NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|167466226|ref|NP_001104486|]
View 

neuron navigator 2 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 15-127 2.60e-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: 237.17  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   15 PVTHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285     1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 167466226   93 LAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 127
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2019-2256 5.70e-08

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


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2019 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2093
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2094 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2144
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2145 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2221
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167466226 2222 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2256
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1570-1646 4.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 4.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466226 1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1646
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 249-643 6.85e-04

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


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   249 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 327
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   328 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 407
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   408 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 486
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   487 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 550
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   551 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 630
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 167466226   631 NVTAESSSAGVSM 643
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1789-1844 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466226 1789 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1844
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
142-335 3.54e-03

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: 42.53  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  142 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 221
Cdd:PRK07003  356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  222 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 298
Cdd:PRK07003  428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 167466226  299 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 335
Cdd:PRK07003  507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1570-1842 4.61e-03

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1649
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1650 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1718
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1719 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1784
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1785 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1842
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 890-1241 6.32e-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: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  890 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 969
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  970 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1048
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1049 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1127
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1128 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1201
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 167466226 1202 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1241
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 15-127 2.60e-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: 237.17  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   15 PVTHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285     1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 167466226   93 LAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 127
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 21-126 4.08e-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: 76.17  E-value: 4.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226    21 EDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINgCPKNRSQMIENIDACLNFLAAK-GIN 99
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100
                   ....*....|....*....|....*..
gi 167466226   100 TQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 25-126 4.91e-12

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: 64.26  E-value: 4.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226     25 RIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINTQGL 103
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 167466226    104 SAEEIRNGNlKAILGLFFSLSRY 126
Cdd:smart00033   80 EPEDLVEGP-KLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-124 6.80e-10

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 64.58  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:COG5069    10 QKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                          90       100
                  ....*....|....*....|..
gi 167466226  103 LSAEEIRNGNLKAILGLFFSLS 124
Cdd:COG5069    89 IGPQDIVDGNPKLILGLIWSLI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2019-2256 5.70e-08

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2019 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2093
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2094 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2144
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2145 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2221
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167466226 2222 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2256
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
AAA_22 pfam13401
AAA domain;
2030-2123 2.11e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  2030 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2095
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80

                           90       100
                   ....*....|....*....|....*...
gi 167466226  2096 SENNAVdmplVIILDNLHHVSslGEIFN 2123
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1570-1646 4.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 4.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466226 1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1646
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2033-2141 5.49e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 5.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   2033 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2106
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 167466226   2107 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2141
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 249-643 6.85e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   249 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 327
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   328 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 407
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   408 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 486
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   487 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 550
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   551 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 630
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 167466226   631 NVTAESSSAGVSM 643
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1789-1844 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466226 1789 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1844
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1781-1839 1.16e-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: 40.24  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167466226 1781 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1839
Cdd:cd22887     7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
142-335 3.54e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  142 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 221
Cdd:PRK07003  356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  222 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 298
Cdd:PRK07003  428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 167466226  299 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 335
Cdd:PRK07003  507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1570-1842 4.61e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1649
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1650 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1718
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1719 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1784
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1785 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1842
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 890-1241 6.32e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  890 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 969
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  970 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1048
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1049 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1127
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1128 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1201
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 167466226 1202 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1241
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
PHA03247 PHA03247
large tegument protein UL36; Provisional
 170-647 7.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  170 GLATPQAPCQLLQPVSHQQGKTqvemqsrlPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPS 249
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVPP--------PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  250 NHEKEPLASSASSHPgmseNVPAPLENSPSVPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP---------- 319
Cdd:PHA03247 2621 THAPDPPPPSPSPAA----NEPDPHPPPTVPPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsl 2695

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  320 ---AGPEAPRPTPEamkPAPNNQKSMLEklklfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGP 396
Cdd:PHA03247 2696 tslADPPPPPPTPE---PAPHALVSATP------LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  397 ASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVT 476
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPT 2837

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  477 EMPKKSSKIASFIPKGGKL------------NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLP 544
Cdd:PHA03247 2838 APPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  545 PQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRS 624
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996

                         490       500
                  ....*....|....*....|...
gi 167466226  625 QTDTEGNVTAESSSAGVSMEPSH 647
Cdd:PHA03247 2997 TGHSLSRVSSWASSLALHEETDP 3019
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 945-1233 8.52e-03

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 8.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   945 KMEPGSKWRRNPSDMSDESDKSVSGKKN---------PVLSQTGSW--------------RRGMTAEVGITMPRTKPSAP 1001
Cdd:pfam17823   32 KMWNGAGKQNASGDAVPRADNKSSEQ*NfcaataapaPVTLTKGTSaahlnstevtaehtPHGTDLSEPATREGAADGAA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1002 TGTLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTVNANSFGFKKQSGSAAGLAMITA 1081
Cdd:pfam17823  112 SRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1082 SGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSN 1161
Cdd:pfam17823  192 SSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN 271

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466226  1162 MSSKSAGLPVPKLREPSKASLGSSLPGLVNQTdkekgisSDSESVASCNSVKVNPATQPVSSSAQATLQPGT 1233
Cdd:pfam17823  272 MGDPHARRLSPAKHMPSDTMARNPAAPMGAQA-------QGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNT 336
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 15-127 2.60e-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: 237.17  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   15 PVTHGLED--QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNF 92
Cdd:cd21285     1 GKSWEAENgfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 167466226   93 LAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 127
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 25-127 4.25e-62

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


Pssm-ID: 409135  Cd Length: 105  Bit Score: 207.19  E-value: 4.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   25 RIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLS 104
Cdd:cd21286     3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 82

                          90       100
                  ....*....|....*....|...
gi 167466226  105 AEEIRNGNLKAILGLFFSLSRYK 127
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSLSRYK 105
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 23-127 1.09e-56

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


Pssm-ID: 409061  Cd Length: 105  Bit Score: 192.03  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                          90       100
                  ....*....|....*....|....*
gi 167466226  103 LSAEEIRNGNLKAILGLFFSLSRYK 127
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 23-127 7.52e-26

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 103.92  E-value: 7.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                          90       100
                  ....*....|....*....|....*.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL-SRYK 127
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALaAHFK 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 23-123 1.52e-20

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 88.61  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21215     5 QKKTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTN 82

                          90       100
                  ....*....|....*....|.
gi 167466226  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-19

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: 84.75  E-value: 3.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21214     6 QRKTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGERLPKPER-GKMRFHKIANVNKALDFIASKGVKLVS 82

                          90       100
                  ....*....|....*....|.
gi 167466226  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 1.51e-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: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   21 EDQKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINT 100
Cdd:cd21227     3 EIQKNTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKL 80

                          90       100
                  ....*....|....*....|...
gi 167466226  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 1.23e-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: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   24 KRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGI-NTQG 102
Cdd:cd00014     1 EEELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79

                          90       100
                  ....*....|....*....|....
gi 167466226  103 LSAEEI-RNGNLKAILGLFFSLSR 125
Cdd:cd00014    80 FEPEDLyEKGNLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 21-126 4.08e-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: 76.17  E-value: 4.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226    21 EDQKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINgCPKNRSQMIENIDACLNFLAAK-GIN 99
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100
                   ....*....|....*....|....*..
gi 167466226   100 TQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRR 106
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 23-119 2.55e-15

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: 74.25  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDIN-GcpKNRSQMIENIDACLNFLAAKgINTQ 101
Cdd:cd21193    17 QKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNrG--RLRVQKIENVNKALAFLKTK-VRLE 91

                          90
                  ....*....|....*...
gi 167466226  102 GLSAEEIRNGNLKAILGL 119
Cdd:cd21193    92 NIGAEDIVDGNPRLILGL 109
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 23-125 6.48e-15

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 72.95  E-value: 6.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGCPKNRSQMIENIDACLNFLAAK-GINT 100
Cdd:cd21225     5 QIKAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFpKKFDLEPKNRIQMIQNLHLAMLFIEEDlKIRV 83

                          90       100
                  ....*....|....*....|....*
gi 167466226  101 QGLSAEEIRNGNLKAILGLFFSLSR 125
Cdd:cd21225    84 QGIGAEDFVDNNKKLILGLLWTLYR 108
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 23-123 8.91e-15

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: 72.87  E-value: 8.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAA-KGINTQ 101
Cdd:cd21311    16 QQNTFTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIV 93

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTL 115
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 23-123 6.17e-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: 69.74  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCpkNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21188     4 QKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGR--MRFHRLQNVQTALDFLKYRKIKLVN 79

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21188    80 IRAEDIVDGNPKLTLGLIWTI 100
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 23-126 5.28e-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: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21190     6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85

                          90       100
                  ....*....|....*....|....
gi 167466226  103 LSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21190    86 INSTDIVDGKPSIVLGLIWTIILY 109
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 23-123 7.12e-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: 66.74  E-value: 7.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21228     5 QQNTFTRWCNEHL-KCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLV 82

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTL 104
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 23-123 4.32e-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: 64.81  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIE-DINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21183     5 QANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADHIKLV 82

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTL 104
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 25-126 4.91e-12

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: 64.26  E-value: 4.91e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226     25 RIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKIEDIN-GCPKNRSQMIENIDACLNFLAAKGINTQGL 103
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 167466226    104 SAEEIRNGNlKAILGLFFSLSRY 126
Cdd:smart00033   80 EPEDLVEGP-KLILGVIWTLISL 101
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 23-119 8.54e-12

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: 63.93  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIEDIN-GcpKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21246    17 QKKTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTkG--KMRIHCLENVDKALQFLKEQRVHLE 92

                          90
                  ....*....|....*...
gi 167466226  102 GLSAEEIRNGNLKAILGL 119
Cdd:cd21246    93 NMGSHDIVDGNHRLTLGL 110
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 23-126 3.61e-11

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: 62.01  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21241     6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKLVN 85

                          90       100
                  ....*....|....*....|....
gi 167466226  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 4.16e-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: 62.36  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21310    17 QQNTFTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHIKLV 94

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTL 116
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 23-123 5.11e-10

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: 59.65  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIedingcPK-NRSQM----IENIDACLNFLAAKG 97
Cdd:cd21318    39 QKKTFTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLLEVLSGEQL------PKpTRGRMrihsLENVDKALQFLKEQR 110

                          90       100
                  ....*....|....*....|....*.
gi 167466226   98 INTQGLSAEEIRNGNLKAILGLFFSL 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 6.41e-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: 59.33  E-value: 6.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21308    21 QQNTFTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21308    99 SIDSKAIVDGNLKLILGLIWTL 120
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
23-124 6.80e-10

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 64.58  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:COG5069    10 QKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKLFN 88

                          90       100
                  ....*....|....*....|..
gi 167466226  103 LSAEEIRNGNLKAILGLFFSLS 124
Cdd:COG5069    89 IGPQDIVDGNPKLILGLIWSLI 110
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 23-123 1.54e-09

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: 58.17  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLaKSGHKRlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21309    18 QQNTFTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLV 95

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21309    96 SIDSKAIVDGNLKLILGLVWTL 117
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 23-123 6.20e-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: 55.47  E-value: 6.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21186     3 QKKTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVN 79

                          90       100
                  ....*....|....*....|.
gi 167466226  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 1.17e-08

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: 54.89  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21191     6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVS 85

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21191    86 IDAAEIADGNPSLVLGLIWNI 106
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 23-123 1.18e-08

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 55.83  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIedingcPKN-----RSQMIENIDACLNFLAAKG 97
Cdd:cd21317    32 QKKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQL------PKPtkgrmRIHCLENVDKALQFLKEQK 103

                          90       100
                  ....*....|....*....|....*.
gi 167466226   98 INTQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21317   104 VHLENMGSHDIVDGNHRLTLGLIWTI 129
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 22-119 1.41e-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: 54.89  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   22 DQKRIYTDWANHYLAKSGH--KRLIKDLQQD-----VTDGVLLAQIIQVVANDKIED--INGC-PKNRSQMIENIDACLN 91
Cdd:cd21217     1 EEKEAFVEHINSLLADDPDlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVPGTIDErkLNKKkPKNIFEATENLNLALN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 167466226   92 flAAK--GINTQGLSAEEIRNGNLKAILGL 119
Cdd:cd21217    81 --AAKkiGCKVVNIGPQDILDGNPHLVLGL 108
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 23-123 4.47e-08

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: 54.66  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKI-EDINGcpKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21316    54 QKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRIHCLENVDKALQFLKEQRVHLE 129

                          90       100
                  ....*....|....*....|..
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21316   130 NMGSHDIVDGNHRLTLGLIWTI 151
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 23-123 5.68e-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: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21235     7 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVKLVN 82

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21235    83 IRNDDIADGNPKLTLGLIWTI 103
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2019-2256 5.70e-08

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2019 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2093
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2094 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2144
Cdd:COG1401   284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2145 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2221
Cdd:COG1401   364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 167466226 2222 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2256
Cdd:COG1401   412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 23-123 5.71e-08

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: 52.91  E-value: 5.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21242     6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG--HNVFQCRSNIETALSFLKNKSIKLIN 83

                          90       100
                  ....*....|....*....|.
gi 167466226  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 1.04e-07

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: 51.89  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   24 KRIYTDWANHYLAKsghKRLI-KDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQM--IENIDACLNFLAAKGINT 100
Cdd:cd21221     3 VRVLTEWINEELAD---DRIVvRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKqkLAVVLACVNFLLGLEEDE 79

                          90       100
                  ....*....|....*....|....*.
gi 167466226  101 QGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21221    80 ARWTVDGIYNKDLVSILHLLVALAHH 105
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 23-123 1.87e-07

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: 51.96  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21237     7 QKKTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGVKLPREKG--RMRFHRLQNVQIALDFLKQRQVKLVN 82

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21237    83 IRNDDITDGNPKLTLGLIWTI 103
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 21-123 2.17e-07

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: 51.46  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   21 ED-QKRIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGIN 99
Cdd:cd21231     4 EDvQKKTFTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKG--STRVHALNNVNKALQVLQKNNVD 80

                          90       100
                  ....*....|....*....|....
gi 167466226  100 TQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSI 104
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 23-123 2.52e-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: 51.52  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21236    18 QKKTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHRLQNVQIALDYLKRRQVKLVN 93

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21236    94 IRNDDITDGNPKLTLGLIWTI 114
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 24-126 4.03e-07

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: 50.74  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   24 KRIYTDWANHYlaksGHKRLIKDLQQDVTDGVLLAQIIqvvanDKIEdiNGC----------PKNRSQMIEN----IDAC 89
Cdd:cd21219     6 ERAFRMWLNSL----GLDPLINNLYEDLRDGLVLLQVL-----DKIQ--PGCvnwkkvnkpkPLNKFKKVENcnyaVDLA 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 167466226   90 LNFlaakGINTQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21219    75 KKL----GFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 23-119 1.25e-05

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: 46.67  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEdingcPKNRSQM----IENIDACLNFLAAKgI 98
Cdd:cd21247    21 QKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLP-----RPSRGKMrvhfLENNSKAITFLKTK-V 94

                          90       100
                  ....*....|....*....|.
gi 167466226   99 NTQGLSAEEIRNGNLKAILGL 119
Cdd:cd21247    95 PVKLIGPENIVDGDRTLILGL 115
AAA_22 pfam13401
AAA domain;
2030-2123 2.11e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  2030 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2095
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80

                           90       100
                   ....*....|....*....|....*...
gi 167466226  2096 SENNAVdmplVIILDNLHHVSslGEIFN 2123
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 24-126 4.39e-05

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 44.89  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   24 KRIYTDWANHYLAKSGhkRLIKDLQQDVTDGVLLAQIIQVVANDKI--EDINGCPKNRSQMIENIDACLNFLAAKGINTQ 101
Cdd:cd21222    18 KELLLQFVNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTP 95

                          90       100
                  ....*....|....*....|....*.
gi 167466226  102 GLSAEEIRNGNLKAILGLFFSL-SRY 126
Cdd:cd21222    96 KIRPEDIVNGDLKSILRVLYSLfSKY 121
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 23-123 7.09e-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: 44.23  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   23 QKRIYTDWANHYLAKSGhKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGcpKNRSQMIENIDACLNFLAAKGINTQG 102
Cdd:cd21232     3 QKKTFTKWINARFSKSG-KPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERG--STRVHALNNVNRVLQVLHQNNVELVN 79

                          90       100
                  ....*....|....*....|.
gi 167466226  103 LSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21232    80 IGGTDIVDGNHKLTLGLLWSI 100
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
 5-125 1.52e-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: 44.19  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226    5 SESSQQQrrkpVTHGL-EDQKRIYTDWANHYLAKSGH-KRLI------KDLQQDVTDGVLLAQIIQVVANDKIED--ING 74
Cdd:cd21292    10 SEASSEG----TTHSYsEEEKVAFVNWINKNLGDDPDcKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDEraINK 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 167466226   75 CPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSR 125
Cdd:cd21292    86 KKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQIIR 136
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1570-1646 4.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 4.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466226 1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1646
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2033-2141 5.49e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 5.49e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   2033 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2106
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 167466226   2107 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2141
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
 21-123 5.62e-04

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: 42.74  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   21 EDQKRIYTDWANHYLAKSGHKRLI-------KDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMI--ENIDACLN 91
Cdd:cd21325    23 EEEKYAFVNWINKALENDPDCRHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIiqENLNLALN 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 167466226   92 FLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21325   103 SASAIGCHVVNIGAEDLRAGKPHLVLGLLWQI 134
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 249-643 6.85e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 6.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   249 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 327
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   328 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 407
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   408 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 486
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   487 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 550
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   551 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 630
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827

                          410
                   ....*....|...
gi 167466226   631 NVTAESSSAGVSM 643
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 44-123 7.89e-04

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: 41.04  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   44 IKDLQQDVTDGVLLAQIIQVVANDKiediNGCPK------NRSQMIENIDACLNFLAAKGINT----QGLSAEEIRNGNL 113
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLTGDW----SLLSKlrvpaiSRLQKLHNVEVALKALKEAGVLRggdgGGITAKDIVDGHR 101

                          90
                  ....*....|
gi 167466226  114 KAILGLFFSL 123
Cdd:cd21223   102 EKTLALLWRI 111
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1789-1844 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466226 1789 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1844
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 18-127 1.15e-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: 40.80  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   18 HGLEDQKRIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAQIIQVVANDKIE--DINGCPKNRSQMIENIDACLNFLAA 95
Cdd:cd21307    12 DKVNTVKKAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFFIHlsEFFLTPSSTSEMLHNVTLALELLKE 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 167466226   96 KGINTQGLSAEEIRNGNLKAILGLFFSL-SRYK 127
Cdd:cd21307    90 GGLLNFPVNPEDIVNGDSKATIRVLYCLfSKYK 122
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 1781-1839 1.16e-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: 40.24  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167466226 1781 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1839
Cdd:cd22887     7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
CH_PLS2_rpt1 cd21324
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ...
 3-123 1.53e-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: 41.15  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226    3 SISESSQQQRRKPVTHGLEDQKRIYTDWANHYLAKSGHKRLI-------KDLQQDVTDGVLLAQIIQVVANDKIED--IN 73
Cdd:cd21324     5 AIGGTSEQSSAGTQHSYSEEEKYAFVNWINKALENDPDCKHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtIN 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 167466226   74 GCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 123
Cdd:cd21324    85 KKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQV 134
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 30-117 1.66e-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: 40.36  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   30 WANHYLAKSGHKRL-IKDLQQDVTDGVLLAQII-QVVANDKIEDINGCPKNRSQMIENIDACLNflAAKGIN-TQGLSAE 106
Cdd:cd21218    18 WVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLhSLAPELCDKELVLEVLSEEDLEKRAEKVLQ--AAEKLGcKYFLTPE 95

                          90
                  ....*....|.
gi 167466226  107 EIRNGNLKAIL 117
Cdd:cd21218    96 DIVSGNPRLNL 106
AAA_18 pfam13238
AAA domain;
2036-2113 1.74e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.49  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  2036 IILSGPSGTGKTYLANRLSEyvVLREGRELTD-----GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILD 2110
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSK--RLGFGDNVRDlalenGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLIID 78


                   ...
gi 167466226  2111 NLH 2113
Cdd:pfam13238   79 GHL 81
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 25-126 3.01e-03

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: 39.22  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   25 RIYTDWANHYLAksGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIE-------DINGCPKNRsQMIENIDACLNFlaaKG 97
Cdd:cd21304     4 KVLIEWINDELA--EQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEvaevtqsEVGQKQKLR-TVLDKINRILNL---PR 77

                          90       100
                  ....*....|....*....|....*....
gi 167466226   98 INTQGLSAEEIRNGNLKAILGLFFSLSRY 126
Cdd:cd21304    78 WSQQKWSVDSIHSKNLVAILHLLVALARH 106
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
142-335 3.54e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  142 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 221
Cdd:PRK07003  356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  222 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 298
Cdd:PRK07003  428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 167466226  299 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 335
Cdd:PRK07003  507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1570-1842 4.61e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1570 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1649
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1650 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1718
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1719 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1784
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1785 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1842
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
AAA_28 pfam13521
AAA domain;
2035-2067 5.77e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 5.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 167466226  2035 RIILSGPSGTGKTYLANRLSE---YVVLRE-GRELTD 2067
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAArfgYPVVPEaAREILE 37
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 2030-2116 5.99e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.93  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 2030 LTEHRRII-LSGPSGTGKTYLANRL-----SEYVVLR------EGRELTDGVIATFNVDHKSS------KELRQYLSNLA 2091
Cdd:COG3267    39 LAQGGGFVvLTGEVGTGKTTLLRRLlerlpDDVKVAYipnpqlSPAELLRAIADELGLEPKGAskadllRQLQEFLLELA 118

                          90       100
                  ....*....|....*....|....*
gi 167466226 2092 DQcnsennavDMPLVIILDNLHHVS 2116
Cdd:COG3267   119 AA--------GRRVVLIIDEAQNLP 135
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 890-1241 6.32e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  890 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 969
Cdd:PHA03307   22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  970 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 1048
Cdd:PHA03307   95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1049 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1127
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1128 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1201
Cdd:PHA03307  244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 167466226 1202 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1241
Cdd:PHA03307  321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1573-1645 6.87e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 6.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167466226 1573 QSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQ 1645
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 170-647 7.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  170 GLATPQAPCQLLQPVSHQQGKTqvemqsrlPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPS 249
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVPP--------PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  250 NHEKEPLASSASSHPgmseNVPAPLENSPSVPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP---------- 319
Cdd:PHA03247 2621 THAPDPPPPSPSPAA----NEPDPHPPPTVPPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsl 2695

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  320 ---AGPEAPRPTPEamkPAPNNQKSMLEklklfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGP 396
Cdd:PHA03247 2696 tslADPPPPPPTPE---PAPHALVSATP------LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  397 ASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVT 476
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPT 2837

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  477 EMPKKSSKIASFIPKGGKL------------NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLP 544
Cdd:PHA03247 2838 APPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  545 PQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRS 624
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996

                         490       500
                  ....*....|....*....|...
gi 167466226  625 QTDTEGNVTAESSSAGVSMEPSH 647
Cdd:PHA03247 2997 TGHSLSRVSSWASSLALHEETDP 3019
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 934-1188 8.00e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  934 KKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSGK----KNPVLSQTGSWRRGMTAEVGITMPRTKPSAPTGTLKT-P 1008
Cdd:PHA03307  190 PAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRsaadDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTrI 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1009 GTGKTDDAKVSEKGRLSPkasqvkrSPSDAGRSSgdeskKTLPSSSRTPTVNANSFGFKKQSGSA-AGLAMITASGATVT 1087
Cdd:PHA03307  270 WEASGWNGPSSRPGPASS-------SSSPRERSP-----SPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSR 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226 1088 SRSATLGKIPKSSALVGRP----TGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMS 1163
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPpppaDPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPL 417

                         250       260
                  ....*....|....*....|....*
gi 167466226 1164 SKSAGLPVPKLREPSKASLGSSLPG 1188
Cdd:PHA03307  418 DAGAASGAFYARYPLLTPSGEPWPG 442
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 945-1233 8.52e-03

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.10  E-value: 8.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226   945 KMEPGSKWRRNPSDMSDESDKSVSGKKN---------PVLSQTGSW--------------RRGMTAEVGITMPRTKPSAP 1001
Cdd:pfam17823   32 KMWNGAGKQNASGDAVPRADNKSSEQ*NfcaataapaPVTLTKGTSaahlnstevtaehtPHGTDLSEPATREGAADGAA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1002 TGTLKTPGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTVNANSFGFKKQSGSAAGLAMITA 1081
Cdd:pfam17823  112 SRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466226  1082 SGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSN 1161
Cdd:pfam17823  192 SSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN 271

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466226  1162 MSSKSAGLPVPKLREPSKASLGSSLPGLVNQTdkekgisSDSESVASCNSVKVNPATQPVSSSAQATLQPGT 1233
Cdd:pfam17823  272 MGDPHARRLSPAKHMPSDTMARNPAAPMGAQA-------QGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNT 336
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH