRWTFTSPPVTTAQATVP--VPPTSQPRFSNLS 839
PHA03247 PHA03247
large tegument protein UL36; Provisional
 141-638 5.84e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  141 PLPPAvsqvagAPSqcqaGTPQQQVPvtpqapcqPHQPAPhqqskaqaemqsRLPGP--TARVSAAGSEAKTRGGSTTAN 218
Cdd:PHA03247  2554 PLPPA------APP----AAPDRSVP--------PPRPAP------------RPSEPavTSRARRPDAPPQSARPRAPVD 2603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  219 NRRSQSFNNYDKSKPVTSPPPPPSSHEKEPLASS-------ASSHPGMSDNAPAsleSGSSSTPTNCSTSSAIPQPGAAT 291
Cdd:PHA03247  2604 DRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEpdphpppTVPPPERPRDDPA---PGRVSRPRRARRLGRAAQASSPP 2680

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  292 KPWRSKSLSVKhSATVSMLSVKPPGPEAPRPTPEAMKPApnnqksmlekLKLFNSKGGSKAGEGPGSRDTSCERLETLPS 371
Cdd:PHA03247  2681 QRPRRRAARPT-VGSLTSLADPPPPPPTPEPAPHALVSA----------TPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  372 feESEELEAASRMLTTVGPASSSPKIALKGIAQRTFSRALTNKKSSlkgnekEKEKQQREKDKEKSKDLAKRASVTERLD 451
Cdd:PHA03247  2750 --TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE------SRESLPSPWDPADPPAAVLAPAAALPPA 2821

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  452 LKEEPKEDPSGAAVPEMPKKSSK-IASFIPKGGKL------------NSAKKEPMAPSH---------------SGIPKP 503
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARppvrrlarpavsrstESFALP 2901

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  504 GMKSMPGKSPSAPAPSKEGERSRSGKLSSGLPQQKPQLDGRHSSSSSSLASSEGKGPGGTTLNHSIssqtVSGSVGTTQT 583
Cdd:PHA03247  2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL----VPGRVAVPRF 2977

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555  584 -TGSNTVSVQLPQPQqqyNHPNTATVAPflyrsqtdtegNVTAESSSTGVSVEPSH 638
Cdd:PHA03247  2978 rVPQPAPSREAPASS---TPPLTGHSLS-----------RVSSWASSLALHEETDP 3019
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 21-125 1.89e-04

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: 43.81  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGH-KRLI------KDLQQDVTDGVLLAQIIQVVANEKIED--INGCPKNRSQMIENIDACLN 91
Cdd:cd21292     23 EEEKVAFVNWINKNLGDDPDcKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDEraINKKKLTVFTIHENLTLALN 102

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462528555   92 FLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSR 125
Cdd:cd21292    103 SASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1990-2098 2.26e-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: 2.26e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  1990 HRRIILSGPSGTGKTYLANRLSEYIVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2063
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 2462528555  2064 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2098
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 24-126 3.64e-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: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   24 KRIYTDWANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANEKI--EDINGCPKNRSQMIENIDACLNFLAAKGINIQ 101
Cdd:cd21222     18 KELLLQFVNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTP 95

                           90       100
                   ....*....|....*....|....*.
gi 2462528555  102 GLSAEEIRNGNLKAILGLFFSL-SRY 126
Cdd:cd21222     96 KIRPEDIVNGDLKSILRVLYSLfSKY 121
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 25-126 5.51e-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: 41.53  E-value: 5.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   25 RIYTDWANHYLAksGHKRLIKDLQQDVTDGVLLAQIIQVVANEKIE-------DINGCPKNRsQMIENIDACLNFlaaKG 97
Cdd:cd21304      4 KVLIEWINDELA--EQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEvaevtqsEVGQKQKLR-TVLDKINRILNL---PR 77

                           90       100
                   ....*....|....*....|....*....
gi 2462528555   98 INIQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21304     78 WSQQKWSVDSIHSKNLVAILHLLVALARH 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
 140-330 7.68e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 7.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  140 SPLPPAVSQVAGAPSQcQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTARVSAAGSEAKTRGGSTTANN 219
Cdd:PHA03247  2738 APAPPAVPAGPATPGG-PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  220 RRSQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASSHPGMSDNAPASLESGSSSTPTNCSTSS-------AIPQPGAATK 292
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPArppvrrlARPAVSRSTE 2896

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462528555  293 PWRSKSLSVKHSATvsmlsvkPPGPEAPRPTPEAMKPA 330
Cdd:PHA03247  2897 SFALPPDQPERPPQ-------PQAPPPPQPQPQPPPPP 2927
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1530-1606 8.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 8.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462528555 1530 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1606
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 21-123 1.06e-03

first calponin homology (CH) domain found in plastin-3; 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. Plastin- 3 contains 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: 409174  Cd Length: 148  Bit Score: 41.58  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGHKRLI-------KDLQQDVTDGVLLAQIIQVVANEKIEDINGCPKNRSQMI--ENIDACLN 91
Cdd:cd21325     23 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENLNLALN 102

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528555   92 FLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21325    103 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQI 134
PHA03247 PHA03247
large tegument protein UL36; Provisional
 140-333 1.55e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  140 SPLP-PAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQA------EMQSRLPGPTARVSAAGSEAKTRG 212
Cdd:PHA03247   279 PPPPeAAAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPAGDAEEEDdedgamEVVSPLPRPRQHYPLGFPKRRRPT 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  213 GSTTANNRRSQSFNNYDKSKPVTSPPPPPSSHEKEPLASSASshpGMSDNAPASLESGSSSTPTNCSTSSAIPQPGAATK 292
Cdd:PHA03247   359 WTPPSSLEDLSAGRHHPKRASLPTRKRRSARHAATPFARGPG---GDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPL 435

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462528555  293 PwrskslsvkhsatvsmlSVKPPGPEAPRPTPEAMKPAPNN 333
Cdd:PHA03247   436 P-----------------SAEPGSDDGPAPPPERQPPAPAT 459
AAA_18 pfam13238
AAA domain;
1993-2070 1.71e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.49  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1993 IILSGPSGTGKTYLANRLSEyiVLREGRELTD-----GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILD 2067
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSK--RLGFGDNVRDlalenGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLIID 78


                   ...
gi 2462528555 2068 NLH 2070
Cdd:pfam13238   79 GHL 81
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1738-1796 1.75e-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: 39.47  E-value: 1.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555 1738 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1796
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1746-1801 2.02e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462528555 1746 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1801
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 138-480 2.27e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  138 LSSPLPPAVSQVAGAPSQCQAGTPQQQVPVTPQAPCQPHQPAPHQQSKAQAEMQSRLPGPTAR---VSAAGSEAKTRGGS 214
Cdd:pfam03154  334 LQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALkplSSLSTHHPPSAHPP 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  215 TTANNRRSQSFNNYDKSKPVTSPPP----PPSSHekePLASSASSHPGMSDNAPASLESGSSS--TPTNC---STSSAIP 285
Cdd:pfam03154  414 PLQLMPQSQQLPPPPAQPPVLTQSQslppPAASH---PPTSGLHQVPSQSPFPQHPFVPGGPPpiTPPSGpptSTSSAMP 490

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  286 --QPGAATKPWRSKSLSVKHSATVSMLSVK------PPGPEAPRPTPEAMKPAPN-----NQKSMLEKLKLFNSKGGSka 352
Cdd:pfam03154  491 giQPPSSASVSSSGPVPAAVSCPLPPVQIKeealdeAEEPESPPPPPRSPSPEPTvvntpSHASQSARFYKHLDRGYN-- 568

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  353 gegpgsrdtSCERLETLpsfeeseeleaasrmlttVGPASSSPKIALKGIAQRTFSRALTNKKSSLKGNEKEKEKQ-QRE 431
Cdd:pfam03154  569 ---------SCARTDLY------------------FMPLAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKErERE 621

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2462528555  432 KDKEKSKDLAKRASVTERLDLKEEPKEDPSGAAVPEMPKKSSKIASFIP 480
Cdd:pfam03154  622 REREREAERAAKASSSSHEGRMGDPQLAGPAHMRPSFEPPPTTIAAVPP 670
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 44-123 2.29e-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: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   44 IKDLQQDVTDGVLLAQIIQVVANekieDINGCPK------NRSQMIENIDACLNFLAAKGI----NIQGLSAEEIRNGNL 113
Cdd:cd21223     26 VTNLAVDLRDGVRLCRLVELLTG----DWSLLSKlrvpaiSRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHR 101

                           90
                   ....*....|
gi 2462528555  114 KAILGLFFSL 123
Cdd:cd21223    102 EKTLALLWRI 111
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 18-126 2.33e-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: 40.03  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   18 HGLEDQKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANEKIE--DINGCPKNRSQMIENIDACLNFLAA 95
Cdd:cd21307     12 DKVNTVKKAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFFIHlsEFFLTPSSTSEMLHNVTLALELLKE 89

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528555   96 KGINIQGLSAEEIRNGNLKAILGLFFSL-SRY 126
Cdd:cd21307     90 GGLLNFPVNPEDIVNGDSKATIRVLYCLfSKY 121
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 30-117 3.30e-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: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   30 WANHYLAKSGHKRL-IKDLQQDVTDGVLLAQII-QVVANEKIEDINGCPKNRSQMIENIDACLNflAAKGINI-QGLSAE 106
Cdd:cd21218     18 WVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLhSLAPELCDKELVLEVLSEEDLEKRAEKVLQ--AAEKLGCkYFLTPE 95

                           90
                   ....*....|.
gi 2462528555  107 EIRNGNLKAIL 117
Cdd:cd21218     96 DIVSGNPRLNL 106
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 21-123 5.37e-03

first calponin homology (CH) domain found in plastin-2; 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-2 contains 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: 409173  Cd Length: 145  Bit Score: 39.61  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555   21 EDQKRIYTDWANHYLAKSGHKRLI-------KDLQQDVTDGVLLAQIIQVVANEKIED--INGCPKNRSQMIENIDACLN 91
Cdd:cd21324     23 EEEKYAFVNWINKALENDPDCKHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtINKKKLTPFTIQENLNLALN 102

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462528555   92 FLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21324    103 SASAIGCHVVNIGAEDLKEGKPYLVLGLLWQV 134
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1993-2073 6.59e-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: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1993 IILSGPSGTGKTYLANRLSEYIVLREGR--ELTdgvIATFNVDHKSSKELRQYLSNLAdqcnSENNAVDMPLVIILDNLH 2070
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPflYLN---ASDLLEGLVVAELFGHFLVRLL----FELAEKAKPGVLFIDEID 94


                   ...
gi 2462528555 2071 HVS 2073
Cdd:cd00009     95 SLS 97
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 879-1180 6.63e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  879 TDDINTSSSISSYANTPASSRKNLDVQTDAEKHSQvernslwSGDDVKKSDGGSDSGIKMEPGSKWRRNPSDVSDESDKS 958
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETAR-------APSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555  959 TSGKKNPVISQTGSWRRGMTAQVGITM-PRTKASAPagaLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSgde 1037
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWgPENECPLP---RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP--- 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462528555 1038 skKPLPSSSRTPTANANSFGFKKQSGSA-AGLAMITASGVTV----TSRSATLGKIPKSSALVSRSAGRKSSMDGAQNQD 1112
Cdd:PHA03307   297 --SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSrgaaVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462528555 1113 DGYLALSSRTNLQYRSLPRPSKSNSRNGAGNRSSTSSIDSNISSKSAGLPVPKLREPSKTALGSSLPG 1180
Cdd:PHA03307   375 PSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEPWPG 442
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1533-1605 7.94e-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: 40.90  E-value: 7.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462528555 1533 QSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQ 1605
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
 
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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