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Conserved domains on  [gi|1370460505|ref|XP_024304511|]
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dixin isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
21-127 1.12e-66

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: 213.31  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80
                          90       100
                  ....*....|....*....|....*..
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
564-639 5.60e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


:

Pssm-ID: 459936  Cd Length: 77  Bit Score: 132.27  E-value: 5.60e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
244-443 6.73e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 244 EEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLII-IQSRLDQSMEENQDLKKELLK 322
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370460505 403 KLEEALRKLSDvsyHQVDLERELEHKDVLLAHCMKREADEA 443
Cdd:COG1196   415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEA 452
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
21-127 1.12e-66

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: 213.31  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80
                          90       100
                  ....*....|....*....|....*..
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
564-639 5.60e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 132.27  E-value: 5.60e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
564-640 4.00e-20

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 85.16  E-value: 4.00e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370460505  564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 640
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
23-126 9.73e-20

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: 84.65  E-value: 9.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  23 QAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgNQQEMKNNVEKVLQFvASKKIRMHQTS 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-SEFDKLENINLALDV-AEKKLGVPKVL 82
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 103 --AKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:pfam00307  83 iePEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
24-124 8.57e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 64.64  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505   24 AYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMHQTS 102
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKiENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 1370460505  103 AKDIVDGNlKSIMRLVLALAAH 124
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
19-125 1.39e-08

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 58.03  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  19 SQQLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRM 98
Cdd:COG5069     8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKL 86
                          90       100
                  ....*....|....*....|....*..
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:COG5069    87 FNIGPQDIVDGNPKLILGLIWSLISRL 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
244-443 6.73e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 244 EEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLII-IQSRLDQSMEENQDLKKELLK 322
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370460505 403 KLEEALRKLSDvsyHQVDLERELEHKDVLLAHCMKREADEA 443
Cdd:COG1196   415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
245-427 2.62e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  245 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 322
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                          170       180
                   ....*....|....*....|....*
gi 1370460505  403 KLEEALRKLSDVSYHQVDLERELEH 427
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLER 411
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
241-445 9.47e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 9.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  241 TSWEEQLLEQQEYLEKEMEE--AKKM--------ISGLQALLlngslpeDEQERPLAlcepGVNPEeqLIIIQSRLDQSM 310
Cdd:pfam15921  464 SSLTAQLESTKEMLRKVVEEltAKKMtlessertVSDLTASL-------QEKERAIE----ATNAE--ITKLRSRVDLKL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  311 EENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNR 381
Cdd:pfam15921  531 QELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRL 604
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370460505  382 LLGEYKKELGQKDrllqqhqAKLEEALRKLSDVSYHQVDL-----ERELEHKDVllahcmKREADEATN 445
Cdd:pfam15921  605 ELQEFKILKDKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
21-127 1.12e-66

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: 213.31  E-value: 1.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80
                          90       100
                  ....*....|....*....|....*..
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFKP 127
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
564-639 5.60e-37

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 132.27  E-value: 5.60e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370460505 564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWV 639
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
21-125 1.96e-28

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: 109.21  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....*
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
564-640 4.00e-20

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 85.16  E-value: 4.00e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370460505  564 TKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEIFHDDDAIPGWEGKIVAWVE 640
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
23-126 9.73e-20

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: 84.65  E-value: 9.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  23 QAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgNQQEMKNNVEKVLQFvASKKIRMHQTS 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNK-SEFDKLENINLALDV-AEKKLGVPKVL 82
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 103 --AKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:pfam00307  83 iePEDLVEGDNKSVLTYLASLFRRFQ 108
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
21-125 5.33e-19

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: 82.72  E-value: 5.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21227     5 QKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEILQGRKLGRVIKKPLNQHQKLENVTLALKAMAEDGIKLVN 82
                          90       100
                  ....*....|....*....|....*
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21227    83 IGNEDIVNGNLKLILGLIWHLILRY 107
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
25-122 5.78e-19

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: 82.39  E-value: 5.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  25 YVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSAK 104
Cdd:cd21286     5 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 84
                          90
                  ....*....|....*...
gi 1370460505 105 DIVDGNLKSIMRLVLALA 122
Cdd:cd21286    85 EIRNGNLKAILGLFFSLS 102
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
20-118 1.62e-18

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


Pssm-ID: 409063  Cd Length: 105  Bit Score: 81.28  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  20 QQLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKK 95
Cdd:cd21214     5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVISGE-----RLPKPERGKMRfhkiANVNKALDFIASKG 77
                          90       100
                  ....*....|....*....|...
gi 1370460505  96 IRMHQTSAKDIVDGNLKSIMRLV 118
Cdd:cd21214    78 VKLVSIGAEEIVDGNLKMTLGMI 100
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
21-125 5.04e-18

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: 79.75  E-value: 5.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPavKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21215     5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTN 82
                          90       100
                  ....*....|....*....|....*
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21215    83 IGAEDIVDGNLKLILGLLWTLILRF 107
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
17-122 9.42e-18

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: 79.62  E-value: 9.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  17 EPSQQLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKI 96
Cdd:cd21285     7 ENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGI 86
                          90       100
                  ....*....|....*....|....*.
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALA 122
Cdd:cd21285    87 NIQGLSAEEIRNGNLKAILGLFFSLS 112
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
22-122 8.45e-17

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: 76.22  E-value: 8.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  22 LQAYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKI-RMHQ 100
Cdd:cd00014     1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENINLFLNACKKLGLpELDL 79
                          90       100
                  ....*....|....*....|...
gi 1370460505 101 TSAKDIV-DGNLKSIMRLVLALA 122
Cdd:cd00014    80 FEPEDLYeKGNLKKVLGTLWALA 102
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
21-126 2.55e-15

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: 72.03  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKK--RPavkPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASK 94
Cdd:cd21186     3 QKKTFTKWINSQLSKanKP---PIKDLFEDLRDGTRLLALLEVLTGKKL------KPEKGRMRvhhlNNVNRALQVLEQN 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370460505  95 KIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21186    74 NVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
21-126 4.14e-15

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 71.28  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21188     4 QKKTFTKWVNKHLIK--ARRRVVDLFEDLRDGHNLISLLEVLSGESL------PRERGRMRfhrlQNVQTALDFLKYRKI 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21188    76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
21-126 1.52e-13

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: 67.40  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQlspGNQqeMK-----NNVEKVLQFVASKK 95
Cdd:cd21241     6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEK---GRR--LKrvhflSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370460505  96 IRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
21-125 1.68e-13

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: 67.16  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSpgNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21242     6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGH--NVFQCRSNIETALSFLKNKSIKLIN 83
                          90       100
                  ....*....|....*....|....*
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21242    84 IHVPDIIEGKPSIILGLIWTIILHF 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
21-121 2.28e-13

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 66.79  E-value: 2.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLS-GVQLSPGNQQEMKNNVEKVLQFVASK-KIRM 98
Cdd:cd21225     5 QIKAFTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSGKKFPkKFDLEPKNRIQMIQNLHLAMLFIEEDlKIRV 83
                          90       100
                  ....*....|....*....|...
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLAL 121
Cdd:cd21225    84 QGIGAEDFVDNNKKLILGLLWTL 106
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
21-126 2.60e-13

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 66.44  E-value: 2.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21190     6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21190    86 INSTDIVDGKPSIVLGLIWTIILYFQ 111
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
21-125 4.84e-13

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: 65.58  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGV-QLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21183     5 QANTFTRWCNEHLKERGMQ--IHDLATDFSDGLCLIALLENLSTRPLKRSyNRRPAFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
24-124 8.57e-13

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 64.64  E-value: 8.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505   24 AYVAWVNAQLKKRPAVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMHQTS 102
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKiENINLALSFAEKLGGKVVLFE 80
                           90       100
                   ....*....|....*....|..
gi 1370460505  103 AKDIVDGNlKSIMRLVLALAAH 124
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
21-121 9.86e-13

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 65.08  E-value: 9.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21246    17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEVLSGERLP-----KPTKGKMRihclENVDKALQFLKEQRV 89
                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21246    90 HLENMGSHDIVDGN----HRLTLGL 110
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
21-121 1.59e-12

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 65.05  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21318    39 QKKTFTKWVNSHLARVPC--RINDLYTDLRDGYVLTRLLEVLSGE-----QLPKPTRGRMRihslENVDKALQFLKEQRV 111
                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21318   112 HLENVGSHDIVDGN----HRLTLGL 132
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
21-121 4.96e-12

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: 63.08  E-value: 4.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKlsgvqLSPGNQQEMK----NNVEKVLQFVASkKI 96
Cdd:cd21193    17 QKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEK-----LGKPNRGRLRvqkiENVNKALAFLKT-KV 88
                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21193    89 RLENIGAEDIVDGN----PRLILGL 109
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
21-125 1.01e-11

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: 61.74  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21228     5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRMyKKYNKRPTFRQMKLENVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
28-121 2.92e-11

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: 60.78  E-value: 2.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  28 WVNAQLKKR-PAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLS-PGNQQEMKNNVEKVLQFVASKKIRMHqTSAKD 105
Cdd:cd21218    18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLeVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED 96
                          90
                  ....*....|....*.
gi 1370460505 106 IVDGNLKSIMRLVLAL 121
Cdd:cd21218    97 IVSGNPRLNLAFVATL 112
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
21-121 1.44e-10

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: 59.30  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21317    32 QKKTFTKWVNSHLAR--VTCRIGDLYTDLRDGRMLIRLLEVLSGE-----QLPKPTKGRMRihclENVDKALQFLKEQKV 104
                          90       100
                  ....*....|....*....|....*
gi 1370460505  97 RMHQTSAKDIVDGNlksiMRLVLAL 121
Cdd:cd21317   105 HLENMGSHDIVDGN----HRLTLGL 125
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
21-125 1.53e-10

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: 59.00  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVAS-KKIRMH 99
Cdd:cd21311    16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEEdEGIKIV 93
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHY 119
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
21-126 4.79e-10

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: 57.20  E-value: 4.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21191     6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVS 85
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21191    86 IDAAEIADGNPSLVLGLIWNIILFFQ 111
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
21-125 9.36e-10

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 56.96  E-value: 9.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMK-NNVEKVLQFVASKKIRMH 99
Cdd:cd21310    17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPRPNFRQMKlENVSVALEFLDREHIKLV 94
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHY 120
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
26-125 3.17e-09

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


Pssm-ID: 409153  Cd Length: 107  Bit Score: 54.62  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  26 VAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGV---QLSPGNQQEMKNNVEKVLQFVASKKIRMHQTS 102
Cdd:cd21304     7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLEVAevtQSEVGQKQKLRTVLDKINRILNLPRWSQQKWS 84
                          90       100
                  ....*....|....*....|...
gi 1370460505 103 AKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21304    85 VDSIHSKNLVAILHLLVALARHF 107
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
21-126 3.82e-09

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


Pssm-ID: 409080  Cd Length: 111  Bit Score: 54.54  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21231     7 QKKTFTKWINAQFAK-FGKPPIEDLFTDLQDGRRLLELLEGLTGQKL--VKEKGSTRVHALNNVNKALQVLQKNNVDLVN 83
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21231    84 IGSADIVDGNHKLTLGLIWSIILHWQ 109
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
42-122 4.79e-09

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: 54.52  E-value: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  42 VQDLRQDLRDGVILAYLIEIVAGEK--LSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQT----SAKDIVDGNLKSIM 115
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVELLTGDWslLSKLRVPAISRLQKLHNVEVALKALKEAGVLRGGDgggiTAKDIVDGHREKTL 105

                  ....*..
gi 1370460505 116 RLVLALA 122
Cdd:cd21223   106 ALLWRII 112
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
21-137 5.24e-09

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 54.65  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21235     7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFKPGSSRTVNQGR 137
Cdd:cd21235    79 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
1-126 1.26e-08

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 53.83  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505   1 MGTQVVMRFNNSllptEPSQQLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEM 80
Cdd:cd21236     2 AYENVLERYKDE----RDKVQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEVLSGDTL------PREKGRM 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370460505  81 K----NNVEKVLQFVASKKIRMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21236    70 RfhrlQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
19-125 1.39e-08

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 58.03  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  19 SQQLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRM 98
Cdd:COG5069     8 KVQKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYNETPETRIHVMENVSGRLEFIKGKGVKL 86
                          90       100
                  ....*....|....*....|....*..
gi 1370460505  99 HQTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:COG5069    87 FNIGPQDIVDGNPKLILGLIWSLISRL 113
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
21-126 3.18e-08

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 51.93  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSpgNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21232     3 QKKTFTKWINARFSKS-GKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGS--TRVHALNNVNRVLQVLHQNNVELVN 79
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21232    80 IGGTDIVDGNHKLTLGLLWSIILHWQ 105
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
27-125 4.30e-08

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


Pssm-ID: 409070  Cd Length: 106  Bit Score: 51.51  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  27 AWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLsgvQLSPGNQQEM--KNNVEKVLQFVaSKKIRMHQTSAK 104
Cdd:cd21221     8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLEKLANEKL---EVPEVAQSEEgqKQKLAVVLACV-NFLLGLEEDEAR 81
                          90       100
                  ....*....|....*....|....*
gi 1370460505 105 DIVDG----NLKSIMRLVLALAAHF 125
Cdd:cd21221    82 WTVDGiynkDLVSILHLLVALAHHY 106
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
26-125 4.63e-08

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


Pssm-ID: 409071  Cd Length: 121  Bit Score: 51.82  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  26 VAWVNAQLkkRPAVKPVQDLRQDLRDGVILAYLIEIVAG--EKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSA 103
Cdd:cd21222    22 LQFVNKHL--AKLNIEVTDLATQFHDGVYLILLIGLLEGffVPLHEYHLTPSTDDEKLHNVKLALELMEDAGISTPKIRP 99
                          90       100
                  ....*....|....*....|..
gi 1370460505 104 KDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21222   100 EDIVNGDLKSILRVLYSLFSKY 121
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
23-126 7.63e-08

second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 51.20  E-value: 7.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  23 QAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGE--KLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQ 100
Cdd:cd21307    19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFfiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFP 96
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 101 TSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21307    97 VNPEDIVNGDSKATIRVLYCLFSKYK 122
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
21-126 1.07e-07

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


Pssm-ID: 409086  Cd Length: 118  Bit Score: 50.80  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPGNQQEMK----NNVEKVLQFVASKKI 96
Cdd:cd21237     7 QKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEVLSGVKL------PREKGRMRfhrlQNVQIALDFLKQRQV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21237    79 KLVNIRNDDITDGNPKLTLGLIWTIILHFQ 108
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
21-118 1.32e-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: 51.58  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvQLSPGNQQ-EMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21316    54 QKKTFTKWVNSHLARVSC--RITDLYMDLRDGRMLIKLLEVLSGERLP--KPTKGRMRiHCLENVDKALQFLKEQRVHLE 129
                          90
                  ....*....|....*....
gi 1370460505 100 QTSAKDIVDGNLKSIMRLV 118
Cdd:cd21316   130 NMGSHDIVDGNHRLTLGLI 148
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
21-125 1.61e-07

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 50.46  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKrpAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21309    18 QQNTFTRWCNEHLKC--VNKRIGNLQTDLSDGLRLIALLEVLSQKRMyRKYHQRPTFRQMQLENVSVALEFLDRESIKLV 95
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21309    96 SIDSKAIVDGNLKLILGLVWTLILHY 121
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
21-125 2.02e-07

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: 50.47  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKkrPAVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPGNQQEMKNNVEKVLQFVASKKIRMH 99
Cdd:cd21308    21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98
                          90       100
                  ....*....|....*....|....*.
gi 1370460505 100 QTSAKDIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21308    99 SIDSKAIVDGNLKLILGLIWTLILHY 124
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
244-443 6.73e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 244 EEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLII-IQSRLDQSMEENQDLKKELLK 322
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370460505 403 KLEEALRKLSDvsyHQVDLERELEHKDVLLAHCMKREADEA 443
Cdd:COG1196   415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
244-413 1.71e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 244 EEQLLEQQEYLEKEMEEAKKMISGLQALLLngslpEDEQERplalcepgvnpeeqlIIIQSRLDQSMEENQDLKKELLKC 323
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 324 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAK 403
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         170
                  ....*....|
gi 1370460505 404 LEEALRKLSD 413
Cdd:COG1196   479 LAELLEELAE 488
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
28-126 1.84e-06

third 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 46.53  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  28 WVNAQLKKRPavkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPgnqQEMKNNVEKVLQfvASKKIRM-HQTSAKDI 106
Cdd:cd21185     9 WVRQLLPDVD----VNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDP---EESENNIQRGLE--AGKSLGVePVLTAEEM 79
                          90       100
                  ....*....|....*....|
gi 1370460505 107 VDGNLKSIMrlVLALAAHFK 126
Cdd:cd21185    80 ADPEVEHLG--IMAYAAQLQ 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
245-452 1.89e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 245 EQLLEQQEYLEKEMEEAKKMISGLQALLlngslpedeQERplalcepgvnpEEQLIIIQSRLDQSMEENQDLKKELLKCK 324
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 325 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKL 404
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370460505 405 EEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNSHNSQ 452
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
245-427 2.62e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  245 EQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEqerplalcepgvnpeEQLIIIQSRLDQSMEENQDLKKELLK 322
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLeeLRLEVSELE---------------EEIEELQKELYALANEISRLEQQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  323 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQA 402
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                          170       180
                   ....*....|....*....|....*
gi 1370460505  403 KLEEALRKLSDVSYHQVDLERELEH 427
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLER 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
244-434 3.78e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  244 EEQLLEQQEYLEKEMEEAKKMISGLQALL--LNGSLPEDEQERplalcepgVNPEEQLIIIQSRLDQSMEENQDLKKELL 321
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI--------EELEAQIEQLKEELKALREALDELRAELT 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  322 KCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQ 401
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1370460505  402 AKLEEALRKLSDVSYHQVDLERELEHKDVLLAH 434
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQ 926
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
296-426 2.65e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 296 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 365
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370460505 366 ------HNQNVDLQRKLD--------ERNRLLGEYKKE---LGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELE 426
Cdd:COG3206   284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
24-118 3.24e-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: 43.33  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  24 AYVAWVNAQLKKRPAVK-------PVQDLRQDLRDGVILAYLIE-IVAG----EKLSGVqlSPGNQQEMKNNVEKVLQfv 91
Cdd:cd21217     5 AFVEHINSLLADDPDLKhllpidpDGDDLFEALRDGVLLCKLINkIVPGtideRKLNKK--KPKNIFEATENLNLALN-- 80
                          90       100
                  ....*....|....*....|....*....
gi 1370460505  92 ASKKIRMHQTS--AKDIVDGNLKSIMRLV 118
Cdd:cd21217    81 AAKKIGCKVVNigPQDILDGNPHLVLGLL 109
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
21-126 4.04e-05

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


Pssm-ID: 409096  Cd Length: 125  Bit Score: 43.59  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  21 QLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPGNQQEMK----NNVEKVLQFVASkKI 96
Cdd:cd21247    21 QKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGE-----QLPRPSRGKMRvhflENNSKAITFLKT-KV 94
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370460505  97 RMHQTSAKDIVDGNLKSIMRLVLALAAHFK 126
Cdd:cd21247    95 PVKLIGPENIVDGDRTLILGLIWIIILRFQ 124
CH_PARVB_rpt1 cd21336
first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is ...
22-125 4.20e-05

first calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409185  Cd Length: 106  Bit Score: 42.96  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  22 LQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSpgnQQEM--KNNVEKVLQFVaSKKIRMH 99
Cdd:cd21336     3 VKVLIDWINDVLVEERII--VKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVT---QSEIgqKQKLQTVLEAV-NDLLRPQ 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 1370460505 100 QTSAKDIVDG----NLKSIMRLVLALAAHF 125
Cdd:cd21336    77 GWAIKWSVDSihgkNLVAILHLLVALAMHF 106
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-414 4.41e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  292 GVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ--DTSVLQLKQELLRANMDKDELHNQN 369
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERLDASS 684
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370460505  370 VD---LQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDV 414
Cdd:COG4913    685 DDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
241-445 9.47e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 9.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  241 TSWEEQLLEQQEYLEKEMEE--AKKM--------ISGLQALLlngslpeDEQERPLAlcepGVNPEeqLIIIQSRLDQSM 310
Cdd:pfam15921  464 SSLTAQLESTKEMLRKVVEEltAKKMtlessertVSDLTASL-------QEKERAIE----ATNAE--ITKLRSRVDLKL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  311 EENQDLKKEllkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNR 381
Cdd:pfam15921  531 QELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRL 604
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370460505  382 LLGEYKKELGQKDrllqqhqAKLEEALRKLSDVSYHQVDL-----ERELEHKDVllahcmKREADEATN 445
Cdd:pfam15921  605 ELQEFKILKDKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
311-426 1.16e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  311 EENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLDERNRLLGEYK-- 387
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEal 367
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370460505  388 -KELGQKD--------RLLQQHQAKLEEALRKLSDVSYHQVDLERELE 426
Cdd:COG4913    368 lAALGLPLpasaeefaALRAEAAALLEALEEELEALEEALAEAEAALR 415
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
245-428 2.05e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  245 EQLLEQQEYLEKEMEEAKKMISGLQALL---------LNGSLpEDEQERPLALCEPGVNPEEQLIIIQSRLDQ------- 308
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKLEAEIdkllaeieeLEREI-EEERKRRDKLTEEYAELKEELEDLRAELEEvdkefae 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  309 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQrkldernrllgeykK 388
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA--------------L 448
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1370460505  389 ELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHK 428
Cdd:TIGR02169  449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
CH_PARVG_rpt1 cd21305
first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
28-125 3.24e-04

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409154  Cd Length: 106  Bit Score: 40.47  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  28 WVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKL--SGVQLSPGNQqemKNNVEKVLQFVaSKKIRMHQTSAK- 104
Cdd:cd21305     9 WINTTLKQEHIV--VKSLEEDLYDGLVLHHLLVKLAGVKLevEEIALTENAQ---KRKLTVILEAV-NQSLQLEESQLKw 82
                          90       100
                  ....*....|....*....|....
gi 1370460505 105 ---DIVDGNLKSIMRLVLALAAHF 125
Cdd:cd21305    83 sveLIHNKDLLATLHLLVAIAKHF 106
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
245-426 6.18e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 245 EQLLEQQEYLEKEMEEAKKMISGLQALLLNgslpedeQERPLALCEPGVNPEEQliIIQSRLDQSMEENQDLKKELLKCK 324
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSN-------TDTALTTLEEALSEKER--IIERLKEQREREDRERLEELESLK 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 325 QEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLDERNRLLGEYKK------------ 388
Cdd:pfam10174 475 KENKDLKEKVSALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahnaeeavrtnp 554
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370460505 389 ELGQKDRLLQQhqakleEALRKLSDVSYHQVDLERELE 426
Cdd:pfam10174 555 EINDRIRLLEQ------EVARYKEESGKAQAEVERLLG 586
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
244-443 6.61e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 6.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  244 EEQLLEQQEY-LEKEMEEAKKMISGLQALL--LNGSLPEDEQERPLALCEPgvnpEEQLIIIQSRLDqsmeeNQDLKKEL 320
Cdd:TIGR00618  564 QMQEIQQSFSiLTQCDNRSKEDIPNLQNITvrLQDLTEKLSEAEDMLACEQ----HALLRKLQPEQD-----LQDVRLHL 634
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  321 LKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQH 400
Cdd:TIGR00618  635 QQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1370460505  401 QAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMK---READEA 443
Cdd:TIGR00618  710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKelmHQARTV 755
CH_AtFIM_like_rpt2 cd21296
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
28-124 1.97e-03

second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family 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, and are probably involved in the 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. 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: 409145  Cd Length: 109  Bit Score: 38.27  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  28 WVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSgvqLSPGNQQEMKNNVEKVLQFVASKKIRMHQTsAKDIV 107
Cdd:cd21296    18 WMNFHLKKAGYKKTVTNFSSDVKDAEAYAYLLNVLAPEHCD---PATLEAKDPLERAKLVLEQAEKMNCKRYLT-AKDIV 93
                          90
                  ....*....|....*..
gi 1370460505 108 DGNlksiMRLVLALAAH 124
Cdd:cd21296    94 EGS----ANLNLAFVAQ 106
CH_PARVA_rpt1 cd21335
first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, ...
22-126 2.16e-03

first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409184  Cd Length: 115  Bit Score: 38.47  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  22 LQAYVAWVNAQLKKRPAVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSP---GNQQEMKNNVEKVlqfvaSKKIRM 98
Cdd:cd21335     8 MKVLIDWINDVLVGERII--VKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQseiAQKQKLQTVLEKI-----NETLKL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370460505  99 HQTSAKDIVDG----NLKSIMRLVLALAAHFK 126
Cdd:cd21335    81 PPRSIKWNVDSvhakSLVAILHLLVALSQYFR 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
286-426 2.24e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 286 LALCEPGVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDEL 365
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370460505 366 HNQNVDLQRKLDERNRLLGE-----YKkeLGQKDRL-LQQHQAKLEEALRKLSDVSYHQVDLERELE 426
Cdd:COG4942    89 EKEIAELRAELEAQKEELAEllralYR--LGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
296-407 2.35e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  296 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKD----------------ALQQRLTQQDTS---VLQLKQELl 356
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaereiaELEAELERLDASsddLAALEEQL- 694
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1370460505  357 ranmdkDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEA 407
Cdd:COG4913    695 ------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
245-423 2.88e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 245 EQLLEQQEYLEKEMEEAKKMISGLQALLLNgslpEDEQERPLALCEPGVNPEEQLIIIQSRLD---QSMEENQDLKKELL 321
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEK----LEKLLQLLPLYQELEALEAELAELPERLEeleERLEELRELEEELE 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 322 KCKQEARNLQGIKDALQQRLTqqdtsvLQLKQELLRANMDKDELHNQNVDLQRKLDErnrllgeykkelgqkdrlLQQHQ 401
Cdd:COG4717   167 ELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEE------------------AQEEL 222
                         170       180
                  ....*....|....*....|..
gi 1370460505 402 AKLEEALRKLSDVSYHQVDLER 423
Cdd:COG4717   223 EELEEELEQLENELEAAALEER 244
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
296-414 3.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 296 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELH-------NQ 368
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQeeleelqKE 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370460505 369 NVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDV 414
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
309-448 3.23e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 309 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 388
Cdd:COG1579     1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370460505 389 ELGQ--KDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNS 448
Cdd:COG1579    81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
296-443 4.09e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 296 EEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ----------------DTSVLQLkqeLLRAN 359
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgeraralyrsggSVSYLDV---LLGSE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 360 mDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKRE 439
Cdd:COG3883   113 -SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191

                  ....
gi 1370460505 440 ADEA 443
Cdd:COG3883   192 AAAE 195
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
306-427 4.98e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 306 LDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQ--QDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLL 383
Cdd:COG4717    83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370460505 384 GEYKkelgQKDRLLQQHQAKLEEALRKLSDVSYHQV-DLERELEH 427
Cdd:COG4717   163 EELE----ELEAELAELQEELEELLEQLSLATEEELqDLAEELEE 203
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
249-443 5.03e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 249 EQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNP-EEQLIIIQSRLDQSMEENQDLKKELLKCKQEa 327
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlARRIRALEQELAALEAELAELEKEIAELRAE- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 328 rnLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEA 407
Cdd:COG4942    99 --LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370460505 408 LRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEA 443
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEKELAELA 212
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
246-411 6.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 246 QLLEQQEYLEKEMEEAKKMISGLQALLlngslpeDEQERPLA-----LCEPGVNPEEQLIIIQSRLDQSMEENQDLKKEL 320
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAEL-------EAQKEELAellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 321 LKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlranmdkDELHNQNVDLQRKLDERNRLLGEYKKELGQKDR---LL 397
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALL-------AELEEERAALEALKAERQKLLARLEKELAELAAelaEL 218
                         170
                  ....*....|....
gi 1370460505 398 QQHQAKLEEALRKL 411
Cdd:COG4942   219 QQEAEELEALIARL 232
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
230-422 6.50e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  230 WRPGSPGTYLETSWEEQLLEQQEYLEKEMEEAKK-MISGLQA--LLLNGSLPEDEQERPLALCEPgVNPEEQLIIIQSRL 306
Cdd:TIGR00618  695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAreDALNQSLKELMHQARTVLKAR-TEAHFNNNEEVTAA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  307 DQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ---DTSVLQLKQELLRAnmDKDELHNQNVDLQRKLDERNRLL 383
Cdd:TIGR00618  774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsDEDILNLQCETLVQ--EEEQFLSRLEEKSATLGEITHQL 851
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1370460505  384 GEYKKELGQKDRLLQQhQAKLEEALRKLSDVSYHQVDLE 422
Cdd:TIGR00618  852 LKYEECSKQLAQLTQE-QAKIIQLSDKLNGINQIKIQFD 889
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
297-426 7.73e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505 297 EQLIIIQ---SRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNV- 370
Cdd:COG1579     7 RALLDLQeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeVEARIKKYEEQLGNVr 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370460505 371 ------DLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELE 426
Cdd:COG1579    87 nnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
17-118 8.49e-03

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: 36.49  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370460505  17 EPSQQLQAYVAWVNAQLKKRPavkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLS---PGNQQEMKNNVEKVLQFVAS 93
Cdd:cd21219     1 EGSREERAFRMWLNSLGLDPL----INNLYEDLRDGLVLLQVLDKIQPGCVNWKKVNkpkPLNKFKKVENCNYAVDLAKK 76
                          90       100
                  ....*....|....*....|....*
gi 1370460505  94 KKIRMHQTSAKDIVDGNLKSIMRLV 118
Cdd:cd21219    77 LGFSLVGIGGKDIADGNRKLTLALV 101
 
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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