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Conserved domains on  [gi|46559410|ref|NP_835219|]
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dixin isoform 1 [Mus musculus]

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 ...
22-154 3.80e-60

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: 197.13  E-value: 3.80e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213   1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213  55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
629-704 3.59e-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: 133.42  E-value: 3.59e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410   629 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 704
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-497 4.63e-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: 53.40  E-value: 4.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190
                ....*....|....*....|....*....|
gi 46559410 468 EEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
22-154 3.80e-60

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: 197.13  E-value: 3.80e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213   1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213  55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
629-704 3.59e-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: 133.42  E-value: 3.59e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410   629 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 704
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
629-705 1.55e-19

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


Pssm-ID: 197474  Cd Length: 83  Bit Score: 83.62  E-value: 1.55e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46559410    629 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 705
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
24-153 4.31e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.85  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 103
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46559410   104 QQEMKSNVERVLQFvASKKIRMHQTS--AKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:pfam00307  58 EFDKLENINLALDV-AEKKLGVPKVLiePEDLVEGDNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
25-151 3.64e-08

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: 51.55  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410     25 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 104
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 46559410    105 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 151
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-497 4.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190
                ....*....|....*....|....*....|
gi 46559410 468 EEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
307-497 2.90e-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: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    307 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 384
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    385 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 462
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 46559410    463 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-152 5.89e-06

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 49.55  E-value: 5.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvqlSP 101
Cdd:COG5069  10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE-----------------------TP 62
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:COG5069  63 ETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRL 113
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
311-508 3.44e-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: 47.42  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    311 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 382
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    383 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 453
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    454 GQKDrlfqqqqAKLEEALRKLSDASYQQVDL-----ERELEQKDVllahcmKGETDEVTN 508
Cdd:pfam15921  614 DKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
PTZ00121 PTZ00121
MAEBL; Provisional
303-492 3.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   303 EATWEEQLLEQQEHLEKEmEEAKKMISGLQAlllngslPEDEQERPValcEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 382
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA-EEEKKKVEQLKK-------KEAEEKKKA---EELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   383 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 455
Cdd:PTZ00121 1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 46559410   456 KDRLfqqQQAKLEEALRKLSDASYQQVDLERELEQKD 492
Cdd:PTZ00121 1756 KKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
22-154 3.80e-60

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: 197.13  E-value: 3.80e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213   1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213  55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
629-704 3.59e-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: 133.42  E-value: 3.59e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410   629 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 704
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
22-152 1.78e-24

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: 98.42  E-value: 1.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21212   1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAV--------------------------AGEKVPGIHSRP 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21212  55 KTRAQKLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
629-705 1.55e-19

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


Pssm-ID: 197474  Cd Length: 83  Bit Score: 83.62  E-value: 1.55e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46559410    629 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDReGNHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 705
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTK-KNYKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
20-152 1.83e-14

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: 70.01  E-value: 1.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  20 EQQLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQL 99
Cdd:cd21227   3 EIQKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEIL--------------------------QGRKLGRVIK 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410 100 SPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21227  55 KPLNQHQKLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRY 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
24-153 4.31e-14

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


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 68.85  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 103
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46559410   104 QQEMKSNVERVLQFvASKKIRMHQTS--AKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:pfam00307  58 EFDKLENINLALDV-AEKKLGVPKVLiePEDLVEGDNKSVLTYLASLFRRFQ 108
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
26-149 1.59e-13

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: 66.98  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  26 YVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPSNQQ 105
Cdd:cd21286   5 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQII--------------------------ANEKVEDINGCPRSQS 58
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46559410 106 EMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALA 149
Cdd:cd21286  59 QMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLS 102
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
21-145 6.36e-13

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: 65.49  E-value: 6.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  21 QQLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEkltgvQLS 100
Cdd:cd21214   5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEVI--------------------------SGE-----RLP 51
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46559410 101 PSNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLV 145
Cdd:cd21214  52 KPERGKMRfhkiANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMI 100
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
19-149 6.87e-13

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: 65.76  E-value: 6.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  19 NEQQLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQ 98
Cdd:cd21285   8 NGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVV--------------------------ANEKIEDIN 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410  99 LSPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALA 149
Cdd:cd21285  62 GCPKNRSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLS 112
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
22-152 1.07e-12

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


Pssm-ID: 409064  Cd Length: 107  Bit Score: 64.73  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfkaagEKLTGVQLSP 101
Cdd:cd21215   5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGD--------------------------ESLGRYNKNP 56
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21215  57 KMRVQKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
23-149 1.64e-11

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: 61.20  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  23 LQAYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPS 102
Cdd:cd00014   1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKL--------------------------SPGSIPKINKKPK 53
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46559410 103 NQQEMKSNVERVLQFVASKKI-RMHQTSAKDIVE-GNLKSIMRLVLALA 149
Cdd:cd00014  54 SPFKKRENINLFLNACKKLGLpELDLFEPEDLYEkGNLKKVLGTLWALA 102
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
22-153 1.11e-10

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: 58.93  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSvKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 101
Cdd:cd21186   3 QKKTFTKWINSQLSKANK-PPIKDLFEDLRDGTRLLALLEV-------------------------------LTGKKLKP 50
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 46559410 102 ---SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21186  51 ekgRMRVHHLNNVNRALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
22-152 6.67e-10

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: 57.15  E-value: 6.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGQLALDSDASvdertdffllHSPFKAagekltgvqlsp 101
Cdd:cd21242   6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG----------HNVFQC------------ 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 snqqemKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21242  64 ------RSNIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHF 108
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
22-153 3.17e-09

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: 54.72  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 101
Cdd:cd21188   4 QKKTFTKWVNKHLIK--ARRRVVDLFEDLRDGHNLISLLEVL--------------------------SGESL------P 49
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21188  50 RERGRMRfhrlQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
22-153 3.90e-09

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: 54.88  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21190   6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVL--------------------------SGQKLPIESGRV 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21190  60 LQRAHKLSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQ 111
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
22-152 1.56e-08

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: 52.87  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhSPFKAAGEKltgvqlSP 101
Cdd:cd21183   5 QANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLST-------------------RPLKRSYNR------RP 57
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21183  58 AFQQHYLENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
22-148 1.91e-08

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


Pssm-ID: 409074  Cd Length: 111  Bit Score: 52.92  E-value: 1.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfKAAGEKLtgvQLSP 101
Cdd:cd21225   5 QIKAFTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSG----------------------KKFPKKF---DLEP 58
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46559410 102 SNQQEMKSNVERVLQFVASK-KIRMHQTSAKDIVEGNLKSIMRLVLAL 148
Cdd:cd21225  59 KNRIQMIQNLHLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
20-153 2.07e-08

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 52.76  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  20 EQ---QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGqlaldsdasvdertdffllhspfkaaGEKLTG 96
Cdd:cd21241   1 EQervQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLS--------------------------GEKLPC 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46559410  97 VQLSPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21241  55 EKGRRLKRVHFLSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
22-152 2.92e-08

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: 52.11  E-value: 2.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllHSPFKAagekltgvqlSP 101
Cdd:cd21228   5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRM---------------YKKYNK----------RP 57
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21228  58 TFRQMKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
25-151 3.64e-08

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: 51.55  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410     25 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 104
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 46559410    105 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 151
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
29-148 4.20e-08

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: 51.92  E-value: 4.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  29 WVNAQLKKR-PSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasVDERTDFFLLHSPfkaagekltgvqLSPSNQQEm 107
Cdd:cd21218  18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSL----------APELCDKELVLEV------------LSEEDLEK- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46559410 108 ksNVERVLQFVASKKIRMHqTSAKDIVEGNLKSIMRLVLAL 148
Cdd:cd21218  75 --RAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFVATL 112
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
42-152 1.60e-07

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: 50.28  E-value: 1.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  42 PVQDLRQDLRDGVilaYLIEIVGQLAldsdasvdertDFFL-LHSPFkaagekltgvqLSPSNQQEMKSNVERVLQFVAS 120
Cdd:cd21222  35 EVTDLATQFHDGV---YLILLIGLLE-----------GFFVpLHEYH-----------LTPSTDDEKLHNVKLALELMED 89
                        90       100       110
                ....*....|....*....|....*....|..
gi 46559410 121 KKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21222  90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
22-148 2.47e-07

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


Pssm-ID: 409095  Cd Length: 117  Bit Score: 49.67  E-value: 2.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 101
Cdd:cd21246  17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEV-------------------------------LSGERLPK 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNlksiMRLVLAL 148
Cdd:cd21246  64 PTKGKMRihclENVDKALQFLKEQRVHLENMGSHDIVDGN----HRLTLGL 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
308-497 4.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                       170       180       190
                ....*....|....*....|....*....|
gi 46559410 468 EEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
24-153 5.09e-07

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


Pssm-ID: 409156 [Multi-domain]  Cd Length: 122  Bit Score: 48.89  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  24 QAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIeivGQLAldsdasvdertDFFLLHSPFkaagekltgvQLSPSN 103
Cdd:cd21307  19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLI---GQLE-----------GFFIHLSEF----------FLTPSS 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 46559410 104 QQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21307  73 TSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
302-496 6.36e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 6.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 302 LEATWEEqLLEQQEHLEKEMEEAKKMISGLQALLlngslpedEQERpvalcepgvnpeEQLIIIRSRLDQSVEENQDLKK 381
Cdd:COG1196 237 LEAELEE-LEAELEELEAELEELEAELAELEAEL--------EELR------------LELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 382 ELLKC-------KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELG 454
Cdd:COG1196 296 ELARLeqdiarlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 46559410 455 QKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
14-148 1.12e-06

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: 48.06  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  14 LQEGFNEQQLQAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagek 93
Cdd:cd21193   9 LQEERINIQKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEI------------------------------- 55
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46559410  94 LTGVQLSPSNQQEMK----SNVERVLQFVASKkIRMHQTSAKDIVEGNlksiMRLVLAL 148
Cdd:cd21193  56 ISGEKLGKPNRGRLRvqkiENVNKALAFLKTK-VRLENIGAEDIVDGN----PRLILGL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
308-491 2.42e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  308 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSVEENQDLKKE 382
Cdd:COG4913  228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  383 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLEERNRLLGEYK---KELGQKD- 457
Cdd:COG4913  297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEallAALGLPLp 376
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 46559410  458 ----------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQK 491
Cdd:COG4913  377 asaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
307-497 2.90e-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: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    307 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 384
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    385 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 462
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 46559410    463 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
317-490 3.50e-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: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    317 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGI 396
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    397 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSD 476
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
                          170
                   ....*....|....
gi 46559410    477 ASYQQVDLERELEQ 490
Cdd:TIGR02168  370 LESRLEELEEQLET 383
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-152 5.89e-06

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 49.55  E-value: 5.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvqlSP 101
Cdd:COG5069  10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE-----------------------TP 62
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:COG5069  63 ETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRL 113
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
359-489 1.34e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 359 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 428
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46559410 429 ------HNQNVDLQRKLE--------ERNRLLGEYKKE---LGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELE 489
Cdd:COG3206 284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
22-152 1.72e-05

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: 44.64  E-value: 1.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdFFLLHSpfkaagekltgvqlSP 101
Cdd:cd21310  17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKM-----------YRKYHP--------------RP 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21310  70 NFRQMKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 120
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
312-492 2.84e-05

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: 47.76  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    312 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 391
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    392 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 471
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
                          170       180
                   ....*....|....*....|.
gi 46559410    472 RKLSDASYQQVDLERELEQKD 492
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKA 447
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
311-508 3.44e-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: 47.42  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    311 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 382
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    383 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 453
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    454 GQKDrlfqqqqAKLEEALRKLSDASYQQVDL-----ERELEQKDVllahcmKGETDEVTN 508
Cdd:pfam15921  614 DKKD-------AKIRELEARVSDLELEKVKLvnagsERLRAVKDI------KQERDQLLN 660
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-496 3.70e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  355 GVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQ--DTSVLQLKQELLRANMDKDELHNQN 432
Cdd:COG4913  605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAELERLDASS 684
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46559410  433 VD---LQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG4913  685 DDlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
308-535 6.91e-05

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: 45.91  E-value: 6.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 308 EQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLK 385
Cdd:COG4942  30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRAL--------EQELAALEAELAELEKEIAELRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 386 CKQEARNL------QGIKDALQQRLTQQDTS------------VLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLG 447
Cdd:COG4942 102 QKEELAELlralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 448 EYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMKGETDEVTNYNSHS--SQRNGFVLPVAG 525
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGfaALKGKLPWPVSG 261
                       250
                ....*....|....*...
gi 46559410 526 R--------GATTVTHRG 535
Cdd:COG4942 262 RvvrrfgerDGGGGRNKG 279
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
308-477 8.04e-05

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: 46.20  E-value: 8.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    308 EQLLEQQEHLEKEMEEAKKMISGLQAlllngSLPEDEQERPVALCEPGVNpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELEALLNERASL-EEALALLRSELEELSEELRELESKRSELR 914
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLEERNRLLGEYKKELG--------- 454
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994
                          170       180
                   ....*....|....*....|....*...
gi 46559410    455 ---QKDRL--FQQQQAKLEEALRKLSDA 477
Cdd:TIGR02168  995 yeeLKERYdfLTAQKEDLTEAKETLEEA 1022
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
27-152 1.01e-04

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


Pssm-ID: 409153  Cd Length: 107  Bit Score: 41.91  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  27 VAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVGQLALDsdasVDERTdffllhspfkaagekltgvQLSPSNQQE 106
Cdd:cd21304   7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLE----VAEVT-------------------QSEVGQKQK 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 46559410 107 MKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21304  62 LRTVLDKINRILNLPRWSQQKWSVDSIHSKNLVAILHLLVALARHF 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
359-490 1.86e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 359 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 438
Cdd:COG4372  44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 46559410 439 LEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 490
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
28-152 1.87e-04

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: 41.10  E-value: 1.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  28 AWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEivgqlaldsdasvdertdffllhspfKAAGEKLTGVQLSPSNQQEm 107
Cdd:cd21221   8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLE--------------------------KLANEKLEVPEVAQSEEGQ- 58
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46559410 108 KSNVERVLQFVaSKKIRMHQTSAKDIVEG----NLKSIMRLVLALAAHF 152
Cdd:cd21221  59 KQKLAVVLACV-NFLLGLEEDEARWTVDGiynkDLVSILHLLVALAHHY 106
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
22-153 2.29e-04

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 41.41  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIV-GQLALDSdasvdertdffllHSPFkaagekltgvqls 100
Cdd:cd21191   6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLsGQNLLQE-------------YKPS------------- 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410 101 pSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21191  60 -SHRIFRLNNIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQ 111
CH_ASPM_rpt1 cd21223
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
43-149 2.87e-04

first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409072  Cd Length: 113  Bit Score: 41.04  E-value: 2.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  43 VQDLRQDLRDGVILAYLIEIvgqLALDSDASVDertdfflLHSPfkaAGEKLtgvqlspsnqQEMkSNVERVLQFVASKK 122
Cdd:cd21223  26 VTNLAVDLRDGVRLCRLVEL---LTGDWSLLSK-------LRVP---AISRL----------QKL-HNVEVALKALKEAG 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 46559410 123 IRMHQT----SAKDIVEGNLKSIMRLVLALA 149
Cdd:cd21223  82 VLRGGDgggiTAKDIVDGHREKTLALLWRII 112
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
22-152 2.88e-04

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: 41.28  E-value: 2.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21311  16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVL--------------------------SGKKFPKFNKRP 67
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 46559410 102 SNQQEMKSNVERVLQFVAS-KKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21311  68 TFRSQKLENVSVALKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHY 119
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
303-500 3.57e-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: 44.19  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    303 EATWEEQLLEQQEHLEKEMEEAKKMISGLQAL---------LLNGSLPEDEQERPvaLCEPGVNPEEQLIIIRSRLDQSV 373
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskeDIPNLQNITVRLQD--LTEKLSEAEDMLACEQHALLRKL 621
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410    374 EE---NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYK 450
Cdd:TIGR00618  622 QPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 46559410    451 KELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMK 500
Cdd:TIGR00618  697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
25-148 4.91e-04

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: 40.25  E-value: 4.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  25 AYVAWVNAQLKKRPSVK-------PVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaageKLTGV 97
Cdd:cd21217   5 AFVEHINSLLADDPDLKhllpidpDGDDLFEALRDGVLLCKLINKI------VPGTIDER---------------KLNKK 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 46559410  98 qlSPSNQQEMKSNVERVLQfvASKKIRMHQTS--AKDIVEGNLKsimrLVLAL 148
Cdd:cd21217  64 --KPKNIFEATENLNLALN--AAKKIGCKVVNigPQDILDGNPH----LVLGL 108
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
22-152 7.79e-04

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: 40.06  E-value: 7.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKltgvqlsP 101
Cdd:cd21309  18 QQNTFTRWCNEHLKCVN--KRIGNLQTDLSDGLRLIALLEVLSQKRM------------------YRKYHQR-------P 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21309  71 TFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHY 121
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
308-489 7.89e-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: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   308 EQLLEQQEHLEKEMEEAKKMISGLQALLLN-----GSLPE--DEQERPValcepgvnpeEQLIIIRSRLDQS-VEENQDL 379
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalTTLEEalSEKERII----------ERLKEQREREDRErLEELESL 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   380 KKELLKCKQEArnlqgikDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLEERNRLLGEYKK---- 451
Cdd:pfam10174 474 KKENKDLKEKV-------SALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahna 546
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 46559410   452 -ELGQKDRLFQQQQAKLE-EALRKLSDASYQQVDLERELE 489
Cdd:pfam10174 547 eEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVERLLG 586
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
22-152 9.43e-04

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 39.68  E-value: 9.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKltgvqlsP 101
Cdd:cd21308  21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKM------------------HRKHNQR-------P 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46559410 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21308  74 TFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHY 124
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
307-490 9.56e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 307 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiiRSRLDQsVEENQDLKKELLKC 386
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL---RAALEQ-AEEYQELKEELEEL 407
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 387 KQEarnLQGIKDALQQRLTQQDTSvlQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK--ELGQKDRLFQQQQ 464
Cdd:COG4717 408 EEQ---LEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELK 482
                       170       180
                ....*....|....*....|....*.
gi 46559410 465 AKLEEALRKLSDASYQQVDLERELEQ 490
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREE 508
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
349-496 1.37e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 349 VALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD---- 424
Cdd:COG3883   5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieer 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 425 KDELHNQNVDLQR----------------------------KLEERNR-LLGEYKKELGQKDRLFQQQQAKLEEALRKLS 475
Cdd:COG3883  85 REELGERARALYRsggsvsyldvllgsesfsdfldrlsalsKIADADAdLLEELKADKAELEAKKAELEAKLAELEALKA 164
                       170       180
                ....*....|....*....|.
gi 46559410 476 DASYQQVDLERELEQKDVLLA 496
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLA 185
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
12-153 1.50e-03

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: 39.20  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  12 DVLQEGFNEQ---QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqLALDSDASVDERTDFFLLHspfk 88
Cdd:cd21236   5 NVLERYKDERdkvQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEV---LSGDTLPREKGRMRFHRLQ---- 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46559410  89 aagekltgvqlspsnqqemksNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21236  76 ---------------------NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
366-496 2.27e-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: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 366 RSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRL 445
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410 446 LGE-----YKKE--------LGQKD------------RLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG4942 106 LAEllralYRLGrqpplallLSPEDfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
PTZ00121 PTZ00121
MAEBL; Provisional
303-492 3.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   303 EATWEEQLLEQQEHLEKEmEEAKKMISGLQAlllngslPEDEQERPValcEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 382
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA-EEEKKKVEQLKK-------KEAEEKKKA---EELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   383 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 455
Cdd:PTZ00121 1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 46559410   456 KDRLfqqQQAKLEEALRKLSDASYQQVDLERELEQKD 492
Cdd:PTZ00121 1756 KKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
300-488 3.66e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   300 TYLEATWEEQLLEQQEHLEKEMEEAKkmISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiirSRLDQSVEENQDL 379
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLTKELEDIK--MSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM----EELNKAKAAHSFV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   380 KKELlkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQK--- 456
Cdd:pfam05483 351 VTEF---EATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqf 427
                         170       180       190
                  ....*....|....*....|....*....|..
gi 46559410   457 DRLFQQQQAKLEEALRKLSDASYQQVDLEREL 488
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQL 459
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
22-164 3.89e-03

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: 37.70  E-value: 3.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 101
Cdd:cd21235   7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVL--------------------------SGDSL------P 52
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46559410 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKPGSSRTVSQGR 164
Cdd:cd21235  53 REKGRMRfhklQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
307-490 4.23e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  307 EEQLLEQQEHLEKEMEEAKKMISGL----QALllngslpeDEQ--------------ERPVALCE-PGVNPE---EQLII 364
Cdd:COG3096  374 AEQLAEAEARLEAAEEEVDSLKSQLadyqQAL--------DVQqtraiqyqqavqalEKARALCGlPDLTPEnaeDYLAA 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  365 IRSRLDQSVEENQDLKKEL---------------LKCK-----------QEARNLqgIKDALQQRLTQQDTSVLQLKQEL 418
Cdd:COG3096  446 FRAKEQQATEEVLELEQKLsvadaarrqfekayeLVCKiageversqawQTAREL--LRRYRSQQALAQRLQQLRAQLAE 523
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46559410  419 LRanmdkdelhnQNVDLQRKLEernRLLGEYKKELGQK-------DRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 490
Cdd:COG3096  524 LE----------QRLRQQQNAE---RLLEEFCQRIGQQldaaeelEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
308-489 4.73e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.22  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   308 EQLLEQQEHLE-----KEMEEAKKMISGLQALLLNGSLPEdeqerpvalcepgvnPEEQLIIIRSRLDQSVEenqDLKKE 382
Cdd:pfam06160 221 REMEEEGYALEhlnvdKEIQQLEEQLEENLALLENLELDE---------------AEEALEEIEERIDQLYD---LLEKE 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   383 LlkckqEARN-LQGIKDALQQRLTQQDTSVLQLKQELLRAN----MDKDELHNQNvDLQRKLEERNRLLGEYKKELGQKD 457
Cdd:pfam06160 283 V-----DAKKyVEKNLPEIEDYLEHAEEQNKELKEELERVQqsytLNENELERVR-GLEKQLEELEKRYDEIVERLEEKE 356
                         170       180       190
                  ....*....|....*....|....*....|..
gi 46559410   458 RLFQQQQAKLEEALRKLSDASYQQVDLERELE 489
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQEEFKESLQ 388
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
360-490 4.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 360 EQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQ--QDTSVLQLKQELLRANMDKDELHNQNVDLQR 437
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEE 153
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46559410 438 KLEERNRLLGEYKkelgQKDRLFQQQQAKLEEALRKLSDASYQQV-DLERELEQ 490
Cdd:COG4717 154 RLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELqDLAEELEE 203
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-498 4.90e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  302 LEATWEE--QLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDL 379
Cdd:COG4913  257 IRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL--------EAELERLEARLDALREELDEL 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  380 KKELLK--------CKQEARNLQGIKDALQQRLTQQDTSVLQLKqelLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK 451
Cdd:COG4913  329 EAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEE 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 46559410  452 ELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ-KDVLLAHC 498
Cdd:COG4913  406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRDALAEAL 453
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
22-153 5.33e-03

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: 37.32  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLsP 101
Cdd:cd21237   7 QKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEV-------------------------------LSGVKL-P 52
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46559410 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21237  53 REKGRMRfhrlQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 108
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
305-492 5.68e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   305 TWEEQLLE---QQEHLEKEMEEAKKmisglqalllngslpedEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDL-- 379
Cdd:pfam13851  30 SLKEEIAElkkKEERNEKLMSEIQQ-----------------ENKR---LTEPLQKAQEEVEELRKQLENYEKDKQSLkn 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410   380 -KKELLKCKQEARNLQGIKDALQQRLTqqdtsvlQLKQEllranmdKDELHNQNV----DLQRKLEERNRLLgeyKKELG 454
Cdd:pfam13851  90 lKARLKVLEKELKDLKWEHEVLEQRFE-------KVERE-------RDELYDKFEaaiqDVQQKTGLKNLLL---EKKLQ 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 46559410   455 QKDRLFQQQQAKLEEALR--KLSDASYQQVD--LERELEQKD 492
Cdd:pfam13851 153 ALGETLEKKEAQLNEVLAaaNLDPDALQAVTekLEDVLESKN 194
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
377-496 7.65e-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: 38.75  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46559410 377 QDLKKELLKCKQEARNLQGIKDALQQRLTQqdtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQ- 455
Cdd:COG1579  13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 46559410 456 -KDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG1579  86 rNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
 
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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