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Conserved domains on  [gi|1907198733|ref|XP_036010975|]
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dixin isoform X6 [Mus musculus]

Protein Classification

calponin homology domain-containing protein( domain architecture ID 15342760)

calponin homology domain-containing protein such as alpha parvin, which plays a role in sarcomere organization and in smooth muscle cell contraction

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 7.27e-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: 194.05  E-value: 7.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213    55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 312-567 1.03e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  312 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 391
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  392 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 471
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  472 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 550
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1907198733  551 VVETQKKQ-ERKVGGRSP 567
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
 
Name Accession Description Interval E-value
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 22-154 7.27e-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: 194.05  E-value: 7.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213    55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 24-153 8.69e-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: 67.70  E-value: 8.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 103
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 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 5.77e-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: 50.78  E-value: 5.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733   25 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 104
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907198733  105 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 151
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 312-567 1.03e-06

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: 51.99  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  312 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 391
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  392 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 471
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  472 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 550
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1907198733  551 VVETQKKQ-ERKVGGRSP 567
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-497 2.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907198733 468 EEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-152 8.04e-06

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.78  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvqlSP 101
Cdd:COG5069    10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE-----------------------TP 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 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. ...
 311-495 3.56e-04

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: 43.57  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  311 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 382
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  383 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 453
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907198733  454 GQKDRLFQQQQAK---LEEALRKLSDASYQQVDLERELEQ-KDVLL 495
Cdd:pfam15921  614 DKKDAKIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQeRDQLL 659
PTZ00121 PTZ00121
MAEBL; Provisional
 303-492 8.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  303 EATWEEQLLEQQEHLEKEMEEAKKMisglqalllngSLPEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 382
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEEKKKV-----------EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  383 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 455
Cdd:PTZ00121  1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907198733  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 7.27e-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: 194.05  E-value: 7.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEIL--------------------------AGEKLPGIDWNP 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 154
Cdd:cd21213    55 TTDAERKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 22-152 3.97e-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: 96.88  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAV--------------------------AGEKVPGIHSRP 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21212    55 KTRAQKLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 20-152 4.57e-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: 68.47  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  20 EQQLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQL 99
Cdd:cd21227     3 EIQKNTFTNWVNEQLK--PTGMSVEDLATDLEDGVKLIALVEIL--------------------------QGRKLGRVIK 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907198733 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 8.69e-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: 67.70  E-value: 8.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllHSPfkaageKLTGVQLSPSN 103
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNK---------------------LAP------GLVDKKKLNKS 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 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 2.49e-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: 66.21  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  26 YVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPSNQQ 105
Cdd:cd21286     5 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQII--------------------------ANEKVEDINGCPRSQS 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907198733 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 1.23e-12

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: 64.33  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  21 QQLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLS 100
Cdd:cd21214     5 QQRKTFTAWCNSHLRKAGT--QIENIEEDFRDGLKLMLLLEV-------------------------------ISGERLP 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907198733 101 PSNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLV 145
Cdd:cd21214    52 KPERGKMRfhkiANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMI 100
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 22-152 1.48e-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: 63.96  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfkaagEKLTGVQLSP 101
Cdd:cd21215     5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGD--------------------------ESLGRYNKNP 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21215    57 KMRVQKLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
 19-149 2.13e-12

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: 64.21  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  19 NEQQLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQ 98
Cdd:cd21285     8 NGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVV--------------------------ANEKIEDIN 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733  99 LSPSNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALA 149
Cdd:cd21285    62 GCPKNRSQMIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLS 112
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 23-149 2.87e-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: 60.43  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  23 LQAYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSPS 102
Cdd:cd00014     1 EEELLKWINEVLGEELPV-SITDLFESLRDGVLLCKLINKL--------------------------SPGSIPKINKKPK 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907198733 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 1.53e-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: 58.55  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSvKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 101
Cdd:cd21186     3 QKKTFTKWINSQLSKANK-PPIKDLFEDLRDGTRLLALLEV-------------------------------LTGKKLKP 50

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198733 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 9.19e-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: 56.38  E-value: 9.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGQLALDSDASvdertdffllHSPFKAagekltgvqlsp 101
Cdd:cd21242     6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKG----------HNVFQC------------ 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 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 5.32e-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: 53.94  E-value: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 101
Cdd:cd21188     4 QKKTFTKWVNKHLIK--ARRRVVDLFEDLRDGHNLISLLEVL--------------------------SGESL------P 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198733 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 5.64e-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: 54.11  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21190     6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVL--------------------------SGQKLPIESGRV 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 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 2.09e-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: 52.48  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhSPFKAAGEKltgvqlSP 101
Cdd:cd21183     5 QANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLST-------------------RPLKRSYNR------RP 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 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 2.96e-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: 52.15  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlaldsdasvdertdffllhspfKAAGEKLtgvQLSP 101
Cdd:cd21225     5 QIKAFTAWVNSVLEKR-GIPKISDLATDLSDGVRLIFFLELVSG----------------------KKFPKKF---DLEP 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907198733 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 ...
 22-153 3.02e-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: 51.99  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVGqlaldsdasvdertdffllhspfkaaGEKLTGVQLSP 101
Cdd:cd21241     6 QKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLS--------------------------GEKLPCEKGRR 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21241    60 LKRVHFLSNINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 29-148 5.46e-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: 51.15  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  29 WVNAQLKKR-PSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasVDERTDFFLLHSPfkaagekltgvqLSPSNQQEm 107
Cdd:cd21218    18 WVNYHLKKAgPTKKRVTNFSSDLKDGEVYALLLHSL----------APELCDKELVLEV------------LSEEDLEK- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907198733 108 ksNVERVLQFVASKKIRMHqTSAKDIVEGNLKSIMRLVLAL 148
Cdd:cd21218    75 --RAEKVLQAAEKLGCKYF-LTPEDIVSGNPRLNLAFVATL 112
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 25-151 5.77e-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: 50.78  E-value: 5.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733   25 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaagekltgvQLSPSNQ 104
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSL------SPGLVDKK--------------------KVAASLS 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907198733  105 QEMK-SNVERVLQFVASKKIRMHQTSAKDIVEGNlKSIMRLVLALAAH 151
Cdd:smart00033  55 RFKKiENINLALSFAEKLGGKVVLFEPEDLVEGP-KLILGVIWTLISL 101
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 22-152 6.43e-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: 50.95  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllHSPFKAagekltgvqlSP 101
Cdd:cd21228     5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRM---------------YKKYNK----------RP 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21228    58 TFRQMKLENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 42-152 1.45e-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: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  42 PVQDLRQDLRDGVilaYLIEIVGQLAldsdasvdertDFFL-LHSPFkaagekltgvqLSPSNQQEMKSNVERVLQFVAS 120
Cdd:cd21222    35 EVTDLATQFHDGV---YLILLIGLLE-----------GFFVpLHEYH-----------LTPSTDDEKLHNVKLALELMED 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907198733 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 3.49e-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: 48.90  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 101
Cdd:cd21246    17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEV-------------------------------LSGERLPK 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNlksiMRLVLAL 148
Cdd:cd21246    64 PTKGKMRihclENVDKALQFLKEQRVHLENMGSHDIVDGN----HRLTLGL 110
CH_PARVG_rpt2 cd21307
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ...
 24-153 5.86e-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: 48.50  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  24 QAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIeivGQLaldsdasvderTDFFLLHSPFkaagekltgvQLSPSN 103
Cdd:cd21307    19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLI---GQL-----------EGFFIHLSEF----------FLTPSS 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907198733 104 QQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21307    73 TSEMLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 312-567 1.03e-06

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: 51.99  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  312 EQQEHLEKEMEEAKKMISGLQALLlngSLPEDEQERpvaLCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 391
Cdd:TIGR02169  287 EEQLRVKEKIGELEAEIASLERSI---AEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  392 NLQGIKDALQQRLTQQDTSVLQLKQELlranmdkdelhnqnVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEAL 471
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDEL--------------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  472 RKLSDASYQQVDLERELEQKDVLLAhcmKGETDEPQTS-DLQLVRDALRSLRNsfsghdpqhhTIDSLEQGISSLMERLH 550
Cdd:TIGR02169  427 AAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAaDLSKYEQELYDLKE----------EYDRVEKELSKLQRELA 493

                          250
                   ....*....|....*...
gi 1907198733  551 VVETQKKQ-ERKVGGRSP 567
Cdd:TIGR02169  494 EAEAQARAsEERVRGGRA 511
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 14-148 2.13e-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: 46.91  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  14 LQEGFNEQQLQAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagek 93
Cdd:cd21193     9 LQEERINIQKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEI------------------------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907198733  94 LTGVQLSPSNQQEMK----SNVERVLQFVASKkIRMHQTSAKDIVEGNlksiMRLVLAL 148
Cdd:cd21193    56 ISGEKLGKPNRGRLRvqkiENVNKALAFLKTK-VRLENIGAEDIVDGN----PRLILGL 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-497 2.26e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190
                  ....*....|....*....|....*....|
gi 1907198733 468 EEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-496 2.93e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAEL------EELRLELEEL-------ELELEEAQAEEYELLAELARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKL 467
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         170       180
                  ....*....|....*....|....*....
gi 1907198733 468 EEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-561 6.70e-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: 49.28  E-value: 6.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  317 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGI 396
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  397 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSD 476
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  477 ASYQQVDLERELEQKDVLLAHCMKGETD--------EPQTSDLQLVRDALRS----LRNSFSGHDPQ--HHTIDSLEQGI 542
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASlnneierlEARLERLEDRRERLQQeieeLLKKLEEAELKelQAELEELEEEL 449

                          250
                   ....*....|....*....
gi 1907198733  543 SSLMERLHVVETQKKQERK 561
Cdd:TIGR02168  450 EELQEELERLEEALEELRE 468
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
22-152 8.04e-06

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


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 48.78  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRpSVKPVQDLRQDLRDGVILAYLIEIVGQlalDSDASVDErtdffllhspfkaagekltgvqlSP 101
Cdd:COG5069    10 QKKTFTKWTNEKLISG-GQKEFGDLDTDLKDGVKLAQLLEALQK---DNAGEYNE-----------------------TP 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:COG5069    63 ETRIHVMENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
308-491 8.49e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 8.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  308 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSVEENQDLKKE 382
Cdd:COG4913    228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  383 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLEERNRLLGEYK---KELGQKD- 457
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEallAALGLPLp 376

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1907198733  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 1.40e-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: 48.13  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  307 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELL 384
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  385 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLEERNRLLGEYKKELGQKDRLFQQ 462
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907198733  463 QQAKLEEALRKLSDASYQQVDLERELEQKDVLLAH 497
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
 22-148 2.92e-05

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


Pssm-ID: 409166  Cd Length: 132  Bit Score: 43.89  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKkRPSVKpVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLSP 101
Cdd:cd21317    32 QKKTFTKWVNSHLA-RVTCR-IGDLYTDLRDGRMLIRLLEV-------------------------------LSGEQLPK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNlksiMRLVLAL 148
Cdd:cd21317    79 PTKGRMRihclENVDKALQFLKEQKVHLENMGSHDIVDGN----HRLTLGL 125
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
 22-152 2.96e-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: 43.87  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdFFLLHSpfkaagekltgvqlSP 101
Cdd:cd21310    17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKM-----------YRKYHP--------------RP 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21310    70 NFRQMKLENVSVALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 120
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
359-489 1.04e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 359 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 428
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198733 429 ------HNQNVDLQRKLE--------ERNRLLGEYKKE---LGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELE 489
Cdd:COG3206   284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
CH_PARVA_B_rpt1 cd21304
first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ...
 27-152 2.45e-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: 40.76  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  27 VAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVGQLALDsdasVDERTdffllhspfkaagekltgvQLSPSNQQE 106
Cdd:cd21304     7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLE----VAEVT-------------------QSEVGQKQK 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907198733 107 MKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21304    62 LRTVLDKINRILNLPRWSQQKWSVDSIHSKNLVAILHLLVALARHF 107
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 311-495 3.56e-04

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: 43.57  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  311 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSVEENQDLKKE 382
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  383 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLEERNRLLGEYKKEL 453
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907198733  454 GQKDRLFQQQQAK---LEEALRKLSDASYQQVDLERELEQ-KDVLL 495
Cdd:pfam15921  614 DKKDAKIRELEARvsdLELEKVKLVNAGSERLRAVKDIKQeRDQLL 659
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
 22-153 3.71e-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: 40.26  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIV-GQLALDSdasvdertdffllHSPFkaagekltgvqls 100
Cdd:cd21191     6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLsGQNLLQE-------------YKPS------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907198733 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 3.80e-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: 40.27  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  43 VQDLRQDLRDGVILAYLIEIvgqLALDSDASVDertdfflLHSPfkaAGEKLtgvqlspsnqQEMkSNVERVLQFVASKK 122
Cdd:cd21223    26 VTNLAVDLRDGVRLCRLVEL---LTGDWSLLSK-------LRVP---AISRL----------QKL-HNVEVALKALKEAG 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907198733 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 3.83e-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: 40.51  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLTGVQLSP 101
Cdd:cd21311    16 QQNTFTRWANEHLKT--ANKHIADLETDLSDGLRLIALVEVL--------------------------SGKKFPKFNKRP 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 102 SNQQEMKSNVERVLQFVAS-KKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21311    68 TFRSQKLENVSVALKFLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHY 119
CH_PARV_rpt1 cd21221
first calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 28-152 4.95e-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: 39.95  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  28 AWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEivgqlaldsdasvdertdffllhspfKAAGEKLTGVQLSPSNQQEm 107
Cdd:cd21221     8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLE--------------------------KLANEKLEVPEVAQSEEGQ- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907198733 108 KSNVERVLQFVaSKKIRMHQTSAKDIVEG----NLKSIMRLVLALAAHF 152
Cdd:cd21221    59 KQKLAVVLACV-NFLLGLEEDEARWTVDGiynkDLVSILHLLVALAHHY 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 308-477 4.98e-04

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: 43.12  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  308 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELI------EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  388 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLEERNRLLGEYKKELG--------- 454
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994

                          170       180
                   ....*....|....*....|....*...
gi 1907198733  455 ---QKDRL--FQQQQAKLEEALRKLSDA 477
Cdd:TIGR02168  995 yeeLKERYdfLTAQKEDLTEAKETLEEA 1022
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 25-145 6.14e-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: 39.86  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  25 AYVAWVNAQLKKRPSVK-------PVQDLRQDLRDGVILAYLIEIVgqlaldSDASVDERtdffllhspfkaageKLTGV 97
Cdd:cd21217     5 AFVEHINSLLADDPDLKhllpidpDGDDLFEALRDGVLLCKLINKI------VPGTIDER---------------KLNKK 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907198733  98 qlSPSNQQEMKSNVERVLQfvASKKIRMHQTS--AKDIVEGNLKSIMRLV 145
Cdd:cd21217    64 --KPKNIFEATENLNLALN--AAKKIGCKVVNigPQDILDGNPHLVLGLL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-530 7.24e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  355 GVNPEEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSV---------LQLKQEL--LRANM 423
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELerLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  424 DK--------DELHNQNVDLQRKLEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLL 495
Cdd:COG4913    685 DDlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907198733  496 AHCMK---GETDEpQTSDLQLVRDALRSLRNSFSGHDP 530
Cdd:COG4913    765 RELREnleERIDA-LRARLNRAEEELERAMRAFNREWP 801
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 312-496 1.12e-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: 41.67  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 312 EQQEHLEKEMEEAKKMISGLQALLlngslpEDEQERPVALcepgvnpEEQLIIIRSRLDQSVEENQDLKKELLKCKQEAR 391
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKEL------AALKKEEKAL-------LKQLAALERRIAALARRIRALEQELAALEAELA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 392 NLQGIKDALQQRLTQQDT---SVLQLKQELLRANMDKDELHNQNVD--------LQRKLEERNRLLGEYKKELGQKDRLF 460
Cdd:COG4942    87 ELEKEIAELRAELEAQKEelaELLRALYRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAALR 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907198733 461 QQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLA 496
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLA 202
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
 22-152 1.60e-03

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: 38.91  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKltgvqlsP 101
Cdd:cd21309    18 QQNTFTRWCNEHLKCVN--KRIGNLQTDLSDGLRLIALLEVLSQKRM------------------YRKYHQR-------P 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21309    71 TFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHY 121
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 376-500 2.08e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  376 NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKKELGQ 455
Cdd:TIGR00618  627 LQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907198733  456 KDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQKDVLLAHCMK 500
Cdd:TIGR00618  702 CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
 22-152 2.16e-03

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: 38.53  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVGQLALdsdasvdertdffllhspFKAAGEKltgvqlsP 101
Cdd:cd21308    21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKM------------------HRKHNQR-------P 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907198733 102 SNQQEMKSNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 152
Cdd:cd21308    74 TFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHY 124
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
 12-153 2.28e-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: 38.43  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  12 DVLQEGFNEQ---QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqLALDSDASVDERTDFFLLHspfk 88
Cdd:cd21236     5 NVLERYKDERdkvQKKTFTKWINQHLMK--VRKHVNDLYEDLRDGHNLISLLEV---LSGDTLPREKGRMRFHRLQ---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907198733  89 aagekltgvqlspsnqqemksNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21236    76 ---------------------NVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 119
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
359-490 5.70e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 359 EEQLIIIRSRLDQSVEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 438
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907198733 439 LEERNRLLGEYKKELGQKDRLFQQQQAKLEEALRKLSDASYQQVDLERELEQ 490
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
 22-164 6.41e-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: 36.93  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVgqlaldsdasvdertdffllhspfkaAGEKLtgvqlsP 101
Cdd:cd21235     7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVL--------------------------SGDSL------P 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198733 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKPGSSRTVSQGR 164
Cdd:cd21235    53 REKGRMRfhklQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 308-489 7.51e-03

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: 39.42  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 308 EQLLEQQEHLEKEMEEAKKMISGLQalllngslpEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKELLKCK 387
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQ---------TDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 388 QEARNLQGIKDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLEERNRLLGEYKK-----ELGQKDR 458
Cdd:pfam10174 475 KENKDLKEKVSALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahnaeEAVRTNP 554

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1907198733 459 LFQQQQAKLE-EALRKLSDASYQQVDLERELE 489
Cdd:pfam10174 555 EINDRIRLLEqEVARYKEESGKAQAEVERLLG 586
PTZ00121 PTZ00121
MAEBL; Provisional
 303-492 8.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  303 EATWEEQLLEQQEHLEKEMEEAKKMisglqalllngSLPEDEQERPVALCEPGVNPEEQLIIIRSRLDQSVEENQDLKKE 382
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEEKKKV-----------EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  383 LLKCKQEARNlqgiKDALQQRLTQQDTSVLQLK----QELLRANMDKDELHNQNV---DLQRKLEERNRLLGEYKKELGQ 455
Cdd:PTZ00121  1680 AKKAEEDEKK----AAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKIkaeEAKKEAEEDKKKAEEAKKDEEE 1755

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907198733  456 KDRLfqqQQAKLEEALRKLSDASYQQVDLERELEQKD 492
Cdd:PTZ00121  1756 KKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
307-490 9.56e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 307 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLiiiRSRLDQsVEENQDLKKELLKC 386
Cdd:COG4717   332 PDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEEL---RAALEQ-AEEYQELKEELEEL 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733 387 KQEarnLQGIKDALQQRLTQQDTSvlQLKQELLRANMDKDELHNQNVDLQRKLEERNRLLGEYKK--ELGQKDRLFQQQQ 464
Cdd:COG4717   408 EEQ---LEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELK 482

                         170       180
                  ....*....|....*....|....*.
gi 1907198733 465 AKLEEALRKLSDASYQQVDLERELEQ 490
Cdd:COG4717   483 AELRELAEEWAALKLALELLEEAREE 508
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
 22-153 9.66e-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: 36.55  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198733  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIvgqlaldsdasvdertdffllhspfkaagekLTGVQLsP 101
Cdd:cd21237     7 QKKTFTKWVNKHLMK--VRKHINDLYEDLRDGHNLISLLEV-------------------------------LSGVKL-P 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198733 102 SNQQEMK----SNVERVLQFVASKKIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 153
Cdd:cd21237    53 REKGRMRfhrlQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ 108
 
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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