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Conserved domains on  [gi|262331533|ref|NP_001160157|]
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centrosomal protein of 95 kDa isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
55-107 1.07e-23

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


:

Pssm-ID: 465945  Cd Length: 59  Bit Score: 94.56  E-value: 1.07e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 262331533   55 PRNQEDEAHNVQAVIDSLALDYLQVSLSHITGENIVKGDNESIRNLLEIFDGL 107
Cdd:pfam19016   7 PSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
541-773 3.43e-07

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   541 LTKMWKQQMAQVEQLKREAQRENRSKKKLQDEI---EEALRRHDLLTALVKKEYDH-NKRLQDFRDRIqrQRLTQSK--I 614
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALANEI--SRLEQQKqiL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   615 KENRHQSVRARKYYDDYRVQLRAKMMKMRTREEMIFKKL----------------FEEGLQIQKQRLRDLR---NYAKEK 675
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelesleaeleeLEAELEELESRLEELEeqlETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   676 RNEEKRQ---HQNELDSMENHYKDqfslLAEAISQERQELK-VRQKFQAQTLHKVKRELrAKMEKEIQQLQHmiTQNDDD 751
Cdd:TIGR02168  388 VAQLELQiasLNNEIERLEARLER----LEDRRERLQQEIEeLLKKLEEAELKELQAEL-EELEEELEELQE--ELERLE 460
                          250       260
                   ....*....|....*....|..
gi 262331533   752 AFFRELEAERFKARLQLASFQY 773
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAER 482
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
7-97 1.26e-03

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).


The actual alignment was detected with superfamily member pfam00307:

Pssm-ID: 469584 [Multi-domain]  Cd Length: 109  Bit Score: 39.19  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533    7 EWVtiaNNLLFKCHIHLRIHELQD--CDANVFIALYQSILGEKVpDLIVLPRNQEDEAHNVQAVIDsLALDYLQVSLSHI 84
Cdd:pfam00307   9 RWI---NSHLAEYGPGVRVTNFTTdlRDGLALCALLNKLAPGLV-DKKKLNKSEFDKLENINLALD-VAEKKLGVPKVLI 83
                          90
                  ....*....|...
gi 262331533   85 TGENIVKGDNESI 97
Cdd:pfam00307  84 EPEDLVEGDNKSV 96
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
55-107 1.07e-23

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 94.56  E-value: 1.07e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 262331533   55 PRNQEDEAHNVQAVIDSLALDYLQVSLSHITGENIVKGDNESIRNLLEIFDGL 107
Cdd:pfam19016   7 PSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
541-773 3.43e-07

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: 53.91  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   541 LTKMWKQQMAQVEQLKREAQRENRSKKKLQDEI---EEALRRHDLLTALVKKEYDH-NKRLQDFRDRIqrQRLTQSK--I 614
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALANEI--SRLEQQKqiL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   615 KENRHQSVRARKYYDDYRVQLRAKMMKMRTREEMIFKKL----------------FEEGLQIQKQRLRDLR---NYAKEK 675
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelesleaeleeLEAELEELESRLEELEeqlETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   676 RNEEKRQ---HQNELDSMENHYKDqfslLAEAISQERQELK-VRQKFQAQTLHKVKRELrAKMEKEIQQLQHmiTQNDDD 751
Cdd:TIGR02168  388 VAQLELQiasLNNEIERLEARLER----LEDRRERLQQEIEeLLKKLEEAELKELQAEL-EELEEELEELQE--ELERLE 460
                          250       260
                   ....*....|....*....|..
gi 262331533   752 AFFRELEAERFKARLQLASFQY 773
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAER 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
550-770 7.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 550 AQVEQLKREAQRENRsKKKLQDEIEE------ALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVR 623
Cdd:COG1196  200 RQLEPLERQAEKAER-YRELKEELKEleaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 624 ARKYYDDYRVQLRAKMMKM-RTREEMIFKKLFEEGLQIQKQRLRDLRNyAKEKRNEEKRQHQNELDSMENHYKDQFSLLA 702
Cdd:COG1196  279 LELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAE 357
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262331533 703 EAISQERQELKVRQKFQAQTLHKVKRELRAKMEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLAS 770
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
561-766 9.00e-04

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 9.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   561 RENRSKKKLQDEIEEALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVRARKYYDdyRVQLRAKMM 640
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD--EQEEIESSK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   641 KMRTREEMIFK---KLFEEGLQIQKQRLRDLRNYAKEKRNEEKRQHQNELDSMENHYKDQFSLLAEAISQERQELKVRQK 717
Cdd:pfam02463  258 QEIEKEEEKLAqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 262331533   718 FQAQTLHKVKRELRAKMEKEIQQL----QHMITQNDDDAFFRELEAERFKARL 766
Cdd:pfam02463  338 EELEKELKELEIKREAEEEEEEELeklqEKLEQLEEELLAKKKLESERLSSAA 390
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
7-97 1.26e-03

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: 39.19  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533    7 EWVtiaNNLLFKCHIHLRIHELQD--CDANVFIALYQSILGEKVpDLIVLPRNQEDEAHNVQAVIDsLALDYLQVSLSHI 84
Cdd:pfam00307   9 RWI---NSHLAEYGPGVRVTNFTTdlRDGLALCALLNKLAPGLV-DKKKLNKSEFDKLENINLALD-VAEKKLGVPKVLI 83
                          90
                  ....*....|...
gi 262331533   85 TGENIVKGDNESI 97
Cdd:pfam00307  84 EPEDLVEGDNKSV 96
PRK12704 PRK12704
phosphodiesterase; Provisional
606-765 3.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 606 RQRLTQSKIKENRHQSVR----ARK----YYDDYRVQLRAKMMKMRTREEMIFKKLFEEgLQIQKQRLR------DLRNY 671
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRileeAKKeaeaIKKEALLEAKEEIHKLRNEFEKELRERRNE-LQKLEKRLLqkeenlDRKLE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 672 AKEKRNEEKRQHQNELDSMENHYKDQFSLLAEAISQERQELkvrQKFQAQTLHKVKRELRAKMEKEIQ-QLQHMITQNDD 750
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL---ERISGLTAEEAKEILLEKVEEEARhEAAVLIKEIEE 180
                        170
                 ....*....|....*
gi 262331533 751 DAffrELEAERfKAR 765
Cdd:PRK12704 181 EA---KEEADK-KAK 191
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
12-101 8.69e-03

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: 36.41  E-value: 8.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  12 ANNLLFKCHIHLRIHELQD--CDANVFIALYQSILGEKVPDLIVLPRNQEDEAHNVQAvidslALDYLQ---VSLSHITG 86
Cdd:cd21212    9 ANHYLEKGGHKRIITDLQKdlGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQA-----CLQFLAalgVDVQGITA 83
                         90
                 ....*....|....*
gi 262331533  87 ENIVKGDNESIRNLL 101
Cdd:cd21212   84 EDIVDGNLKAILGLF 98
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
55-107 1.07e-23

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 94.56  E-value: 1.07e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 262331533   55 PRNQEDEAHNVQAVIDSLALDYLQVSLSHITGENIVKGDNESIRNLLEIFDGL 107
Cdd:pfam19016   7 PSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
541-773 3.43e-07

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: 53.91  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   541 LTKMWKQQMAQVEQLKREAQRENRSKKKLQDEI---EEALRRHDLLTALVKKEYDH-NKRLQDFRDRIqrQRLTQSK--I 614
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALANEI--SRLEQQKqiL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   615 KENRHQSVRARKYYDDYRVQLRAKMMKMRTREEMIFKKL----------------FEEGLQIQKQRLRDLR---NYAKEK 675
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelesleaeleeLEAELEELESRLEELEeqlETLRSK 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   676 RNEEKRQ---HQNELDSMENHYKDqfslLAEAISQERQELK-VRQKFQAQTLHKVKRELrAKMEKEIQQLQHmiTQNDDD 751
Cdd:TIGR02168  388 VAQLELQiasLNNEIERLEARLER----LEDRRERLQQEIEeLLKKLEEAELKELQAEL-EELEEELEELQE--ELERLE 460
                          250       260
                   ....*....|....*....|..
gi 262331533   752 AFFRELEAERFKARLQLASFQY 773
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAER 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
550-770 7.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 7.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 550 AQVEQLKREAQRENRsKKKLQDEIEE------ALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVR 623
Cdd:COG1196  200 RQLEPLERQAEKAER-YRELKEELKEleaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 624 ARKYYDDYRVQLRAKMMKM-RTREEMIFKKLFEEGLQIQKQRLRDLRNyAKEKRNEEKRQHQNELDSMENHYKDQFSLLA 702
Cdd:COG1196  279 LELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAE 357
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262331533 703 EAISQERQELKVRQKFQAQTLHKVKRELRAKMEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLAS 770
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
541-769 1.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 541 LTKMWKQQMAQVEQLKREAQRENRSKKKLQDEIEEALRRH----DLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKE 616
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELeeleLELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 617 NRHQSVRARKyyddyrvQLRAKMMKMRTREEMIFKKLfeEGLQIQKQRLRDLRNYAKEKRNEEKRQHQNELDSMENHYKD 696
Cdd:COG1196  317 RLEELEEELA-------ELEEELEELEEELEELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262331533 697 QFSLLAEAISQERQELKVRQKFQA--QTLHKVKRELRAKMEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLA 769
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEAllERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
546-779 7.17e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 546 KQQMAQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTALVKK----EYDHNKRLQDFRDRIQRQrltQSKIKENRhqs 621
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqeLAALEAELAELEKEIAEL---RAELEAQK--- 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 622 vrarkyyDDYRVQLRAkMMKMRTREEMIFKKLFEEGLQIQKqRLRDLRNYAKEKRN--EEKRQHQNEL----DSMENHYK 695
Cdd:COG4942  104 -------EELAELLRA-LYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaEELRADLAELaalrAELEAERA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 696 DQFSLLAEaISQERQELKVRQKFQAQTLHKVKRELRAKmEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLASFQYSK 775
Cdd:COG4942  175 ELEALLAE-LEEERAALEALKAERQKLLARLEKELAEL-AAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252

                 ....
gi 262331533 776 NPFP 779
Cdd:COG4942  253 GKLP 256
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
550-770 1.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 550 AQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTAlvkkeydhnkRLQDFRDRIQRQRLTQSKIKENRHQSVRARKyyd 629
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEE----------ELEELEEELEELEEELEEAEEELEEAEAELA--- 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 630 dyrvQLRAKMMKMRTREEMIFKKLFEEgLQIQKQRLRDLRNYAKEKRNEEKRQhQNELDSMENHYKDQFSLLAEAISQER 709
Cdd:COG1196  362 ----EAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEE 435
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262331533 710 QELKVRQKFQAQtLHKVKRELRAKMEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLAS 770
Cdd:COG1196  436 EEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
561-766 9.00e-04

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.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 9.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   561 RENRSKKKLQDEIEEALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVRARKYYDdyRVQLRAKMM 640
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD--EQEEIESSK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   641 KMRTREEMIFK---KLFEEGLQIQKQRLRDLRNYAKEKRNEEKRQHQNELDSMENHYKDQFSLLAEAISQERQELKVRQK 717
Cdd:pfam02463  258 QEIEKEEEKLAqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 262331533   718 FQAQTLHKVKRELRAKMEKEIQQL----QHMITQNDDDAFFRELEAERFKARL 766
Cdd:pfam02463  338 EELEKELKELEIKREAEEEEEEELeklqEKLEQLEEELLAKKKLESERLSSAA 390
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
7-97 1.26e-03

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: 39.19  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533    7 EWVtiaNNLLFKCHIHLRIHELQD--CDANVFIALYQSILGEKVpDLIVLPRNQEDEAHNVQAVIDsLALDYLQVSLSHI 84
Cdd:pfam00307   9 RWI---NSHLAEYGPGVRVTNFTTdlRDGLALCALLNKLAPGLV-DKKKLNKSEFDKLENINLALD-VAEKKLGVPKVLI 83
                          90
                  ....*....|...
gi 262331533   85 TGENIVKGDNESI 97
Cdd:pfam00307  84 EPEDLVEGDNKSV 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
550-770 1.55e-03

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: 42.35  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   550 AQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKI---KENRHQSVR--- 623
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldeLRAELTLLNeea 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   624 --ARKYYDDYRVQLRAKMMKMRTREEMIfKKLFEEGLQIQKQrLRDLRnYAKEKRNEEKRQHQNELDSMENHYKDQFSLL 701
Cdd:TIGR02168  820 anLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAE-IEELE-ELIEELESELEALLNERASLEEALALLRSEL 896
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   702 AEAISQERQELKVRQKFQAQT------LHKVKRELrAKMEKEIQQLQ------HMITQNDDDAFFRELEAERFKARLQLA 769
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELeelrekLAQLELRL-EGLEVRIDNLQerlseeYSLTLEEAEALENKIEDDEEEARRRLK 975

                   .
gi 262331533   770 S 770
Cdd:TIGR02168  976 R 976
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
545-714 2.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 545 WKQQMAQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTALVKKEyDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVRA 624
Cdd:COG4717   90 YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-ALEAELAELPERLEELEERLEELRELEEELEEL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 625 RKYYDDYRVQLRAKMMKMRTREEMIFKKLFEEgLQIQKQRLRDLRNyAKEKRNEEKRQHQNELDSMENhykdqfSLLAEA 704
Cdd:COG4717  169 EAELAELQEELEELLEQLSLATEEELQDLAEE-LEELQQRLAELEE-ELEEAQEELEELEEELEQLEN------ELEAAA 240
                        170
                 ....*....|
gi 262331533 705 ISQERQELKV 714
Cdd:COG4717  241 LEERLKEARL 250
PRK12704 PRK12704
phosphodiesterase; Provisional
606-765 3.70e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 606 RQRLTQSKIKENRHQSVR----ARK----YYDDYRVQLRAKMMKMRTREEMIFKKLFEEgLQIQKQRLR------DLRNY 671
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRileeAKKeaeaIKKEALLEAKEEIHKLRNEFEKELRERRNE-LQKLEKRLLqkeenlDRKLE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 672 AKEKRNEEKRQHQNELDSMENHYKDQFSLLAEAISQERQELkvrQKFQAQTLHKVKRELRAKMEKEIQ-QLQHMITQNDD 750
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL---ERISGLTAEEAKEILLEKVEEEARhEAAVLIKEIEE 180
                        170
                 ....*....|....*
gi 262331533 751 DAffrELEAERfKAR 765
Cdd:PRK12704 181 EA---KEEADK-KAK 191
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
542-769 5.07e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  542 TKMWKQQMAQVEQLKREAQRENRSkkklQDEIEEALRRHDLLTALVKKEYDHNKRLQdFRDRIQRQrltqskIKENRHQS 621
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  622 VRARKYYDDYRVQLRAKMMKMRTREEMIFKKLFEEGLQIQKQRLRDLRNyAKEKRNEEKRQHQNELDSMENHYKDQFSLL 701
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEE-QAEWKELEKEEEREEDERILEYLKEKAERE 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262331533  702 AEAISQERQELKVRQKFQAQTLHKVKRELRAKMEKEIQQLQHMITQNDDDAFFRELEAERFKARLQLA 769
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
546-767 5.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  546 KQQMAQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTALVKKEYD---HNKRLQDFRDRIQRQRLTQSKIKENRHQSV 622
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasAEREIAELEAELERLDASSDDLAALEEQLE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  623 RARKYYDDYRVQLRAkmmkmrtreemifkklfeegLQIQKQRLRDLRNYAKEKRNEEKRQHQNELDSMENHYKDQFSLLA 702
Cdd:COG4913   696 ELEAELEELEEELDE--------------------LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  703 EAISQERQELKVRQKFQAQT------LHKVKRELRAKMEkEIQQLQHMITQNDD---------DAFFRELEAE---RFKA 764
Cdd:COG4913   756 AAALGDAVERELRENLEERIdalrarLNRAEEELERAMR-AFNREWPAETADLDadleslpeyLALLDRLEEDglpEYEE 834

                  ...
gi 262331533  765 RLQ 767
Cdd:COG4913   835 RFK 837
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
545-753 6.42e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 6.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   545 WKQQMAQVEQLKREAQRENRSKKKLQDEIEEALrrHDLLTALVKKEYDHNKRLQDFrdriQRQRLTQSKIKENRHQSVRA 624
Cdd:TIGR00618  695 WKEMLAQCQTLLRELETHIEEYDREFNEIENAS--SSLGSDLAAREDALNQSLKEL----MHQARTVLKARTEAHFNNNE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533   625 RKYYDDYRVQLRAKMMkmrtREEMIFKKLFEEGLQIQKQRLRDLRNYAKekrneekrqhqneldsmenHYKDQFSLLAEA 704
Cdd:TIGR00618  769 EVTAALQTGAELSHLA----AEIQFFNRLREEDTHLLKTLEAEIGQEIP-------------------SDEDILNLQCET 825
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 262331533   705 ISQERQELKVRQKFQAQTLHKVKREL-----RAKMEKEIQQLQHMITQNDDDAF 753
Cdd:TIGR00618  826 LVQEEEQFLSRLEEKSATLGEITHQLlkyeeCSKQLAQLTQEQAKIIQLSDKLN 879
PRK12705 PRK12705
hypothetical protein; Provisional
600-747 7.57e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 7.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 600 FRDRIQRQRLTQSKIKENRHQSVRARKYYDDYRVQLRAKMmKMRTREEmifkklfEEGLQIQKQRLRDlRNYAKEKRNEE 679
Cdd:PRK12705  29 QRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQ-RQEARRE-------REELQREEERLVQ-KEEQLDARAEK 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262331533 680 KRQHQNELDSMENHYKDQFSLLAEAISQERQELK-VRQKFQAQTLHKVKRELRAKMEKEIQQLQHMITQ 747
Cdd:PRK12705 100 LDNLENQLEEREKALSARELELEELEKQLDNELYrVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
552-748 8.00e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 552 VEQLKREAQR----ENRSKKKLQDEIEEALRRHDLLTALVKKEYDHNKRLQDFRDRIQRQRLTQSKIKENRHQSVRARKY 627
Cdd:COG4717   48 LERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533 628 YDDY--RVQLRAKMMKMRTREEMIFKKLFEegLQIQKQRLRDLRNYAKEKRNEEKRQHQNELDSMENHYKDqFSLLAEAI 705
Cdd:COG4717  128 LPLYqeLEALEAELAELPERLEELEERLEE--LRELEEELEELEAELAELQEELEELLEQLSLATEEELQD-LAEELEEL 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 262331533 706 SQERQELKVRQKFQAQTLHKVKREL-RAKMEKEIQQLQHMITQN 748
Cdd:COG4717  205 QQRLAELEEELEEAQEELEELEEELeQLENELEAAALEERLKEA 248
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
546-769 8.41e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 8.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  546 KQQMAQVEQLKREAQRENRSKKKLQDEIEEALRRHDLLTALVKKEydHNKRLQDFRDRI--QRQRLTQSKIKENRHQSVR 623
Cdd:pfam13868  79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLE--KQRQLREEIDEFneEQAEWKELEKEEEREEDER 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  624 ARKYYDDYRVQLRAKMMKMRTRE---EMIFKKLFEEGLQIQKQR-----LRDLRNYAKEKRNEEKRQHQneldsmenhyk 695
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKaerdeLRAKLYQEEQERKERQKERE----------- 225
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262331533  696 dqfsllaEAISQERQELKVRQKFQAQTLHKvKRELRAKMEKEIQQLQHMITQND-DDAFFRELEAERFKARLQLA 769
Cdd:pfam13868 226 -------EAEKKARQRQELQQAREEQIELK-ERRLAEEAEREEEEFERMLRKQAeDEEIEQEEAEKRRMKRLEHR 292
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
12-101 8.69e-03

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: 36.41  E-value: 8.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262331533  12 ANNLLFKCHIHLRIHELQD--CDANVFIALYQSILGEKVPDLIVLPRNQEDEAHNVQAvidslALDYLQ---VSLSHITG 86
Cdd:cd21212    9 ANHYLEKGGHKRIITDLQKdlGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQA-----CLQFLAalgVDVQGITA 83
                         90
                 ....*....|....*
gi 262331533  87 ENIVKGDNESIRNLL 101
Cdd:cd21212   84 EDIVDGNLKAILGLF 98
 
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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