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Conserved domains on  [gi|442628495|ref|NP_001260607|]
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sickie, isoform J [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
535-638 3.72e-43

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: 153.51  E-value: 3.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21212     3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGV-DVQGI 81
                          90       100
                  ....*....|....*....|....
gi 442628495  615 TTNDICAGRLKAVLALFFALSRFK 638
Cdd:cd21212    82 TAEDIVDGNLKAILGLFFSLSRYK 105
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2368-2597 6.17e-07

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


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 54.78  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2368 PRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLvarSARGNPSEAIATFNVDHKSSKDLRQYL----------- 2436
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRpsldegkyept 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2437 -GHIAEQAAIANGVSELPSVIILD--NLHHAS-ALGDVFScLLSAG----------PANKLPC---------IIGTMsqa 2493
Cdd:COG1401   284 pGIFLRFCLKAEKNPDKPYVLIIDeiNRANVEkYFGELLS-LLESDkrgeelsielPYSGEGEefsippnlyIIGTM--- 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2494 tcNT--TNLqlhhnfrwvltanhmepvkGFLGRFLRRRlFQLEL----QTQHPQPELAAVLawlpsvwQHINRFLEvhsS 2567
Cdd:COG1401   360 --NTddRSL-------------------ALSDKALRRR-FTFEFldpdLDKLSNEEVVDLL-------EELNEILE---K 407
                         250       260       270
                  ....*....|....*....|....*....|
gi 442628495 2568 SDVTIGPRLFLACPMDLKDSQVWFTDIWNY 2597
Cdd:COG1401   408 RDFQIGHRALLLLDGLLSGDLDLLLLLLLL 437
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
985-1182 2.96e-06

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   985 APQLLQSPSSggLPKPiAAIKGTSKLPSLGGGAGHLPAAE-SQQNQQLlkretsdissnisQPPPAEPPISThahihQNQ 1063
Cdd:pfam03154  380 GPSPFQMNSN--LPPP-PALKPLSSLSTHHPPSAHPPPLQlMPQSQQL-------------PPPPAQPPVLT-----QSQ 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  1064 TPPPPyyANSQPTSHiSSHGFLSEPSTPQHSSGIYGSSRLPPPksalSAPRKLEYNAGPHILSSPTHHQRQGLPRPLVNS 1143
Cdd:pfam03154  439 SLPPP--AASHPPTS-GLHQVPSQSPFPQHPFVPGGPPPITPP----SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVS 511
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 442628495  1144 APNTPTaspnkfhtipsKIVGTIYESKEEQLLPAPPPAS 1182
Cdd:pfam03154  512 CPLPPV-----------QIKEEALDEAEEPESPPPPPRS 539
PHA03247 super family cl33720
large tegument protein UL36; Provisional
729-1182 1.87e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  729 GGTAIPLPATVM---VQRRCPPDKVRPLPPTP-----NHTPSIPG--------LGKSGSDFNTSRPNSPPTSNHtiqslk 792
Cdd:PHA03247 2549 GDPPPPLPPAAPpaaPDRSVPPPRPAPRPSEPavtsrARRPDAPPqsarprapVDDRGDPRGPAPPSPLPPDTH------ 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  793 sgnnnslRPPsiksgiPSPSSPQTAPQKHSMLDKLKLFNKEKQQNAVNAASVASKTQIQSKRTSSSSGFSSARSERSDSS 872
Cdd:PHA03247 2623 -------APD------PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  873 LSLNDGHGSQLKPPSISVSSQKPQPKTKQSKLLAAQQKKEQANKATKLDKKEKSPA-----------RSLNKEESGNESR 941
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPagpatpggparPARPPTTAGPPAP 2769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  942 SSTMGRTG---KSSLVRAVGGVEKNTPKTSSKSSLHSKSDSKSSLKAPQLLQSPSSGGLPKPIAAIKGTSKLPSlGGGAG 1018
Cdd:PHA03247 2770 APPAAPAAgppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPP 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1019 HLPAAESQQNQQLLKRETSdissniSQPPPAEPPISTHAHIHQNQTPPPPYYANSQPTSHISSHGF----LSEPSTPQHS 1094
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPP------SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPpqpqAPPPPQPQPQ 2922
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1095 SGIYGSSRLPPPKSALSAPrKLEYNAGPHILSSPTHHQ-----------RQGLPRPLVNS-APN--TPTASPNKFHTIPS 1160
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVpqpwlgalvpgRVAVPRFRVPQpAPSreAPASSTPPLTGHSL 3001
                         490       500
                  ....*....|....*....|..
gi 442628495 1161 KIVGTIYESKEEQLLPAPPPAS 1182
Cdd:PHA03247 3002 SRVSSWASSLALHEETDPPPVS 3023
 
Name Accession Description Interval E-value
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
535-638 3.72e-43

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: 153.51  E-value: 3.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21212     3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGV-DVQGI 81
                          90       100
                  ....*....|....*....|....
gi 442628495  615 TTNDICAGRLKAVLALFFALSRFK 638
Cdd:cd21212    82 TAEDIVDGNLKAILGLFFSLSRYK 105
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
535-636 1.73e-12

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: 66.16  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTsfkvPDLVKK---PKNQQQMFDNVNSCLHVLRsQSVG-G 610
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLA----PGLVDKkklNKSEFDKLENINLALDVAE-KKLGvP 79
                           90       100
                   ....*....|....*....|....*.
gi 442628495   611 LENITTNDICAGRLKAVLALFFALSR 636
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFR 105
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2368-2597 6.17e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 54.78  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2368 PRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLvarSARGNPSEAIATFNVDHKSSKDLRQYL----------- 2436
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRpsldegkyept 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2437 -GHIAEQAAIANGVSELPSVIILD--NLHHAS-ALGDVFScLLSAG----------PANKLPC---------IIGTMsqa 2493
Cdd:COG1401   284 pGIFLRFCLKAEKNPDKPYVLIIDeiNRANVEkYFGELLS-LLESDkrgeelsielPYSGEGEefsippnlyIIGTM--- 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2494 tcNT--TNLqlhhnfrwvltanhmepvkGFLGRFLRRRlFQLEL----QTQHPQPELAAVLawlpsvwQHINRFLEvhsS 2567
Cdd:COG1401   360 --NTddRSL-------------------ALSDKALRRR-FTFEFldpdLDKLSNEEVVDLL-------EELNEILE---K 407
                         250       260       270
                  ....*....|....*....|....*....|
gi 442628495 2568 SDVTIGPRLFLACPMDLKDSQVWFTDIWNY 2597
Cdd:COG1401   408 RDFQIGHRALLLLDGLLSGDLDLLLLLLLL 437
AAA_22 pfam13401
AAA domain;
2385-2476 1.04e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 50.03  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  2385 LILCGPSGTGKSYLARRLAEFLVARSAR---------GNPSE---AIAT-FNVDHKSSKDLRQYLGHIAEQAAIANgvse 2451
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvdlpsgTSPKDllrALLRaLGLPLSGRLSKEELLAALQQLLLALA---- 83
                           90       100       110
                   ....*....|....*....|....*....|...
gi 442628495  2452 LPSVIILDNLHHASA--------LGDVFSCLLS 2476
Cdd:pfam13401   84 VAVVLIIDEAQHLSLealeelrdLLNLSSKLLQ 116
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2382-2531 1.67e-06

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: 50.06  E-value: 1.67e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   2382 HRRLILCGPSGTGKSYLARRLAEFLVARSAR-----GNPSEAIATFNVDHKSSKDLRQYLGHIAEQA-AIANGVSELPSV 2455
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRlALALARKLKPDV 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628495   2456 IILDNLHhaSALGDVFSCLLSAGPANKLpciigtmsqatcnTTNLQLHHNFRWVLTANH-MEPVKGFLGRFLRRRLF 2531
Cdd:smart00382   82 LILDEIT--SLLDAEQEALLLLLEELRL-------------LLLLKSEKNLTVILTTNDeKDLGPALLRRRFDRRIV 143
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
985-1182 2.96e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   985 APQLLQSPSSggLPKPiAAIKGTSKLPSLGGGAGHLPAAE-SQQNQQLlkretsdissnisQPPPAEPPISThahihQNQ 1063
Cdd:pfam03154  380 GPSPFQMNSN--LPPP-PALKPLSSLSTHHPPSAHPPPLQlMPQSQQL-------------PPPPAQPPVLT-----QSQ 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  1064 TPPPPyyANSQPTSHiSSHGFLSEPSTPQHSSGIYGSSRLPPPksalSAPRKLEYNAGPHILSSPTHHQRQGLPRPLVNS 1143
Cdd:pfam03154  439 SLPPP--AASHPPTS-GLHQVPSQSPFPQHPFVPGGPPPITPP----SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVS 511
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 442628495  1144 APNTPTaspnkfhtipsKIVGTIYESKEEQLLPAPPPAS 1182
Cdd:pfam03154  512 CPLPPV-----------QIKEEALDEAEEPESPPPPPRS 539
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
2385-2466 1.05e-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: 47.91  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2385 LILCGPSGTGKSYLARRLAEFLVARSARgnpseaIATFNV-DHKSSKDLRQYLGHIAEQAAIANGVSELPSVIILDNLHH 2463
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNAsDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDS 95

                  ...
gi 442628495 2464 ASA 2466
Cdd:cd00009    96 LSR 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
729-1182 1.87e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  729 GGTAIPLPATVM---VQRRCPPDKVRPLPPTP-----NHTPSIPG--------LGKSGSDFNTSRPNSPPTSNHtiqslk 792
Cdd:PHA03247 2549 GDPPPPLPPAAPpaaPDRSVPPPRPAPRPSEPavtsrARRPDAPPqsarprapVDDRGDPRGPAPPSPLPPDTH------ 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  793 sgnnnslRPPsiksgiPSPSSPQTAPQKHSMLDKLKLFNKEKQQNAVNAASVASKTQIQSKRTSSSSGFSSARSERSDSS 872
Cdd:PHA03247 2623 -------APD------PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  873 LSLNDGHGSQLKPPSISVSSQKPQPKTKQSKLLAAQQKKEQANKATKLDKKEKSPA-----------RSLNKEESGNESR 941
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPagpatpggparPARPPTTAGPPAP 2769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  942 SSTMGRTG---KSSLVRAVGGVEKNTPKTSSKSSLHSKSDSKSSLKAPQLLQSPSSGGLPKPIAAIKGTSKLPSlGGGAG 1018
Cdd:PHA03247 2770 APPAAPAAgppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPP 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1019 HLPAAESQQNQQLLKRETSdissniSQPPPAEPPISTHAHIHQNQTPPPPYYANSQPTSHISSHGF----LSEPSTPQHS 1094
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPP------SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPpqpqAPPPPQPQPQ 2922
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1095 SGIYGSSRLPPPKSALSAPrKLEYNAGPHILSSPTHHQ-----------RQGLPRPLVNS-APN--TPTASPNKFHTIPS 1160
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVpqpwlgalvpgRVAVPRFRVPQpAPSreAPASSTPPLTGHSL 3001
                         490       500
                  ....*....|....*....|..
gi 442628495 1161 KIVGTIYESKEEQLLPAPPPAS 1182
Cdd:PHA03247 3002 SRVSSWASSLALHEETDPPPVS 3023
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
2364-2411 5.10e-03

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 41.99  E-value: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442628495 2364 DSLIPRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLVARSA 2411
Cdd:PRK11331  176 DLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA 223
 
Name Accession Description Interval E-value
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
535-638 3.72e-43

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: 153.51  E-value: 3.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21212     3 EIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGV-DVQGI 81
                          90       100
                  ....*....|....*....|....
gi 442628495  615 TTNDICAGRLKAVLALFFALSRFK 638
Cdd:cd21212    82 TAEDIVDGNLKAILGLFFSLSRYK 105
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
533-644 3.05e-29

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: 114.29  E-value: 3.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  533 YMEIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLE 612
Cdd:cd21285    11 DKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGI-NIQ 89
                          90       100       110
                  ....*....|....*....|....*....|..
gi 442628495  613 NITTNDICAGRLKAVLALFFALSRFKQQAKQT 644
Cdd:cd21285    90 GLSAEEIRNGNLKAILGLFFSLSRYKQQQQQP 121
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
535-638 6.04e-28

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: 110.12  E-value: 6.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21286     3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGV-NVQGL 81
                          90       100
                  ....*....|....*....|....
gi 442628495  615 TTNDICAGRLKAVLALFFALSRFK 638
Cdd:cd21286    82 SAEEIRNGNLKAILGLFFSLSRYK 105
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
537-638 1.99e-16

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: 76.95  E-value: 1.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21213     5 YVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRI-RMHQTSA 83
                          90       100
                  ....*....|....*....|...
gi 442628495  617 NDICAGRLKAVLALFFAL-SRFK 638
Cdd:cd21213    84 KDIVDGNLKAIMRLILALaAHFK 106
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
534-636 1.34e-14

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: 71.60  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  534 MEIYTDWANYYLERaKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVGGLEN 613
Cdd:cd00014     1 EEELLKWINEVLGE-ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLPELDL 79
                          90       100
                  ....*....|....*....|....
gi 442628495  614 ITTNDI-CAGRLKAVLALFFALSR 636
Cdd:cd00014    80 FEPEDLyEKGNLKKVLGTLWALAL 103
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
537-634 6.79e-13

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: 67.31  E-value: 6.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLEraKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21227     9 FTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGI-KLVNIGN 85
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21227    86 EDIVNGNLKLILGLIWHL 103
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
535-636 1.73e-12

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: 66.16  E-value: 1.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   535 EIYTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTsfkvPDLVKK---PKNQQQMFDNVNSCLHVLRsQSVG-G 610
Cdd:pfam00307    5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLA----PGLVDKkklNKSEFDKLENINLALDVAE-KKLGvP 79
                           90       100
                   ....*....|....*....|....*.
gi 442628495   611 LENITTNDICAGRLKAVLALFFALSR 636
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFR 105
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
537-634 6.19e-12

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: 64.34  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLEraKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21215     9 FTKWLNTKLS--SRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGV-KLTNIGA 85
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21215    86 EDIVDGNLKLILGLLWTL 103
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
537-634 8.32e-09

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: 55.92  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKskRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVGGLENITT 616
Cdd:cd21311    20 FTRWANEHLKTAN--KHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEDEGIKIVNIDS 97
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21311    98 SDIVDGKLKLILGLIWTL 115
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
537-630 1.84e-08

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: 54.61  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKrkVTDLSADCRDGLLLAEVIEAVTSFKVPdlvkKPKNQQ---QMFDNVNSCLHVLRSQSvgGLEN 613
Cdd:cd21193    21 FTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEKLG----KPNRGRlrvQKIENVNKALAFLKTKV--RLEN 92
                          90
                  ....*....|....*..
gi 442628495  614 ITTNDICAGRLKAVLAL 630
Cdd:cd21193    93 IGAEDIVDGNPRLILGL 109
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
537-636 7.90e-08

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: 52.92  E-value: 7.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAkSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKK-PKNQQQMFDNVNSCLHVLRSQSVGGLENIT 615
Cdd:cd21225     9 FTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSGKKFPKKFDLePKNRIQMIQNLHLAMLFIEEDLKIRVQGIG 87
                          90       100
                  ....*....|....*....|.
gi 442628495  616 TNDICAGRLKAVLALFFALSR 636
Cdd:cd21225    88 AEDFVDNNKKLILGLLWTLYR 108
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
537-634 4.89e-07

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: 51.21  E-value: 4.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKrkVTDLSADCRDGLLLAEVIEAVTSFKVPdlvKKPKNQQQM--FDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21317    36 FTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQLP---KPTKGRMRIhcLENVDKALQFLKEQKV-HLENM 109
                          90       100
                  ....*....|....*....|
gi 442628495  615 TTNDICAGRLKAVLALFFAL 634
Cdd:cd21317   110 GSHDIVDGNHRLTLGLIWTI 129
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
528-630 4.90e-07

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: 50.48  E-value: 4.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  528 DSVQgyMEIYTDWANYYLEraKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDlvKKPKNQQQMFDNVNSCLHVLRSQS 607
Cdd:cd21188     1 DAVQ--KKTFTKWVNKHLI--KARRRVVDLFEDLRDGHNLISLLEVLSGESLPR--ERGRMRFHRLQNVQTALDFLKYRK 74
                          90       100
                  ....*....|....*....|...
gi 442628495  608 VgGLENITTNDICAGRLKAVLAL 630
Cdd:cd21188    75 I-KLVNIRAEDIVDGNPKLTLGL 96
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
2368-2597 6.17e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 54.78  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2368 PRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLvarSARGNPSEAIATFNVDHKSSKDLRQYL----------- 2436
Cdd:COG1401   207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEAL---GGEDNGRIEFVQFHPSWSYEDFLLGYRpsldegkyept 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2437 -GHIAEQAAIANGVSELPSVIILD--NLHHAS-ALGDVFScLLSAG----------PANKLPC---------IIGTMsqa 2493
Cdd:COG1401   284 pGIFLRFCLKAEKNPDKPYVLIIDeiNRANVEkYFGELLS-LLESDkrgeelsielPYSGEGEefsippnlyIIGTM--- 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2494 tcNT--TNLqlhhnfrwvltanhmepvkGFLGRFLRRRlFQLEL----QTQHPQPELAAVLawlpsvwQHINRFLEvhsS 2567
Cdd:COG1401   360 --NTddRSL-------------------ALSDKALRRR-FTFEFldpdLDKLSNEEVVDLL-------EELNEILE---K 407
                         250       260       270
                  ....*....|....*....|....*....|
gi 442628495 2568 SDVTIGPRLFLACPMDLKDSQVWFTDIWNY 2597
Cdd:COG1401   408 RDFQIGHRALLLLDGLLSGDLDLLLLLLLL 437
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
528-634 6.92e-07

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: 50.79  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  528 DSVQgyMEIYTDWANYYLERAKSKrkVTDLSADCRDGLLLAEVIEAVTSFKVPdlvkKP---KNQQQMFDNVNSCLHVLR 604
Cdd:cd21318    36 EAVQ--KKTFTKWVNSHLARVPCR--INDLYTDLRDGYVLTRLLEVLSGEQLP----KPtrgRMRIHSLENVDKALQFLK 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 442628495  605 SQSVgGLENITTNDICAGRLKAVLALFFAL 634
Cdd:cd21318   108 EQRV-HLENVGSHDIVDGNHRLTLGLIWTI 136
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
537-630 7.83e-07

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: 50.07  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPdlVKKPKNQQQM--FDNVNSCLHVLRSQSVgGLENI 614
Cdd:cd21241    10 FTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLP--CEKGRRLKRVhfLSNINTALKFLESKKI-KLVNI 86
                          90
                  ....*....|....*.
gi 442628495  615 TTNDICAGRLKAVLAL 630
Cdd:cd21241    87 NPTDIVDGKPSIVLGL 102
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
537-634 8.57e-07

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: 49.79  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKskRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLV-KKPKNQQQMFDNVNSCLHVLRSQSVgGLENIT 615
Cdd:cd21228     9 FTRWCNEHLKCVN--KRIYNLETDLSDGLRLIALLEVLSQKRMYKKYnKRPTFRQMKLENVSVALEFLERESI-KLVSID 85
                          90
                  ....*....|....*....
gi 442628495  616 TNDICAGRLKAVLALFFAL 634
Cdd:cd21228    86 SSAIVDGNLKLILGLIWTL 104
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
537-634 9.79e-07

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: 50.81  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKrkVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKpKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21316    58 FTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLPKPTKG-RMRIHCLENVDKALQFLKEQRV-HLENMGS 133
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21316   134 HDIVDGNHRLTLGLIWTI 151
AAA_22 pfam13401
AAA domain;
2385-2476 1.04e-06

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 50.03  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  2385 LILCGPSGTGKSYLARRLAEFLVARSAR---------GNPSE---AIAT-FNVDHKSSKDLRQYLGHIAEQAAIANgvse 2451
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvdlpsgTSPKDllrALLRaLGLPLSGRLSKEELLAALQQLLLALA---- 83
                           90       100       110
                   ....*....|....*....|....*....|...
gi 442628495  2452 LPSVIILDNLHHASA--------LGDVFSCLLS 2476
Cdd:pfam13401   84 VAVVLIIDEAQHLSLealeelrdLLNLSSKLLQ 116
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
528-630 1.04e-06

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: 49.67  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  528 DSVQGymEIYTDWANYYLERAKSKrkVTDLSADCRDGLLLAEVIEAVTSFKVPDlVKKPKNQQQMFDNVNSCLHVLRSQS 607
Cdd:cd21246    14 EAVQK--KTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPK-PTKGKMRIHCLENVDKALQFLKEQR 88
                          90       100
                  ....*....|....*....|...
gi 442628495  608 VgGLENITTNDICAGRLKAVLAL 630
Cdd:cd21246    89 V-HLENMGSHDIVDGNHRLTLGL 110
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
537-630 1.60e-06

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: 48.92  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAkSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDlvKKPKNQQQMFDNVNSCLHVLRSQSVGgLENITT 616
Cdd:cd21186     7 FTKWINSQLSKA-NKPPIKDLFEDLRDGTRLLALLEVLTGKKLKP--EKGRMRVHHLNNVNRALQVLEQNNVK-LVNISS 82
                          90
                  ....*....|....
gi 442628495  617 NDICAGRLKAVLAL 630
Cdd:cd21186    83 NDIVDGNPKLTLGL 96
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
537-634 1.67e-06

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: 49.11  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21190    10 FTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCI-KLVNINS 88
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21190    89 TDIVDGKPSIVLGLIWTI 106
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
2382-2531 1.67e-06

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: 50.06  E-value: 1.67e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   2382 HRRLILCGPSGTGKSYLARRLAEFLVARSAR-----GNPSEAIATFNVDHKSSKDLRQYLGHIAEQA-AIANGVSELPSV 2455
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRlALALARKLKPDV 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628495   2456 IILDNLHhaSALGDVFSCLLSAGPANKLpciigtmsqatcnTTNLQLHHNFRWVLTANH-MEPVKGFLGRFLRRRLF 2531
Cdd:smart00382   82 LILDEIT--SLLDAEQEALLLLLEELRL-------------LLLLKSEKNLTVILTTNDeKDLGPALLRRRFDRRIV 143
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
554-634 2.53e-06

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: 48.36  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  554 VTDLSADCRDGLLLAEVIEAVTSFkvPDLVKKPKN-----QQQMFdNVNSCLHVLRSQSVGGLE---NITTNDICAGRLK 625
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLTGD--WSLLSKLRVpaisrLQKLH-NVEVALKALKEAGVLRGGdggGITAKDIVDGHRE 102

                  ....*....
gi 442628495  626 AVLALFFAL 634
Cdd:cd21223   103 KTLALLWRI 111
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
985-1182 2.96e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 53.23  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495   985 APQLLQSPSSggLPKPiAAIKGTSKLPSLGGGAGHLPAAE-SQQNQQLlkretsdissnisQPPPAEPPISThahihQNQ 1063
Cdd:pfam03154  380 GPSPFQMNSN--LPPP-PALKPLSSLSTHHPPSAHPPPLQlMPQSQQL-------------PPPPAQPPVLT-----QSQ 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  1064 TPPPPyyANSQPTSHiSSHGFLSEPSTPQHSSGIYGSSRLPPPksalSAPRKLEYNAGPHILSSPTHHQRQGLPRPLVNS 1143
Cdd:pfam03154  439 SLPPP--AASHPPTS-GLHQVPSQSPFPQHPFVPGGPPPITPP----SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVS 511
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 442628495  1144 APNTPTaspnkfhtipsKIVGTIYESKEEQLLPAPPPAS 1182
Cdd:pfam03154  512 CPLPPV-----------QIKEEALDEAEEPESPPPPPRS 539
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
537-634 4.90e-06

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: 47.48  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLeRAKSKRkVTDLSADCRDGLLLAEVIEAVTSFKV-PDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENIT 615
Cdd:cd21183     9 FTRWCNEHL-KERGMQ-IHDLATDFSDGLCLIALLENLSTRPLkRSYNRRPAFQQHYLENVSTALKFIEADHI-KLVNIG 85
                          90
                  ....*....|....*....
gi 442628495  616 TNDICAGRLKAVLALFFAL 634
Cdd:cd21183    86 SGDIVNGNIKLILGLIWTL 104
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
2385-2533 5.62e-06

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: 47.97  E-value: 5.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  2385 LILCGPSGTGKSYLARRLAEFLVARSARGNPSEAIATFNVDhkSSKDLRQYLGHIAEQAaiangvselPSVIILDNLHHA 2464
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGE--SEKRLRELFEAAKKLA---------PCVIFIDEIDAL 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  2465 SALGDVFSCLLSAGPANKLpciIGTMSQATCNTtnlqlhHNFRWVLTANHMEPV-KGFLGRFLRRRLFQL 2533
Cdd:pfam00004   70 AGSRGSGGDSESRRVVNQL---LTELDGFTSSN------SKVIVIAATNRPDKLdPALLGRFDRIIEFPL 130
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
552-637 7.00e-06

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


Pssm-ID: 409068  Cd Length: 113  Bit Score: 47.28  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  552 RKVTDLSADCRDGLLLAEVIEAVTSFKV---PDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITTNDICAGRLKAVL 628
Cdd:cd21219    20 PLINNLYEDLRDGLVLLQVLDKIQPGCVnwkKVNKPKPLNKFKKVENCNYAVDLAKKLGF-SLVGIGGKDIADGNRKLTL 98

                  ....*....
gi 442628495  629 ALFFALSRF 637
Cdd:cd21219    99 ALVWQLMRY 107
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
2385-2466 1.05e-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: 47.91  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2385 LILCGPSGTGKSYLARRLAEFLVARSARgnpseaIATFNV-DHKSSKDLRQYLGHIAEQAAIANGVSELPSVIILDNLHH 2463
Cdd:cd00009    22 LLLYGPPGTGKTTLARAIANELFRPGAP------FLYLNAsDLLEGLVVAELFGHFLVRLLFELAEKAKPGVLFIDEIDS 95

                  ...
gi 442628495 2464 ASA 2466
Cdd:cd00009    96 LSR 98
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
537-634 1.33e-05

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: 46.36  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDlvKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21242    10 FTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPR--EKGHNVFQCRSNIETALSFLKNKSI-KLINIHV 86
                          90
                  ....*....|....*...
gi 442628495  617 NDICAGRLKAVLALFFAL 634
Cdd:cd21242    87 PDIIEGKPSIILGLIWTI 104
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
537-630 7.61e-05

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


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 44.49  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAK--SKRKVTDLSAD-----CRDGLLLAEVIEAVtsfkVPDLV-------KKPKNQQQMFDNVNsclHV 602
Cdd:cd21217     6 FVEHINSLLADDPdlKHLLPIDPDGDdlfeaLRDGVLLCKLINKI----VPGTIderklnkKKPKNIFEATENLN---LA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 442628495  603 LRS-QSVGG-LENITTNDICAGRLKAVLAL 630
Cdd:cd21217    79 LNAaKKIGCkVVNIGPQDILDGNPHLVLGL 108
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
528-634 8.35e-05

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: 44.25  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  528 DSVQgyMEIYTDWANYYLerAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDlvKKPKNQQQMFDNVNSCLHVLRSQS 607
Cdd:cd21235     4 DRVQ--KKTFTKWVNKHL--IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQ 77
                          90       100
                  ....*....|....*....|....*..
gi 442628495  608 VgGLENITTNDICAGRLKAVLALFFAL 634
Cdd:cd21235    78 V-KLVNIRNDDIADGNPKLTLGLIWTI 103
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
528-634 1.21e-04

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: 43.87  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  528 DSVQgyMEIYTDWANYYLerAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDlvKKPKNQQQMFDNVNSCLHVLRSQS 607
Cdd:cd21237     4 DRVQ--KKTFTKWVNKHL--MKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPR--EKGRMRFHRLQNVQIALDFLKQRQ 77
                          90       100
                  ....*....|....*....|....*..
gi 442628495  608 VgGLENITTNDICAGRLKAVLALFFAL 634
Cdd:cd21237    78 V-KLVNIRNDDITDGNPKLTLGLIWTI 103
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
537-639 1.41e-04

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: 43.72  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKSKRKVTDLSADCRDGLLLAEVIEAVTSFKVPDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENITT 616
Cdd:cd21191    10 FTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNV-KLVSIDA 88
                          90       100
                  ....*....|....*....|...
gi 442628495  617 NDICAGRLKAVLALFFALSRFKQ 639
Cdd:cd21191    89 AEIADGNPSLVLGLIWNIILFFQ 111
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1023-1186 1.47e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  1023 AESQQNQQLLKRETSDISSNISQPPPAEPPISTHAHIHQNQTPPPPYYANSQPTSHISSHGFLSEPSTPQHSSGIYGSS- 1101
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTl 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  1102 ---RLPPPKSALS--APRKLEYNAGPHILSSPTHH-QRQGLPRPLVNSAPNTPtaspnkfHTIPSKIVGTIYESKEEQLL 1175
Cdd:pfam03154  238 hpqRLPSPHPPLQpmTQPPPPSQVSPQPLPQPSLHgQMPPMPHSLQTGPSHMQ-------HPVPPQPFPLTPQSSQSQVP 310
                          170
                   ....*....|.
gi 442628495  1176 PAPPPASGGSS 1186
Cdd:pfam03154  311 PGPSPAAPGQS 321
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
537-634 1.90e-04

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: 43.48  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLEraKSKRKVTDLSADCRDGLLLAEVIEAVTSFKV-PDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENIT 615
Cdd:cd21310    21 FTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKMyRKYHPRPNFRQMKLENVSVALEFLDREHI-KLVSID 97
                          90
                  ....*....|....*....
gi 442628495  616 TNDICAGRLKAVLALFFAL 634
Cdd:cd21310    98 SKAIVDGNLKLILGLIWTL 116
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
535-630 3.62e-04

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: 42.29  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  535 EIYTDWANYYLERAKSKRK-VTDLSADCRDGLLLAEVIEAVT-SFKVPDLVKKPKNQQQMFDNVNsclHVLRS-QSVGGL 611
Cdd:cd21218    13 EILLRWVNYHLKKAGPTKKrVTNFSSDLKDGEVYALLLHSLApELCDKELVLEVLSEEDLEKRAE---KVLQAaEKLGCK 89
                          90
                  ....*....|....*....
gi 442628495  612 ENITTNDICAGRLKAVLAL 630
Cdd:cd21218    90 YFLTPEDIVSGNPRLNLAF 108
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
537-634 5.34e-04

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: 42.38  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  537 YTDWANYYLERAKskRKVTDLSADCRDGLLLAEVIEAVTSFKV-PDLVKKPKNQQQMFDNVNSCLHVLRSQSVgGLENIT 615
Cdd:cd21308    25 FTRWCNEHLKCVS--KRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESI-KLVSID 101
                          90
                  ....*....|....*....
gi 442628495  616 TNDICAGRLKAVLALFFAL 634
Cdd:cd21308   102 SKAIVDGNLKLILGLIWTL 120
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
2385-2406 1.31e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.82  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|..
gi 442628495 2385 LILCGPSGTGKSYLARRLAEFL 2406
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERL 23
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
2369-2408 1.37e-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: 41.88  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 442628495 2369 RSIVHRYISLLteHRRLILCGPSGTGKSYLARRLAEFLVA 2408
Cdd:cd19481    15 GSRLRRYGLGL--PKGILLYGPPGTGKTLLAKALAGELGL 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
729-1182 1.87e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  729 GGTAIPLPATVM---VQRRCPPDKVRPLPPTP-----NHTPSIPG--------LGKSGSDFNTSRPNSPPTSNHtiqslk 792
Cdd:PHA03247 2549 GDPPPPLPPAAPpaaPDRSVPPPRPAPRPSEPavtsrARRPDAPPqsarprapVDDRGDPRGPAPPSPLPPDTH------ 2622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  793 sgnnnslRPPsiksgiPSPSSPQTAPQKHSMLDKLKLFNKEKQQNAVNAASVASKTQIQSKRTSSSSGFSSARSERSDSS 872
Cdd:PHA03247 2623 -------APD------PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  873 LSLNDGHGSQLKPPSISVSSQKPQPKTKQSKLLAAQQKKEQANKATKLDKKEKSPA-----------RSLNKEESGNESR 941
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPagpatpggparPARPPTTAGPPAP 2769
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  942 SSTMGRTG---KSSLVRAVGGVEKNTPKTSSKSSLHSKSDSKSSLKAPQLLQSPSSGGLPKPIAAIKGTSKLPSlGGGAG 1018
Cdd:PHA03247 2770 APPAAPAAgppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPP-GPPPP 2848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1019 HLPAAESQQNQQLLKRETSdissniSQPPPAEPPISTHAHIHQNQTPPPPYYANSQPTSHISSHGF----LSEPSTPQHS 1094
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPP------SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPpqpqAPPPPQPQPQ 2922
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 1095 SGIYGSSRLPPPKSALSAPrKLEYNAGPHILSSPTHHQ-----------RQGLPRPLVNS-APN--TPTASPNKFHTIPS 1160
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQP-PLAPTTDPAGAGEPSGAVpqpwlgalvpgRVAVPRFRVPQpAPSreAPASSTPPLTGHSL 3001
                         490       500
                  ....*....|....*....|..
gi 442628495 1161 KIVGTIYESKEEQLLPAPPPAS 1182
Cdd:PHA03247 3002 SRVSSWASSLALHEETDPPPVS 3023
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
2385-2460 3.55e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 40.37  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495  2385 LILCGPSGTGKSYLARRLAEFL---------VARSARGNPSEAIATFNvdhKSSKDLRQYLGHIAEQAAiANGVSelpsv 2455
Cdd:pfam13671    2 ILLVGLPGSGKSTLARRLLEELgavrlssddERKRLFGEGRPSISYYT---DATDRTYERLHELARIAL-RAGRP----- 72

                   ....*
gi 442628495  2456 IILDN 2460
Cdd:pfam13671   73 VILDA 77
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
2373-2468 4.98e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 41.41  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2373 HRYISLLTEH-----RRLILCGPSGTGKSYLARRLAE-----FLVARsargnPSEAIatfnvdhkSSkdlrqYLGHIAEQ 2442
Cdd:COG1223    21 LRRRENLRKFglwppRKILFYGPPGTGKTMLAEALAGelklpLLTVR-----LDSLI--------GS-----YLGETARN 82
                          90       100
                  ....*....|....*....|....*..
gi 442628495 2443 -AAIANGVSELPSVIILDNLHhasALG 2468
Cdd:COG1223    83 lRKLFDFARRAPCVIFFDEFD---AIA 106
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
2364-2411 5.10e-03

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 41.99  E-value: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442628495 2364 DSLIPRSIVHRYISLLTEHRRLILCGPSGTGKSYLARRLAEFLVARSA 2411
Cdd:PRK11331  176 DLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA 223
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
2386-2406 5.68e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 5.68e-03
                          10        20
                  ....*....|....*....|.
gi 442628495 2386 ILCGPSGTGKSYLARRLAEFL 2406
Cdd:COG0542   583 LFLGPTGVGKTELAKALAEFL 603
COG3903 COG3903
Predicted ATPase [General function prediction only];
2378-2479 6.03e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 42.31  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2378 LLTEHRRLILCGPSGTGKSYLARRLAEFLVARSARG----------NPSEAIATF----NVDHKSSKDLR-QYLGHIAEQ 2442
Cdd:COG3903   172 LLSAARLVTLTGPGGVGKTRLALEVAHRLADRFPDGvwfvdlagvtDPALVLAAVaralGVRDAPGRDPAaRLRAALADR 251
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 442628495 2443 aaiangvselPSVIILDNL-HHASALGDVFSCLLSAGP 2479
Cdd:COG3903   252 ----------RLLLVLDNCeHVVDAAAALVRPLLPAAP 279
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
2385-2410 7.16e-03

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.20  E-value: 7.16e-03
                           10        20
                   ....*....|....*....|....*.
gi 442628495  2385 LILCGPSGTGKSYLARRLAEFLVARS 2410
Cdd:pfam07728    2 VLLVGPPGTGKTELAERLAAALSNRP 27
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
2383-2459 8.12e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 39.54  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628495 2383 RRLILCGPSGTGKSYLARRLAEFLvarsargNPSEAIATFNVDHKSSKDLRQYLGHIA--------EQ--AAIANGVSEL 2452
Cdd:cd00267    26 EIVALVGPNGSGKSTLLRAIAGLL-------KPTSGEILIDGKDIAKLPLEELRRRIGyvpqlsggQRqrVALARALLLN 98

                  ....*..
gi 442628495 2453 PSVIILD 2459
Cdd:cd00267    99 PDLLLLD 105
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
2379-2404 9.99e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 41.05  E-value: 9.99e-03
                          10        20
                  ....*....|....*....|....*.
gi 442628495 2379 LTEHRRLILCGPSGTGKSYLARRLAE 2404
Cdd:COG0464   188 LPPPRGLLLYGPPGTGKTLLARALAG 213
 
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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