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Conserved domains on  [gi|971371041|ref|XP_015137329|]
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neuron navigator 3 isoform X1 [Gallus gallus]

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 8.19e-70

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: 229.53  E-value: 8.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286     1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80
                          90       100
                  ....*....|....*....|....*
gi 971371041  159 LSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21286    81 LSAEEIRNGNLKAILGLFFSLSRYK 105
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2021-2258 8.05e-09

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


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.55  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2021 PKPITQRYFNLLMEHRRIILSGPSGTGKTYLANRLAEYII-TKSGRKKtedaIATFNVDHKSSKDLRQYLANLAEQ---- 2095
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYRPSLDEGkyep 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2096 --------CSADNNGADLPVVIILD--NLHHISS-LSDIF------------NGFLNCKYNKCP-------YIIGTMNQG 2145
Cdd:COG1401   283 tpgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNTD 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2146 VSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRKLIETEIE---KNIRNNELIKIIDwipktwhHLNSFLEthsSSDV 2222
Cdd:COG1401   363 DRS----------------------LALSDKALRRRFTFEFLDpdlDKLSNEEVVDLLE-------ELNEILE---KRDF 410
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 971371041 2223 TIGPRLFLPCPMDVDGSRVWFTDLWNYSLVPYLLEA 2258
Cdd:COG1401   411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
287-651 2.81e-06

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: 53.00  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   287 GNEKADSPKGPQPSAGMNGN-VQHPTSTGQQQVSAIPSPSASKPWRSKSMNVKHSATSTMLSVKQPSPATSPTPSSDRLK 365
Cdd:pfam05109  480 GTTSGASPVTPSPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   366 PP---PSEGVKPPSSGQKSmlekfklvnartalrpPLSLSSGPSDSGreddTFSECGEVDVLSGGVN-SGGSTSSSPKVS 441
Cdd:pfam05109  560 PAvttPTPNATIPTLGKTS----------------PTSAVTTPTPNA----TSPTVGETSPQANTTNhTLGGTSSTPVVT 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   442 pklTPPKAGSKNLSNKKSLLQPKDKEEKNRDKNKVCTEKTvkeekDQVTETSTKKSSKIASLIPKGSK-----TATAKKE 516
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLS-----PSTSDNSTSHMPLLTSAHPTGGEnitqvTPASTST 691
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   517 SLIPSSSGIPKPGSkvpTAKQNASSACAGSKEAEKLRTTKGnqsqsTPKSQLNEKASPScglafsevkEPNTALTPGPST 596
Cdd:pfam05109  692 HHVSTSSPAPRPGT---TSQASGPGNSSTSTKPGEVNVTKG-----TPPKNATSPQAPS---------GQKTAVPTVTST 754
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 971371041   597 ALSGTATSSGQ-STGNGVvqlpqqQQYSHPNTATVAPFIYRTLSENDSTSLPPSDS 651
Cdd:pfam05109  755 GGKANSTTGGKhTTGHGA------RTSTEPTTDYGGDSTTPRTRYNATTYLPPSTS 804
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1577-1657 1.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 1577 EQIQKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1656
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                  .
gi 971371041 1657 Q 1657
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 8.19e-70

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: 229.53  E-value: 8.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286     1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80
                          90       100
                  ....*....|....*....|....*
gi 971371041  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 1.07e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 71.93  E-value: 1.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041    81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINgCPRSQSQMIENVDVCLSFLAAR-GVNVQGL 159
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLI 83
                           90       100
                   ....*....|....*....|...
gi 971371041   160 SAEEIRNGNLKAILGLFFSLSRY 182
Cdd:pfam00307   84 EPEDLVEGDNKSVLTYLASLFRR 106
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2021-2258 8.05e-09

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.55  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2021 PKPITQRYFNLLMEHRRIILSGPSGTGKTYLANRLAEYII-TKSGRKKtedaIATFNVDHKSSKDLRQYLANLAEQ---- 2095
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYRPSLDEGkyep 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2096 --------CSADNNGADLPVVIILD--NLHHISS-LSDIF------------NGFLNCKYNKCP-------YIIGTMNQG 2145
Cdd:COG1401   283 tpgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNTD 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2146 VSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRKLIETEIE---KNIRNNELIKIIDwipktwhHLNSFLEthsSSDV 2222
Cdd:COG1401   363 DRS----------------------LALSDKALRRRFTFEFLDpdlDKLSNEEVVDLLE-------ELNEILE---KRDF 410
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 971371041 2223 TIGPRLFLPCPMDVDGSRVWFTDLWNYSLVPYLLEA 2258
Cdd:COG1401   411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
70-180 4.85e-08

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 58.41  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   70 LQGKTQELEDSKIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFL 149
Cdd:COG5069     1 MEAKKWQKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFI 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 971371041  150 AARGVNVQGLSAEEIRNGNLKAILGLFFSLS 180
Cdd:COG5069    80 KGKGVKLFNIGPQDIVDGNPKLILGLIWSLI 110
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
287-651 2.81e-06

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: 53.00  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   287 GNEKADSPKGPQPSAGMNGN-VQHPTSTGQQQVSAIPSPSASKPWRSKSMNVKHSATSTMLSVKQPSPATSPTPSSDRLK 365
Cdd:pfam05109  480 GTTSGASPVTPSPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   366 PP---PSEGVKPPSSGQKSmlekfklvnartalrpPLSLSSGPSDSGreddTFSECGEVDVLSGGVN-SGGSTSSSPKVS 441
Cdd:pfam05109  560 PAvttPTPNATIPTLGKTS----------------PTSAVTTPTPNA----TSPTVGETSPQANTTNhTLGGTSSTPVVT 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   442 pklTPPKAGSKNLSNKKSLLQPKDKEEKNRDKNKVCTEKTvkeekDQVTETSTKKSSKIASLIPKGSK-----TATAKKE 516
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLS-----PSTSDNSTSHMPLLTSAHPTGGEnitqvTPASTST 691
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   517 SLIPSSSGIPKPGSkvpTAKQNASSACAGSKEAEKLRTTKGnqsqsTPKSQLNEKASPScglafsevkEPNTALTPGPST 596
Cdd:pfam05109  692 HHVSTSSPAPRPGT---TSQASGPGNSSTSTKPGEVNVTKG-----TPPKNATSPQAPS---------GQKTAVPTVTST 754
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 971371041   597 ALSGTATSSGQ-STGNGVvqlpqqQQYSHPNTATVAPFIYRTLSENDSTSLPPSDS 651
Cdd:pfam05109  755 GGKANSTTGGKhTTGHGA------RTSTEPTTDYGGDSTTPRTRYNATTYLPPSTS 804
AAA_22 pfam13401
AAA domain;
2032-2125 3.54e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 48.49  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  2032 LMEHRRII-LSGPSGTGKTYLANRLAE----------YIITKSGRKKTE--DAIAT-FNVDHKSSKDLRQYLANLAEQCS 2097
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRaLGLPLSGRLSKEELLAALQQLLL 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 971371041  2098 AdnngADLPVVIILDNLHHISS-----LSDIFN 2125
Cdd:pfam13401   81 A----LAVAVVLIIDEAQHLSLealeeLRDLLN 109
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
2038-2118 1.07e-05

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: 47.53  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2038 IILSGPSGTGKTYLANRLAEYIITKSGRKKTEDAIATFNVDHKSSKDLRQYLANLAEQCSADNNGadlpvVIILDNLHHI 2117
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96

                  .
gi 971371041 2118 S 2118
Cdd:cd00009    97 S 97
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2035-2155 4.83e-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: 4.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   2035 HRRIILSGPSGTGKTYLANRLAEYIITKSGR-------------KKTEDAIATFNVDHKSSKDLRQYLAN-LAEQCSADn 2100
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALaLARKLKPD- 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971371041   2101 ngadlpvVIILDNLHH---------ISSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2155
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
PLN03131 PLN03131
hypothetical protein; Provisional
196-467 4.36e-04

hypothetical protein; Provisional


Pssm-ID: 178677 [Multi-domain]  Cd Length: 705  Bit Score: 45.54  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  196 LVELQQQVPSSPAEISQSKTQDMQSSLTARYATQSNHsgiatsqkkasrlpgPSRVPAAGSSTKvqgasnlnrrSQSFNS 275
Cdd:PLN03131  364 LFQLPATSPAPPVDLFEIPPLDPAPAINAYQPPQTSL---------------PSSIDLFGGITQ----------QQSINS 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  276 IDKNKPPQYANGNEKADSPKGPQPSAGMNGN------VQHPTSTGQQQVSAIPSPSASKPWRSKSMNVKHSATST----- 344
Cdd:PLN03131  419 LDEKSPELSIPKNEGWATFDGIQPIASTPGNenltpfSIGPSMAGSANFDQVPSLDKGMQWPPFQNSSDEESASGpapwl 498
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  345 --MLSVKQPSPATSPTPSS----DRLKPPPSEGVKPPSSGQksmlekfklvnarTALRPP--------LSLSSGPSDSGR 410
Cdd:PLN03131  499 gdLHNVEAPDNTSAQNWNAfefdDSVAGIPLEGIKQSSEPQ-------------TAANMPptadqligCKALEDFNKDGI 565
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 971371041  411 EDDTFSECGEVDVLSGGVNSGGSTSSSPKVSPKLTPPKAGSKNLSNKKSLLQPKDKE 467
Cdd:PLN03131  566 KRTAPHGQGELPGLDEPSDILAEPSYTPPAHPIMEHAQSHANDHKSINPFDLPYDSD 622
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1577-1657 1.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 1577 EQIQKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1656
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                  .
gi 971371041 1657 Q 1657
Cdd:COG4372   146 A 146
PRK06835 PRK06835
DNA replication protein DnaC; Validated
2002-2141 3.74e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 41.81  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2002 NLKGV-EENSLDSF---VFDTLI--PKPITQR-----------YF--NLLMEHRRIILSGPSGTGKTYLANRLAEYIITk 2062
Cdd:PRK06835  131 NLKEIlKEENFSNFnlnYYSDEKddDEPLSPRknmekilekckNFieNFDKNNENLLFYGNTGTGKTFLSNCIAKELLD- 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2063 sgRKKT---EDAIATFNV--DHK--SSKDLRQYLANLAEqcsadnngADLpvvIILDNL--HHIS--SLSDIFNgFLNCK 2131
Cdd:PRK06835  210 --RGKSviyRTADELIEIlrEIRfnNDKELEEVYDLLIN--------CDL---LIIDDLgtEKITefSKSELFN-LINKR 275
                         170
                  ....*....|.
gi 971371041 2132 YNK-CPYIIGT 2141
Cdd:PRK06835  276 LLRqKKMIIST 286
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
1569-1650 5.28e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  1569 TAEEK------AHSE---QIQKLRRELVASQEKVATLTSQL-SANAHLVAAfEKSLgnmtgrlqsltmtAEQK---ESEL 1635
Cdd:pfam07926   40 EAQQNyerelvLHAEdikALQALREELNELKAEIAELKAEAeSAKAELEES-EESW-------------EEQKkelEKEL 105
                           90
                   ....*....|....*
gi 971371041  1636 IELRETIEMLKAQNS 1650
Cdd:pfam07926  106 SELEKRIEDLNEQNK 120
 
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 8.19e-70

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: 229.53  E-value: 8.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   79 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 158
Cdd:cd21286     1 DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQG 80
                          90       100
                  ....*....|....*....|....*
gi 971371041  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 ...
72-183 2.29e-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: 222.92  E-value: 2.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   72 GKTQELE---DSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSF 148
Cdd:cd21285     1 GKSWEAEngfDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSF 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 971371041  149 LAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 183
Cdd:cd21285    81 LAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
81-183 9.02e-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: 189.33  E-value: 9.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21212     3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQGIT 82
                          90       100
                  ....*....|....*....|...
gi 971371041  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 1.74e-26

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


Pssm-ID: 409062  Cd Length: 107  Bit Score: 105.84  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 162
Cdd:cd21213     5 YVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSAK 84
                          90       100
                  ....*....|....*....|..
gi 971371041  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 ...
73-179 3.91e-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: 87.46  E-value: 3.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   73 KTQEledsKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAAR 152
Cdd:cd21215     3 DVQK----KTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSR 76
                          90       100
                  ....*....|....*....|....*..
gi 971371041  153 GVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21215    77 GVKLTNIGAEDIVDGNLKLILGLLWTL 103
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
76-179 3.55e-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: 82.05  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   76 ELEDSKIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEdingcPRSQSQM----IENVDVCLSFLAA 151
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQ--IENIEEDFRDGLKLMLLLEVISGERLP-----KPERGKMrfhkIANVNKALDFIAS 75
                          90       100
                  ....*....|....*....|....*...
gi 971371041  152 RGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21214    76 KGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
66-175 1.44e-16

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


Pssm-ID: 409042  Cd Length: 116  Bit Score: 77.72  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDIN-GcpRSQSQMIENVDV 144
Cdd:cd21193    12 ERINIQKKT--------FTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLGKPNrG--RLRVQKIENVNK 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 971371041  145 CLSFLAARgVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21193    80 ALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
81-181 1.40e-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: 74.30  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNV-QGL 159
Cdd:cd00014     2 EELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPElDLF 80
                          90       100
                  ....*....|....*....|...
gi 971371041  160 SAEEI-RNGNLKAILGLFFSLSR 181
Cdd:cd00014    81 EPEDLyEKGNLKKVLGTLWALAL 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
81-179 1.88e-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: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21227     7 NTFTNWVNEQLKPTGMS--VEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVNIG 84
                          90
                  ....*....|....*....
gi 971371041  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21227    85 NEDIVNGNLKLILGLIWHL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
81-182 1.07e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 71.93  E-value: 1.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041    81 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINgCPRSQSQMIENVDVCLSFLAAR-GVNVQGL 159
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK-LNKSEFDKLENINLALDVAEKKlGVPKVLI 83
                           90       100
                   ....*....|....*....|...
gi 971371041   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 8.67e-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: 67.09  E-value: 8.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLAKSGhkRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAA-RGVNVQGLSA 161
Cdd:cd21311    20 FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIVNIDS 97
                          90
                  ....*....|....*...
gi 971371041  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21311    98 SDIVDGKLKLILGLIWTL 115
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
81-181 1.33e-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: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAAR-GVNVQG 158
Cdd:cd21225     7 KAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFpKKFDLEPKNRIQMIQNLHLAMLFIEEDlKIRVQG 85
                          90       100
                  ....*....|....*....|...
gi 971371041  159 LSAEEIRNGNLKAILGLFFSLSR 181
Cdd:cd21225    86 IGAEDFVDNNKKLILGLLWTLYR 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
81-179 2.88e-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: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQsqMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21188     6 KTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFH--RLQNVQTALDFLKYRKIKLVNIR 81
                          90
                  ....*....|....*....
gi 971371041  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21188    82 AEDIVDGNPKLTLGLIWTI 100
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
65-175 4.33e-12

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 65.08  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   65 GERRALQGKTqeledskiYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVEDIN-GcpRSQSQMIENVD 143
Cdd:cd21246    11 DEREAVQKKT--------FTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKPTkG--KMRIHCLENVD 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 971371041  144 VCLSFLAARGVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21246    79 KALQFLKEQRVHLENMGSHDIVDGNHRLTLGL 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
38-179 6.81e-12

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: 65.05  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   38 SPKSLELTGAESSMLSCQlTLKSTCDfgERRALQGKTqeledskiYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEII 117
Cdd:cd21318     9 TERPWDEPAATAKLFECS-RIKALAD--EREAVQKKT--------FTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLL 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 971371041  118 QIIANEKV-EDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21318    76 EVLSGEQLpKPTRG--RMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTI 136
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
83-179 7.34e-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: 64.05  E-value: 7.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21228     9 FTRWCNEHL-KCVNKR-IYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLVSIDS 86
                          90
                  ....*....|....*...
gi 971371041  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 ...
81-179 2.07e-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: 62.88  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVE-DINGCPRSQSQMIENVDVCLSFLAARGVNVQGL 159
Cdd:cd21183     7 NTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKrSYNRRPAFQQHYLENVSTALKFIEADHIKLVNI 84
                          90       100
                  ....*....|....*....|
gi 971371041  160 SAEEIRNGNLKAILGLFFSL 179
Cdd:cd21183    85 GSGDIVNGNIKLILGLIWTL 104
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
83-179 3.21e-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: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21310    21 FTRWCNEHLKCVQKR--LNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHIKLVSIDS 98
                          90
                  ....*....|....*...
gi 971371041  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 7.42e-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: 58.35  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   75 QELEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGV 154
Cdd:cd21190     2 QERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCI 81
                          90       100
                  ....*....|....*....|....*...
gi 971371041  155 NVQGLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21190    82 KLVNINSTDIVDGKPSIVLGLIWTIILY 109
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
66-179 1.59e-09

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 58.14  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGcpRSQSQMIENVDV 144
Cdd:cd21317    27 EREAVQKKT--------FTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQLpKPTKG--RMRIHCLENVDK 94
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 971371041  145 CLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21317    95 ALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTI 129
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
83-179 2.21e-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: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21308    25 FTRWCNEHL-KCVSKR-IANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 102
                          90
                  ....*....|....*...
gi 971371041  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 4.72e-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: 56.63  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLaKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSA 161
Cdd:cd21309    22 FTRWCNEHL-KCVNKR-IGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLVSIDS 99
                          90
                  ....*....|....*...
gi 971371041  162 EEIRNGNLKAILGLFFSL 179
Cdd:cd21309   100 KAIVDGNLKLILGLVWTL 117
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
75-182 6.10e-09

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: 55.84  E-value: 6.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   75 QELEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGV 154
Cdd:cd21241     2 QERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKKI 81
                          90       100
                  ....*....|....*....|....*...
gi 971371041  155 NVQGLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21241    82 KLVNINPTDIVDGKPSIVLGLIWTIILY 109
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2021-2258 8.05e-09

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 60.55  E-value: 8.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2021 PKPITQRYFNLLMEHRRIILSGPSGTGKTYLANRLAEYII-TKSGRKKtedaIATFNVDHKSSKDLRQYLANLAEQ---- 2095
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYRPSLDEGkyep 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2096 --------CSADNNGADLPVVIILD--NLHHISS-LSDIF------------NGFLNCKYNKCP-------YIIGTMNQG 2145
Cdd:COG1401   283 tpgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLsllesdkrgeelSIELPYSGEGEEfsippnlYIIGTMNTD 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2146 VSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRKLIETEIE---KNIRNNELIKIIDwipktwhHLNSFLEthsSSDV 2222
Cdd:COG1401   363 DRS----------------------LALSDKALRRRFTFEFLDpdlDKLSNEEVVDLLE-------ELNEILE---KRDF 410
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 971371041 2223 TIGPRLFLPCPMDVDGSRVWFTDLWNYSLVPYLLEA 2258
Cdd:COG1401   411 QIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
66-179 1.32e-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: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKV-EDINGcpRSQSQMIENVDV 144
Cdd:cd21316    49 EREAVQKKT--------FTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLpKPTKG--RMRIHCLENVDK 116
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 971371041  145 CLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21316   117 ALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTI 151
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
66-179 1.61e-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: 55.03  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IEN 141
Cdd:cd21235     2 ERDRVQKKT--------FTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMrfhkLQN 65
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 971371041  142 VDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21235    66 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTI 103
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
81-182 1.92e-08

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 54.20  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKsghKRLI-KDLQQDIADGVLLAEIIQIIANEKVE--DINGCPRSQSQMIENVDVCLSFLAARGVNVQ 157
Cdd:cd21221     4 RVLTEWINEELAD---DRIVvRDLEEDLFDGQVLQALLEKLANEKLEvpEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80
                          90       100
                  ....*....|....*....|....*
gi 971371041  158 GLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21221    81 RWTVDGIYNKDLVSILHLLVALAHH 105
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
70-180 4.85e-08

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 58.41  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   70 LQGKTQELEDSKIYTDWANHYLAKSGHKRlIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFL 149
Cdd:COG5069     1 MEAKKWQKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFI 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 971371041  150 AARGVNVQGLSAEEIRNGNLKAILGLFFSLS 180
Cdd:COG5069    80 KGKGVKLFNIGPQDIVDGNPKLILGLIWSLI 110
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
81-179 6.96e-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: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 156
Cdd:cd21237     9 KTFTKWVNKHLMKV--RKHINDLYEDLRDGHNLISLLEVLSGVKL------PREKGRMrfhrLQNVQIALDFLKQRQVKL 80
                          90       100
                  ....*....|....*....|...
gi 971371041  157 QGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21237    81 VNIRNDDITDGNPKLTLGLIWTI 103
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
66-179 7.39e-08

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: 53.06  E-value: 7.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IEN 141
Cdd:cd21236    13 ERDKVQKKT--------FTKWINQHLMKV--RKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhrLQN 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 971371041  142 VDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21236    77 VQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTI 114
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
81-179 7.47e-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: 52.38  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGHKrLIKDLQQDIADGVLLAEIIQIIANEKVEDINGcpRSQSQMIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21186     5 KTFTKWINSQLSKANKP-PIKDLFEDLRDGTRLLALLEVLTGKKLKPEKG--RMRVHHLNNVNRALQVLEQNNVKLVNIS 81
                          90
                  ....*....|....*....
gi 971371041  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21186    82 SNDIVDGNPKLTLGLVWSI 100
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
66-179 7.67e-08

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 52.62  E-value: 7.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSGhKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVC 145
Cdd:cd21231     2 EREDVQKKT--------FTKWINAQFAKFG-KPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHA--LNNVNKA 70
                          90       100       110
                  ....*....|....*....|....*....|....
gi 971371041  146 LSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21231    71 LQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSI 104
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
75-179 2.98e-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: 50.98  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   75 QELEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQS----QMIENVDVCLSFLA 150
Cdd:cd21242     2 QEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQL------PREKGhnvfQCRSNIETALSFLK 75
                          90       100
                  ....*....|....*....|....*....
gi 971371041  151 ARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21242    76 NKSIKLINIHVPDIIEGKPSIILGLIWTI 104
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
76-182 6.88e-07

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 49.97  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   76 ELEDSKIYTDWANHYlaksGHKRLIKDLQQDIADGVLLAEIIqiianEKVEdiNGC----------PRSQSQMIENVDVC 145
Cdd:cd21219     2 GSREERAFRMWLNSL----GLDPLINNLYEDLRDGLVLLQVL-----DKIQ--PGCvnwkkvnkpkPLNKFKKVENCNYA 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 971371041  146 LSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21219    71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
87-182 1.36e-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: 49.51  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   87 ANHYLAKSGhkRLIKDLQQDIADGVLLAEIIQIIANEKV--EDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEI 164
Cdd:cd21222    25 VNKHLAKLN--IEVTDLATQFHDGVYLILLIGLLEGFFVplHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRPEDI 102
                          90
                  ....*....|....*....
gi 971371041  165 RNGNLKAILGLFFSL-SRY 182
Cdd:cd21222   103 VNGDLKSILRVLYSLfSKY 121
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
65-175 2.54e-06

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 48.60  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   65 GERRALQGKTQELEDsKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPR-SQSQM----I 139
Cdd:cd21247     8 GHIRKLQEQRMTMQK-KTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL------PRpSRGKMrvhfL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 971371041  140 ENVDVCLSFLAARgVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21247    81 ENNSKAITFLKTK-VPVKLIGPENIVDGDRTLILGL 115
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
287-651 2.81e-06

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: 53.00  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   287 GNEKADSPKGPQPSAGMNGN-VQHPTSTGQQQVSAIPSPSASKPWRSKSMNVKHSATSTMLSVKQPSPATSPTPSSDRLK 365
Cdd:pfam05109  480 GTTSGASPVTPSPSPRDNGTeSKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPT 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   366 PP---PSEGVKPPSSGQKSmlekfklvnartalrpPLSLSSGPSDSGreddTFSECGEVDVLSGGVN-SGGSTSSSPKVS 441
Cdd:pfam05109  560 PAvttPTPNATIPTLGKTS----------------PTSAVTTPTPNA----TSPTVGETSPQANTTNhTLGGTSSTPVVT 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   442 pklTPPKAGSKNLSNKKSLLQPKDKEEKNRDKNKVCTEKTvkeekDQVTETSTKKSSKIASLIPKGSK-----TATAKKE 516
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLS-----PSTSDNSTSHMPLLTSAHPTGGEnitqvTPASTST 691
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   517 SLIPSSSGIPKPGSkvpTAKQNASSACAGSKEAEKLRTTKGnqsqsTPKSQLNEKASPScglafsevkEPNTALTPGPST 596
Cdd:pfam05109  692 HHVSTSSPAPRPGT---TSQASGPGNSSTSTKPGEVNVTKG-----TPPKNATSPQAPS---------GQKTAVPTVTST 754
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 971371041   597 ALSGTATSSGQ-STGNGVvqlpqqQQYSHPNTATVAPFIYRTLSENDSTSLPPSDS 651
Cdd:pfam05109  755 GGKANSTTGGKhTTGHGA------RTSTEPTTDYGGDSTTPRTRYNATTYLPPSTS 804
AAA_22 pfam13401
AAA domain;
2032-2125 3.54e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 48.49  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  2032 LMEHRRII-LSGPSGTGKTYLANRLAE----------YIITKSGRKKTE--DAIAT-FNVDHKSSKDLRQYLANLAEQCS 2097
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRaLGLPLSGRLSKEELLAALQQLLL 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 971371041  2098 AdnngADLPVVIILDNLHHISS-----LSDIFN 2125
Cdd:pfam13401   81 A----LAVAVVLIIDEAQHLSLealeeLRDLLN 109
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
100-183 3.57e-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: 48.12  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  100 IKDLQQDIADGVLLAEIIQIIANE--KVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFF 177
Cdd:cd21307    36 VKDLDSQFADGVILLLLIGQLEGFfiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLY 115

                  ....*..
gi 971371041  178 SL-SRYK 183
Cdd:cd21307   116 CLfSKYK 122
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
66-179 6.06e-06

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: 47.19  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   66 ERRALQGKTqeledskiYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINgcpRSQSQMI---ENV 142
Cdd:cd21191     1 ERENVQKRT--------FTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEY---KPSSHRIfrlNNI 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 971371041  143 DVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 179
Cdd:cd21191    70 AKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNI 106
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
2038-2118 1.07e-05

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: 47.53  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2038 IILSGPSGTGKTYLANRLAEYIITKSGRKKTEDAIATFNVDHKSSKDLRQYLANLAEQCSADNNGadlpvVIILDNLHHI 2117
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96

                  .
gi 971371041 2118 S 2118
Cdd:cd00009    97 S 97
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
83-175 1.78e-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: 46.03  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   83 YTDWANHYLAKSGH--KRLIKDLQQD-----IADGVLLAEIIQIIANEKVED--INGC-PRSQSQMIENVDVCLSFLAAR 152
Cdd:cd21217     6 FVEHINSLLADDPDlkHLLPIDPDGDdlfeaLRDGVLLCKLINKIVPGTIDErkLNKKkPKNIFEATENLNLALNAAKKI 85
                          90       100
                  ....*....|....*....|...
gi 971371041  153 GVNVQGLSAEEIRNGNLKAILGL 175
Cdd:cd21217    86 GCKVVNIGPQDILDGNPHLVLGL 108
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
81-182 4.19e-05

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: 44.61  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAksGHKRLIKDLQQDIADGVLLAEIIQIIANEKVE--DINGCPRSQSQMIENV-DVCLSFLAARGVNVQ 157
Cdd:cd21304     4 KVLIEWINDELA--EQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEvaEVTQSEVGQKQKLRTVlDKINRILNLPRWSQQ 81
                          90       100
                  ....*....|....*....|....*
gi 971371041  158 GLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21304    82 KWSVDSIHSKNLVAILHLLVALARH 106
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2035-2155 4.83e-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: 4.83e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   2035 HRRIILSGPSGTGKTYLANRLAEYIITKSGR-------------KKTEDAIATFNVDHKSSKDLRQYLAN-LAEQCSADn 2100
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALaLARKLKPD- 80
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 971371041   2101 ngadlpvVIILDNLHH---------ISSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2155
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
81-179 7.97e-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: 43.84  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSGhKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSqmIENVDVCLSFLAARGVNVQGLS 160
Cdd:cd21232     5 KTFTKWINARFSKSG-KPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHA--LNNVNRVLQVLHQNNVELVNIG 81
                          90
                  ....*....|....*....
gi 971371041  161 AEEIRNGNLKAILGLFFSL 179
Cdd:cd21232    82 GTDIVDGNHKLTLGLLWSI 100
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
100-179 4.33e-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: 41.81  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  100 IKDLQQDIADGVLLAEIIQIIANEK--VEDINGCPRSQSQMIENVDVCLSFLAARGV----NVQGLSAEEIRNGNLKAIL 173
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLTGDWslLSKLRVPAISRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKTL 105

                  ....*.
gi 971371041  174 GLFFSL 179
Cdd:cd21223   106 ALLWRI 111
PLN03131 PLN03131
hypothetical protein; Provisional
196-467 4.36e-04

hypothetical protein; Provisional


Pssm-ID: 178677 [Multi-domain]  Cd Length: 705  Bit Score: 45.54  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  196 LVELQQQVPSSPAEISQSKTQDMQSSLTARYATQSNHsgiatsqkkasrlpgPSRVPAAGSSTKvqgasnlnrrSQSFNS 275
Cdd:PLN03131  364 LFQLPATSPAPPVDLFEIPPLDPAPAINAYQPPQTSL---------------PSSIDLFGGITQ----------QQSINS 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  276 IDKNKPPQYANGNEKADSPKGPQPSAGMNGN------VQHPTSTGQQQVSAIPSPSASKPWRSKSMNVKHSATST----- 344
Cdd:PLN03131  419 LDEKSPELSIPKNEGWATFDGIQPIASTPGNenltpfSIGPSMAGSANFDQVPSLDKGMQWPPFQNSSDEESASGpapwl 498
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  345 --MLSVKQPSPATSPTPSS----DRLKPPPSEGVKPPSSGQksmlekfklvnarTALRPP--------LSLSSGPSDSGR 410
Cdd:PLN03131  499 gdLHNVEAPDNTSAQNWNAfefdDSVAGIPLEGIKQSSEPQ-------------TAANMPptadqligCKALEDFNKDGI 565
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 971371041  411 EDDTFSECGEVDVLSGGVNSGGSTSSSPKVSPKLTPPKAGSKNLSNKKSLLQPKDKE 467
Cdd:PLN03131  566 KRTAPHGQGELPGLDEPSDILAEPSYTPPAHPIMEHAQSHANDHKSINPFDLPYDSD 622
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
73-182 9.34e-04

first calponin homology (CH) domain found in alpha-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. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-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: 409184  Cd Length: 115  Bit Score: 41.17  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   73 KTQELedSKIYTDWANHYLAksGHKRLIKDLQQDIADGVLLAEIIQIIANEK--VEDINGCPRSQSQ----MIENVDVCL 146
Cdd:cd21335     3 KLQEL--MKVLIDWINDVLV--GERIIVKDLAEDLYDGQVLQKLFEKLEGEKlnVAEVTQSEIAQKQklqtVLEKINETL 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 971371041  147 SfLAARGV--NVQGLSAEeirngNLKAILGLFFSLSRY 182
Cdd:cd21335    79 K-LPPRSIkwNVDSVHAK-----SLVAILHLLVALSQY 110
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1577-1657 1.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 1577 EQIQKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1656
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                  .
gi 971371041 1657 Q 1657
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 1.15e-03

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


Pssm-ID: 409067  Cd Length: 114  Bit Score: 40.75  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   86 WANHYLAKSGHKRL-IKDLQQDIADGVLLAEII-QIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNvQGLSAEE 163
Cdd:cd21218    18 WVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLhSLAPELCDKELVLEVLSEEDLEKRAEKVLQAAEKLGCK-YFLTPED 96
                          90
                  ....*....|
gi 971371041  164 IRNGNLKAIL 173
Cdd:cd21218    97 IVSGNPRLNL 106
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
2036-2122 1.22e-03

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 42.31  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  2036 RRIILSGPSGTGKTYLANRLAE--YIITKSGRKKTEDAIATFNVDHKSSKDLRQYLANLAEqcsADNNGADlpvVIILDN 2113
Cdd:pfam13479    3 LKILIYGPSGIGKTTFAKTLPKplFLDTEKGSKALDGDRFPDIVIRDSWQDFLDAIDELTA---AELADYK---TIVIDT 76

                   ....*....
gi 971371041  2114 LHHISSLSD 2122
Cdd:pfam13479   77 VDWLERLCL 85
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
81-182 1.43e-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: 40.26  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   81 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEK--VEDINGCPRSQSQMIENV-DVCLSFLAARGVNVQ 157
Cdd:cd21336     4 KVLIDWINDVLVEE--RIIVKDLEEDLYDGQVLQKLLEKLAGRKlnVAEVTQSEIGQKQKLQTVlEAVNDLLRPQGWAIK 81
                          90       100
                  ....*....|....*....|....*
gi 971371041  158 gLSAEEIRNGNLKAILGLFFSLSRY 182
Cdd:cd21336    82 -WSVDSIHGKNLVAILHLLVALAMH 105
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
2036-2140 1.48e-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: 41.14  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2036 RRIILSGPSGTGKTYLANRLAEY-------II--TKSGRKKTEDAIATFNVDH-------KSSKDLR---------QYLA 2090
Cdd:cd17926    19 RRGILVLPTGSGKTLTALALIAYlkelrtlIVvpTDALLDQWKERFEDFLGDSsigliggGKKKDFDdanvvvatyQSLS 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 971371041 2091 NLAEQCSAdnnGADLPVVIILDNLHHISSLSdiFNGFLncKYNKCPYIIG 2140
Cdd:cd17926    99 NLAEEEKD---LFDQFGLLIVDEAHHLPAKT--FSEIL--KELNAKYRLG 141
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
271-386 1.71e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 43.61  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  271 QSFNSIDKNKPPQyanGNEKADSPKGPQPSAGMNGNVQHPTSTGQQQVSAIPSPSASKPwrskSMNVKHSATSTMLSVKQ 350
Cdd:PRK14971  361 QLTQKGDDASGGR---GPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQS----ATQPAGTPPTVSVDPPA 433
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 971371041  351 PSPATSPTPSSDRLKPPPSEGVKPPSSGQKSMLEKF 386
Cdd:PRK14971  434 AVPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPS 469
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
2038-2129 2.19e-03

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 40.27  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  2038 IILSGPSGTGKTYLANRLAEY----IITKSGRKKTEDAIAtfnvdhKSSKDLRQYLANLAEQcsadnngadLPVVIILDN 2113
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKElgapFIEISGSELVSKYVG------ESEKRLRELFEAAKKL---------APCVIFIDE 65
                           90       100
                   ....*....|....*....|....*
gi 971371041  2114 LHHI---------SSLSDIFNGFLN 2129
Cdd:pfam00004   66 IDALagsrgsggdSESRRVVNQLLT 90
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
2035-2130 2.30e-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: 40.73  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2035 HRRIILSGPSGTGKTYLANRLA-----EYIITKSGRkktedaIATFNVDhKSSKDLRQyLANLAEQCSadnngadlPVVI 2109
Cdd:cd19481    26 PKGILLYGPPGTGKTLLAKALAgelglPLIVVKLSS------LLSKYVG-ESEKNLRK-IFERARRLA--------PCIL 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 971371041 2110 ILD----------NLHHISSLSDIFNGFLNC 2130
Cdd:cd19481    90 FIDeidaigrkrdSSGESGELRRVLNQLLTE 120
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
2033-2079 3.18e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 41.36  E-value: 3.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 971371041 2033 MEHRRIIL-SGPSGTGKTYLANRLAEYIitksgrkkTEDAIATFNVDH 2079
Cdd:COG0572     4 SGKPRIIGiAGPSGSGKTTFARRLAEQL--------GADKVVVISLDD 43
PRK06835 PRK06835
DNA replication protein DnaC; Validated
2002-2141 3.74e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 41.81  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2002 NLKGV-EENSLDSF---VFDTLI--PKPITQR-----------YF--NLLMEHRRIILSGPSGTGKTYLANRLAEYIITk 2062
Cdd:PRK06835  131 NLKEIlKEENFSNFnlnYYSDEKddDEPLSPRknmekilekckNFieNFDKNNENLLFYGNTGTGKTFLSNCIAKELLD- 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2063 sgRKKT---EDAIATFNV--DHK--SSKDLRQYLANLAEqcsadnngADLpvvIILDNL--HHIS--SLSDIFNgFLNCK 2131
Cdd:PRK06835  210 --RGKSviyRTADELIEIlrEIRfnNDKELEEVYDLLIN--------CDL---LIIDDLgtEKITefSKSELFN-LINKR 275
                         170
                  ....*....|.
gi 971371041 2132 YNK-CPYIIGT 2141
Cdd:PRK06835  276 LLRqKKMIIST 286
CH_PLS_rpt2 cd21295
second calponin homology (CH) domain found in the family of plastin; The plastin family ...
86-158 5.02e-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: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041   86 WANHYLAKSGHKRLIKDLQQDIADGV----LLAeiiQIIANEKVEDINGCPRSQSQ-----MIENVDV--CLSFLAARGV 154
Cdd:cd21295    20 WVNYHLERAGCDRRIKNFSGDIKDSEaythLLK---QIAPKDAGVDTSALRESDLLqraelMLQNADKigCRKFVTPKDV 96

                  ....
gi 971371041  155 nVQG 158
Cdd:cd21295    97 -VTG 99
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
1569-1650 5.28e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  1569 TAEEK------AHSE---QIQKLRRELVASQEKVATLTSQL-SANAHLVAAfEKSLgnmtgrlqsltmtAEQK---ESEL 1635
Cdd:pfam07926   40 EAQQNyerelvLHAEdikALQALREELNELKAEIAELKAEAeSAKAELEES-EESW-------------EEQKkelEKEL 105
                           90
                   ....*....|....*
gi 971371041  1636 IELRETIEMLKAQNS 1650
Cdd:pfam07926  106 SELEKRIEDLNEQNK 120
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
1578-1675 6.95e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 40.75  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041  1578 QIQKLRRELVASQEKVATLTSQLSANAHLvAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQ---A 1654
Cdd:pfam12795   52 ELRELRQELAALQAKAEAAPKEILASLSL-EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARqrlQ 130
                           90       100
                   ....*....|....*....|.
gi 971371041  1655 AIQGALNGPDHTHKDLRIRRQ 1675
Cdd:pfam12795  131 QIRNRLNGPAPPGEPLSEAQR 151
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
2015-2055 7.02e-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: 7.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 971371041  2015 VFDTLIPKPITQRY---FNLLMEHRR-IILSGPSGTGKTYLANRL 2055
Cdd:pfam12775    7 FSEILVPTVDTVRYtylLDLLLKNGKpVLLVGPTGTGKTVIIQNL 51
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
2032-2118 8.77e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.54  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971371041 2032 LMEHRRII-LSGPSGTGKTYLANRLAE---------YII-TKSGRKKTEDAIA-TFNVDHKSS------KDLRQYLANLA 2093
Cdd:COG3267    39 LAQGGGFVvLTGEVGTGKTTLLRRLLErlpddvkvaYIPnPQLSPAELLRAIAdELGLEPKGAskadllRQLQEFLLELA 118
                          90       100
                  ....*....|....*....|....*
gi 971371041 2094 EQcsadnngaDLPVVIILDNLHHIS 2118
Cdd:COG3267   119 AA--------GRRVVLIIDEAQNLP 135
 
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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