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Conserved domains on  [gi|1584352038|ref|NP_001355744|]
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neuron navigator 3 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 79-183 3.01e-69

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: 227.99  E-value: 3.01e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1584352038  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 204-582 5.33e-10

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: 64.94  E-value: 5.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  204 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 283
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  284 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPWRSKSmnvkhSATSTMltvkqpspaTSPTPSS 363
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSPTLGKT-----SPTSAV---------TTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  364 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 443
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  444 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 517
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584352038  518 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 582
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2009-2274 2.13e-07

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: 55.93  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2009 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 2076
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2077 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 2127
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2128 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2204
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584352038 2205 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2274
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 979-1294 1.37e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  979 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 1057
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1058 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 1135
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1136 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1212
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1213 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1292
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1584352038 1293 SP 1294
Cdd:PHA03307   409 AG 410
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1572-1652 3.40e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1572 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1651
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1584352038 1652 Q 1652
Cdd:COG4372    146 A 146
 
Name Accession Description Interval E-value
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 79-183 3.01e-69

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: 227.99  E-value: 3.01e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1584352038  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 81-182 9.02e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 9.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINgCPRSQSQMIENVDVCLSFLAAR-GVNVQGL 159
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLI 83

                           90       100
                   ....*....|....*....|...
gi 1584352038  160 SAEEIRNGNLKAILGLFFSLSRY 182
Cdd:pfam00307   84 EPEDLVEGDNKSVLTYLASLFRR 106
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 204-582 5.33e-10

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: 64.94  E-value: 5.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  204 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 283
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  284 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPWRSKSmnvkhSATSTMltvkqpspaTSPTPSS 363
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSPTLGKT-----SPTSAV---------TTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  364 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 443
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  444 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 517
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584352038  518 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 582
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
76-180 1.01e-07

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 57.26  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   76 EIEDSKIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVN 155
Cdd:COG5069      7 QKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVK 85

                           90       100
                   ....*....|....*....|....*
gi 1584352038  156 VQGLSAEEIRNGNLKAILGLFFSLS 180
Cdd:COG5069     86 LFNIGPQDIVDGNPKLILGLIWSLI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2009-2274 2.13e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 55.93  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2009 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 2076
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2077 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 2127
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2128 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2204
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584352038 2205 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2274
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 273-684 4.08e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 4.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  273 SQSFNSIDKNKPPNYANGNEKDSPKGPQPSSGINGNTQPPSTSGQPPASAiPSPSASKPWRSKSMNVKHSATSTMLTVKQ 352
Cdd:PTZ00449   482 TQEIKKLIKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEE-GEHEDSKESDEPKEGGKPGETKEGEVGKK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  353 PSPATSPTPSsdrlKPPVtegVKSAPSGQKSMLEKFKLVNARTALRP--PQAPSSGPNDGGREDDAFSESGEMEgfnsgl 430
Cdd:PTZ00449   561 PGPAKEHKPS----KIPT---LSKKPEFPKDPKHPKDPEEPKKPKRPrsAQRPTRPKSPKLPELLDIPKSPKRP------ 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  431 nsggSTNSSPKVSPKLTPPKA-----GSKNFSNKKSLLQPK-----EKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKT 500
Cdd:PTZ00449   628 ----ESPKSPKRPPPPQRPSSperpeGPKIIKSPKPPKSPKppfdpKFKEKFYDDYLDAAAKSKETKTTVVLDESFESIL 703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  501 SKIASLIPKGSKTAAAKKESLIPSSSGIPKPGSKVPTPKQTISPGSAASKESEKFRTSKGSSSQAFPkAITAEKASTPSL 580
Cdd:PTZ00449   704 KETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP-DILAEEFKEEDI 782

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  581 STPLDGREAGQASPSSScvmqvTHSSGQSPGNGAvQLPQQQQHSHPNTATVAPFiyrahsENEGTSLpPADSCTSPTKMD 660
Cdd:PTZ00449   783 HAETGEPDEAMKRPDSP-----SEHEDKPPGDHP-SLPKKRHRLDGLALSTTDL------ESDAGRI-AKDASGKIVKLK 849

                          410       420
                   ....*....|....*....|....
gi 1584352038  661 SSYSKTAKQCLEEISGEDPEARRM 684
Cdd:PTZ00449   850 RSKSFDDLTTVEEAEEMGAEARKI 873
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 979-1294 1.37e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  979 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 1057
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1058 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 1135
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1136 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1212
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1213 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1292
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1584352038 1293 SP 1294
Cdd:PHA03307   409 AG 410
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2023-2143 4.24e-05

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: 45.83  E-value: 4.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  2023 HHRIILSGPSGTGKTYLANKLAEY-------VITKSGRKKTEDA------IATFNVDHKSSKELQQYLAN-LAEQCSADn 2088
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARElgppgggVIYIDGEDILEEVldqlllIIVGGKKASGSGELRLRLALaLARKLKPD- 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1584352038  2089 ngvelpvVIILDNLHH---------VGSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2143
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2026-2106 1.95e-04

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 44.06  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2026 IILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGvelpvVIILDNLHHV 2105
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96


                   .
gi 1584352038 2106 G 2106
Cdd:cd00009     97 S 97
AAA_22 pfam13401
AAA domain;
2026-2113 5.59e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2026 IILSGPSGTGKTYLANKLAE----------YVITKSGRKKTE--DAIATF----NVDHKSSKELQQYLANLAEQCSAdnn 2089
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRAlglpLSGRLSKEELLAALQQLLLALAV--- 84

                           90       100
                   ....*....|....*....|....*....
gi 1584352038 2090 gvelPVVIILDNLHHVGS-----LSDIFN 2113
Cdd:pfam13401   85 ----AVVLIIDEAQHLSLealeeLRDLLN 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1572-1652 3.40e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1572 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1651
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1584352038 1652 Q 1652
Cdd:COG4372    146 A 146
 
Name Accession Description Interval E-value
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 79-183 3.01e-69

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: 227.99  E-value: 3.01e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286      1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80

                           90       100
                   ....*....|....*....|....*
gi 1584352038  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286     81 LSAEEIRNGNLKAILGLFFSLSRYK 105
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 79-183 4.80e-67

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: 222.15  E-value: 4.80e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21285     11 DKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGINIQG 90

                           90       100
                   ....*....|....*....|....*
gi 1584352038  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21285     91 LSAEEIRNGNLKAILGLFFSLSRYK 115
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 81-183 4.47e-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: 190.10  E-value: 4.47e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21212      3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGIT 82

                           90       100
                   ....*....|....*....|...
gi 1584352038  161 AEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21212     83 AEDIVDGNLKAILGLFFSLSRYK 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 83-183 4.06e-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: 104.69  E-value: 4.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 162
Cdd:cd21213      5 YVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSAK 84

                           90       100
                   ....*....|....*....|..
gi 1584352038  163 EIRNGNLKAILGLFFSL-SRYK 183
Cdd:cd21213     85 DIVDGNLKAIMRLILALaAHFK 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 81-179 7.91e-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: 86.69  E-value: 7.91e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21215      7 KTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTNIG 84

                           90
                   ....*....|....*....
gi 1584352038  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21215     85 AEDIVDGNLKLILGLLWTL 103
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 76-179 2.09e-18

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 82.44  E-value: 2.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   76 EIEDSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEdingcPRSQSQM----IENVDVCLSFLAA 151
Cdd:cd21214      3 EKQQRKTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGERLP-----KPERGKMrfhkIANVNKALDFIAS 75

                           90       100
                   ....*....|....*....|....*...
gi 1584352038  152 RGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21214     76 KGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 81-179 2.02e-15

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: 74.25  E-value: 2.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21227      7 NTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIG 84

                           90
                   ....*....|....*....
gi 1584352038  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21227     85 NEDIVNGNLKLILGLIWHL 103
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 63-175 2.20e-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: 2.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   63 EFGEKKALQGTAKEIEdSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDIN-GcpRSQSQMIEN 141
Cdd:cd21193      2 EKGRIRALQEERINIQ-KKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNrG--RLRVQKIEN 76

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1584352038  142 VDVCLSFLAARgVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21193     77 VNKALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 81-181 4.14e-15

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: 73.14  E-value: 4.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNV-QGL 159
Cdd:cd00014      2 EELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPElDLF 80

                           90       100
                   ....*....|....*....|...
gi 1584352038  160 SAEEI-RNGNLKAILGLFFSLSR 181
Cdd:cd00014     81 EPEDLyEKGNLKKVLGTLWALAL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 81-182 9.02e-15

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 72.32  E-value: 9.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINgCPRSQSQMIENVDVCLSFLAAR-GVNVQGL 159
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLI 83

                           90       100
                   ....*....|....*....|...
gi 1584352038  160 SAEEIRNGNLKAILGLFFSLSRY 182
Cdd:pfam00307   84 EPEDLVEGDNKSVLTYLASLFRR 106
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
 83-179 7.17e-13

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: 67.48  E-value: 7.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLAKSGhkRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAA-RGVNVQGLSA 161
Cdd:cd21311     20 FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIVNIDS 97

                           90
                   ....*....|....*...
gi 1584352038  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21311     98 SDIVDGKLKLILGLIWTL 115
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 76-181 1.31e-12

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: 66.40  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   76 EIEDSKIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAAR-G 153
Cdd:cd21225      2 EKVQIKAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFpKKFDLEPKNRIQMIQNLHLAMLFIEEDlK 80

                           90       100
                   ....*....|....*....|....*...
gi 1584352038  154 VNVQGLSAEEIRNGNLKAILGLFFSLSR 181
Cdd:cd21225     81 IRVQGIGAEDFVDNNKKLILGLLWTLYR 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 81-179 3.07e-12

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: 65.12  E-value: 3.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQsqMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21188      6 KTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFH--RLQNVQTALDFLKYRKIKLVNIR 81

                           90
                   ....*....|....*....
gi 1584352038  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21188     82 AEDIVDGNPKLTLGLIWTI 100
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 83-179 9.88e-12

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: 63.66  E-value: 9.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21228      9 FTRWCNEHL-KCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLVSIDS 86

                           90
                   ....*....|....*...
gi 1584352038  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21228     87 SAIVDGNLKLILGLIWTL 104
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 75-179 1.03e-11

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: 63.65  E-value: 1.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   75 KEIEdSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARG 153
Cdd:cd21183      2 KRIQ-ANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADH 78

                           90       100
                   ....*....|....*....|....*.
gi 1584352038  154 VNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21183     79 IKLVNIGSGDIVNGNIKLILGLIWTL 104
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
 68-175 7.06e-11

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 61.61  E-value: 7.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   68 KALQGTaKEIEDSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKVEDIN-GcpRSQSQMIENVDVCL 146
Cdd:cd21246      7 KALADE-REAVQKKTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTkG--KMRIHCLENVDKAL 81

                           90       100
                   ....*....|....*....|....*....
gi 1584352038  147 SFLAARGVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21246     82 QFLKEQRVHLENMGSHDIVDGNHRLTLGL 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
 40-179 2.79e-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: 60.42  E-value: 2.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   40 RPLEFATPERSMLSCQlTLKSTCEfgEKKALQgtakeiedSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQI 119
Cdd:cd21318     11 RPWDEPAATAKLFECS-RIKALAD--EREAVQ--------KKTFTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLLEV 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584352038  120 IANEKV-EDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21318     78 LSGEQLpKPTRG--RMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTI 136
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 83-179 3.11e-10

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: 60.04  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21310     21 FTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHIKLVSIDS 98

                           90
                   ....*....|....*...
gi 1584352038  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21310     99 KAIVDGNLKLILGLIWTL 116
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
 75-182 3.96e-10

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: 59.12  E-value: 3.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   75 KEIEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGV 154
Cdd:cd21190      2 QERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCI 81

                           90       100
                   ....*....|....*....|....*...
gi 1584352038  155 NVQGLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21190     82 KLVNINSTDIVDGKPSIVLGLIWTIILY 109
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 204-582 5.33e-10

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: 64.94  E-value: 5.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  204 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 283
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  284 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPWRSKSmnvkhSATSTMltvkqpspaTSPTPSS 363
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSPTLGKT-----SPTSAV---------TTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  364 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 443
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  444 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 517
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1584352038  518 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 582
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 83-179 2.08e-09

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: 57.79  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21308     25 FTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 102

                           90
                   ....*....|....*...
gi 1584352038  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21308    103 KAIVDGNLKLILGLIWTL 120
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 83-179 3.95e-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: 57.01  E-value: 3.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLADIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21309     22 FTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99

                           90
                   ....*....|....*...
gi 1584352038  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21309    100 KAIVDGNLKLILGLVWTL 117
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 63-179 6.74e-09

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 56.22  E-value: 6.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   63 EFGEKKALQgTAKEIEDSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGcpRSQSQMIEN 141
Cdd:cd21317     17 ERSRIKALA-DEREAVQKKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQLpKPTKG--RMRIHCLEN 91

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1584352038  142 VDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21317     92 VDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTI 129
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
 60-179 1.30e-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: 56.21  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   60 STCEFGEKKALQGTAKEIE--DSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLADIIQIIANEKV-EDINGcpRSQS 136
Cdd:cd21316     33 SSARLFERSRIKALADEREavQKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRI 108

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1584352038  137 QMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21316    109 HCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTI 151
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 81-179 1.91e-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: 54.65  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLADIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 156
Cdd:cd21235      9 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMrfhkLQNVQIALDYLRHRQVKL 80

                           90       100
                   ....*....|....*....|...
gi 1584352038  157 QGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21235     81 VNIRNDDIADGNPKLTLGLIWTI 103
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 81-182 2.41e-08

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 53.82  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKsghKRLI-KDLQQDIADGVLLADIIQIIANEKVE--DINGCPRSQSQMIENVDVCLSFLAARGVNVQ 157
Cdd:cd21221      4 RVLTEWINEELAD---DRIVvRDLEEDLFDGQVLQALLEKLANEKLEvpEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                           90       100
                   ....*....|....*....|....*
gi 1584352038  158 GLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21221     81 RWTVDGIYNKDLVSILHLLVALAHH 105
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 81-179 2.58e-08

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: 53.92  E-value: 2.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKrLIKDLQQDIADGVLLADIIQIIANEKVEDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21186      5 KTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVNIS 81

                           90
                   ....*....|....*....
gi 1584352038  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21186     82 SNDIVDGNPKLTLGLVWSI 100
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
 81-182 3.73e-08

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: 53.53  E-value: 3.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21241      8 KTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKIKLVNIN 87

                           90       100
                   ....*....|....*....|..
gi 1584352038  161 AEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21241     88 PTDIVDGKPSIVLGLIWTIILY 109
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 81-179 6.29e-08

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 53.11  E-value: 6.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLADIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 156
Cdd:cd21237      9 KTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGVKL------PREKGRMrfhrLQNVQIALDFLKQRQVKL 80

                           90       100
                   ....*....|....*....|...
gi 1584352038  157 QGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21237     81 VNIRNDDITDGNPKLTLGLIWTI 103
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
76-180 1.01e-07

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 57.26  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   76 EIEDSKIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVN 155
Cdd:COG5069      7 QKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVK 85

                           90       100
                   ....*....|....*....|....*
gi 1584352038  156 VQGLSAEEIRNGNLKAILGLFFSLS 180
Cdd:COG5069     86 LFNIGPQDIVDGNPKLILGLIWSLI 110
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 81-179 1.31e-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: 52.68  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLADIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 156
Cdd:cd21236     20 KTFTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhrLQNVQIALDYLKRRQVKL 91

                           90       100
                   ....*....|....*....|...
gi 1584352038  157 QGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21236     92 VNIRNDDITDGNPKLTLGLIWTI 114
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
 76-179 1.34e-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: 51.85  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   76 EIED--SKIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARG 153
Cdd:cd21231      2 EREDvqKKTFTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHA--LNNVNKALQVLQKNN 78

                           90       100
                   ....*....|....*....|....*.
gi 1584352038  154 VNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21231     79 VDLVNIGSADIVDGNHKLTLGLIWSI 104
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
 81-179 1.80e-07

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


Pssm-ID: 409091  Cd Length: 111  Bit Score: 51.76  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVedingcPRSQS----QMIENVDVCLSFLAARGVNV 156
Cdd:cd21242      8 RTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQL------PREKGhnvfQCRSNIETALSFLKNKSIKL 81

                           90       100
                   ....*....|....*....|...
gi 1584352038  157 QGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21242     82 INIHVPDIIEGKPSIILGLIWTI 104
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 2009-2274 2.13e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 55.93  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2009 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 2076
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2077 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 2127
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2128 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2204
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1584352038 2205 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2274
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 87-182 1.68e-06

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: 49.12  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   87 ANHYLAKSGhkRLIKDLQQDIADGVLLADIIQIIANEKV--EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEI 164
Cdd:cd21222     25 VNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPEDI 102

                           90
                   ....*....|....*....
gi 1584352038  165 RNGNLKAILGLFFSL-SRY 182
Cdd:cd21222    103 VNGDLKSILRVLYSLfSKY 121
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 273-684 4.08e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 4.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  273 SQSFNSIDKNKPPNYANGNEKDSPKGPQPSSGINGNTQPPSTSGQPPASAiPSPSASKPWRSKSMNVKHSATSTMLTVKQ 352
Cdd:PTZ00449   482 TQEIKKLIKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEE-GEHEDSKESDEPKEGGKPGETKEGEVGKK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  353 PSPATSPTPSsdrlKPPVtegVKSAPSGQKSMLEKFKLVNARTALRP--PQAPSSGPNDGGREDDAFSESGEMEgfnsgl 430
Cdd:PTZ00449   561 PGPAKEHKPS----KIPT---LSKKPEFPKDPKHPKDPEEPKKPKRPrsAQRPTRPKSPKLPELLDIPKSPKRP------ 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  431 nsggSTNSSPKVSPKLTPPKA-----GSKNFSNKKSLLQPK-----EKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKT 500
Cdd:PTZ00449   628 ----ESPKSPKRPPPPQRPSSperpeGPKIIKSPKPPKSPKppfdpKFKEKFYDDYLDAAAKSKETKTTVVLDESFESIL 703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  501 SKIASLIPKGSKTAAAKKESLIPSSSGIPKPGSKVPTPKQTISPGSAASKESEKFRTSKGSSSQAFPkAITAEKASTPSL 580
Cdd:PTZ00449   704 KETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP-DILAEEFKEEDI 782

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  581 STPLDGREAGQASPSSScvmqvTHSSGQSPGNGAvQLPQQQQHSHPNTATVAPFiyrahsENEGTSLpPADSCTSPTKMD 660
Cdd:PTZ00449   783 HAETGEPDEAMKRPDSP-----SEHEDKPPGDHP-SLPKKRHRLDGLALSTTDL------ESDAGRI-AKDASGKIVKLK 849

                          410       420
                   ....*....|....*....|....
gi 1584352038  661 SSYSKTAKQCLEEISGEDPEARRM 684
Cdd:PTZ00449   850 RSKSFDDLTTVEEAEEMGAEARKI 873
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 100-183 4.48e-06

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: 47.73  E-value: 4.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  100 IKDLQQDIADGVLLadIIQIIANE----KVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21307     36 VKDLDSQFADGVIL--LLLIGQLEgffiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRV 113


                   ....*....
gi 1584352038  176 FFSL-SRYK 183
Cdd:cd21307    114 LYCLfSKYK 122
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 78-182 5.25e-06

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 47.28  E-value: 5.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   78 EDSKIYTDWANHYlaksGHKRLIKDLQQDIADGVLLadiIQIIanEKVEdiNGC----------PRSQSQMIENVDVCLS 147
Cdd:cd21219      4 REERAFRMWLNSL----GLDPLINNLYEDLRDGLVL---LQVL--DKIQ--PGCvnwkkvnkpkPLNKFKKVENCNYAVD 72

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1584352038  148 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21219     73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
 81-175 8.72e-06

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 47.06  E-value: 8.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVedingcPR-SQSQM----IENVDVCLSFLAARgVN 155
Cdd:cd21247     23 KTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL------PRpSRGKMrvhfLENNSKAITFLKTK-VP 95

                           90       100
                   ....*....|....*....|
gi 1584352038  156 VQGLSAEEIRNGNLKAILGL 175
Cdd:cd21247     96 VKLIGPENIVDGDRTLILGL 115
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
 81-179 1.24e-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: 46.16  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLADIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21232      5 KTFTKWINARFSKSG-KPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHA--LNNVNRVLQVLHQNNVELVNIG 81

                           90
                   ....*....|....*....
gi 1584352038  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21232     82 GTDIVDGNHKLTLGLLWSI 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 979-1294 1.37e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  979 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 1057
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1058 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 1135
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1136 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1212
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1213 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1292
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1584352038 1293 SP 1294
Cdd:PHA03307   409 AG 410
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2023-2143 4.24e-05

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: 45.83  E-value: 4.24e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  2023 HHRIILSGPSGTGKTYLANKLAEY-------VITKSGRKKTEDA------IATFNVDHKSSKELQQYLAN-LAEQCSADn 2088
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARElgppgggVIYIDGEDILEEVldqlllIIVGGKKASGSGELRLRLALaLARKLKPD- 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1584352038  2089 ngvelpvVIILDNLHH---------VGSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2143
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 83-175 5.09e-05

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: 44.49  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   83 YTDWANHYLAKSGH--KRLIKDLQQD-----IADGVLLADIIQIIANEKVED--INGC-PRSQSQMIENVDVCLSFLAAR 152
Cdd:cd21217      6 FVEHINSLLADDPDlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVPGTIDErkLNKKkPKNIFEATENLNLALNAAKKI 85

                           90       100
                   ....*....|....*....|...
gi 1584352038  153 GVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21217     86 GCKVVNIGPQDILDGNPHLVLGL 108
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 81-179 6.55e-05

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: 44.49  E-value: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLADIIQIIANEKVEDINgcpRSQSQMI---ENVDVCLSFLAARGVNVQ 157
Cdd:cd21191      8 RTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEY---KPSSHRIfrlNNIAKALKFLEDSNVKLV 84

                           90       100
                   ....*....|....*....|..
gi 1584352038  158 GLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21191     85 SIDAAEIADGNPSLVLGLIWNI 106
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 81-182 1.15e-04

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


Pssm-ID: 409153  Cd Length: 107  Bit Score: 43.45  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAksGHKRLIKDLQQDIADGVLLADIIQIIANEKVE--DINGCPRSQSQMIENV-DVCLSFLAARGVNVQ 157
Cdd:cd21304      4 KVLIEWINDELA--EQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEvaEVTQSEVGQKQKLRTVlDKINRILNLPRWSQQ 81

                           90       100
                   ....*....|....*....|....*
gi 1584352038  158 GLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21304     82 KWSVDSIHSKNLVAILHLLVALARH 106
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2026-2106 1.95e-04

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 44.06  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2026 IILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGvelpvVIILDNLHHV 2105
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96


                   .
gi 1584352038 2106 G 2106
Cdd:cd00009     97 S 97
AAA_22 pfam13401
AAA domain;
2026-2113 5.59e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2026 IILSGPSGTGKTYLANKLAE----------YVITKSGRKKTE--DAIATF----NVDHKSSKELQQYLANLAEQCSAdnn 2089
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRAlglpLSGRLSKEELLAALQQLLLALAV--- 84

                           90       100
                   ....*....|....*....|....*....
gi 1584352038 2090 gvelPVVIILDNLHHVGS-----LSDIFN 2113
Cdd:pfam13401   85 ----AVVLIIDEAQHLSLealeeLRDLLN 109
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
 100-179 7.06e-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: 41.42  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  100 IKDLQQDIADGVLLADIIQIIANEK--VEDINGCPRSQSQMIENVDVCLSFLAARGV----NVQGLSAEEIRNGNLKAIL 173
Cdd:cd21223     26 VTNLAVDLRDGVRLCRLVELLTGDWslLSKLRVPAISRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKTL 105


                   ....*.
gi 1584352038  174 GLFFSL 179
Cdd:cd21223    106 ALLWRI 111
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 223-596 7.22e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 7.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  223 SSLTARYAAQSKHSGIATSQKKPTrlPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKNKPPnyANGNEKDSPKGPQPS 302
Cdd:PHA03307    93 STLAPASPAREGSPTPPGPSSPDP--PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP--AAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  303 SGingNTQPPSTSGQPPASAIPSPSASKPWRSKSmnvkHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSAPSGQK 382
Cdd:PHA03307   169 SR---QAALPLSSPEETARAPSSPPAEPPPSTPP----AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  383 SMLEKFKLVNARTALRPPQAPSSGPndgGREDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKltPPKAGSKNFSNKKSl 462
Cdd:PHA03307   242 SESSGCGWGPENECPLPRPAPITLP---TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS--SPGSGPAPSSPRAS- 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  463 lqpkEKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKTSkiasliPKGSKtaaakkesliPSSSGIPKPGSKVPTPKQTI 542
Cdd:PHA03307   316 ----SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS------PSPSR----------PPPPADPSSPRKRPRPSRAP 375

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1584352038  543 SPGSAASKESEKFRTSKGSSSQAFPKAITAEKASTPSLSTPLDGREAGQASPSS 596
Cdd:PHA03307   376 SSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
PHA03378 PHA03378
EBNA-3B; Provisional
 226-409 7.94e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 7.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  226 TARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKNKPPNYANGNEKD---SPKGPQPS 302
Cdd:PHA03378   678 PTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPpaaAPGRARPP 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038  303 SGINGNTQPPSTSG-----QPPASAIPSPSaSKPWRSKSMNVKHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSA 377
Cdd:PHA03378   758 AAAPGRARPPAAAPgaptpQPPPQAPPAPQ-QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRG 836

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1584352038  378 -PSGQK-SMLEKfklvnaRTALRPPQAPSSGPND 409
Cdd:PHA03378   837 rPSLKKpAALER------QAAAGPTPSPGSGTSD 864
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
 81-182 2.35e-03

first calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin 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: 409185  Cd Length: 106  Bit Score: 39.87  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLADIIQIIANEK--VEDINGCPRSQSQMIENV-DVCLSFLAARGVNVQ 157
Cdd:cd21336      4 KVLIDWINDVLVEE--RIIVKDLEEDLYDGQVLQKLLEKLAGRKlnVAEVTQSEIGQKQKLQTVlEAVNDLLRPQGWAIK 81

                           90       100
                   ....*....|....*....|....*
gi 1584352038  158 gLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21336     82 -WSVDSIHGKNLVAILHLLVALAMH 105
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1572-1652 3.40e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 1572 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1651
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1584352038 1652 Q 1652
Cdd:COG4372    146 A 146
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 86-173 4.64e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 39.20  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   86 WANHYLAKSGHKRL-IKDLQQDIADGVLLADII-QIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNvQGLSAEE 163
Cdd:cd21218     18 WVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLhSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCK-YFLTPED 96

                           90
                   ....*....|
gi 1584352038  164 IRNGNLKAIL 173
Cdd:cd21218     97 IVSGNPRLNL 106
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
 86-158 5.00e-03

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


Pssm-ID: 409144  Cd Length: 113  Bit Score: 38.79  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038   86 WANHYLAKSGHKRLIKDLQQDIADGV----LLAdiiQIIANEKVEDINGCPRSQSQ-----MIENVDV--CLSFLAARGV 154
Cdd:cd21295     20 WVNYHLERAGCDRRIKNFSGDIKDSEaythLLK---QIAPKDAGVDTSALRESDLLqraelMLQNADKigCRKFVTPKDV 96


                   ....
gi 1584352038  155 nVQG 158
Cdd:cd21295     97 -VTG 99
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 2024-2128 7.21e-03

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 39.21  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2024 HRIILSGPSGTGKTYLANKLAEY---------VITKSGRKKTEDAIATFNVDHKS------SKELQ----------QYLA 2078
Cdd:cd17926     19 RRGILVLPTGSGKTLTALALIAYlkelrtlivVPTDALLDQWKERFEDFLGDSSIgligggKKKDFddanvvvatyQSLS 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2079 NLAEQCSADNNgveLPVVIILDNLHHVGSLSdiFNGFLncKYNKCPYIIG 2128
Cdd:cd17926     99 NLAEEEKDLFD---QFGLLIVDEAHHLPAKT--FSEIL--KELNAKYRLG 141
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 2003-2043 8.57e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 39.68  E-value: 8.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1584352038 2003 VFDTLIPKPITQRY---FNLLMEHHR-IILSGPSGTGKTYLANKL 2043
Cdd:pfam12775    7 FSEILVPTVDTVRYtylLDLLLKNGKpVLLVGPTGTGKTVIIQNL 51
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 2026-2118 9.95e-03

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 39.19  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352038 2026 IILSGPSGTGKTYLANKLAEY----VITKSGRKKTEDAIAtfnvdhKSSKELQQyLANLAEQCSadnngvelPVVIILD- 2100
Cdd:cd19481     29 ILLYGPPGTGKTLLAKALAGElglpLIVVKLSSLLSKYVG------ESEKNLRK-IFERARRLA--------PCILFIDe 93

                           90       100
                   ....*....|....*....|....*..
gi 1584352038 2101 ---------NLHHVGSLSDIFNGFLNC 2118
Cdd:cd19481     94 idaigrkrdSSGESGELRRVLNQLLTE 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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