NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2024395567|ref|XP_040554172|]
View 

rho guanine nucleotide exchange factor 33 isoform X1 [Gallus gallus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RhoGEF super family cl47571
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 281-448 9.12e-16

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


The actual alignment was detected with superfamily member pfam00621:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 75.80  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 281 IALELLESERKYVINLSLILKIKATLQGPDVKRSTKE-RSFFPNsLRYLVQQHVDLLhaLQERVLSWPRQGILGDIFLKL 359
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEiKTIFSN-IEEIYELHRQLL--LEELLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 360 TNdennFLDYYVAYLRDLPECISLIH---------VVILKEVEEEIK------SDLYILffhIVQRIPEYLIHLQNVLKF 424
Cdd:pfam00621  78 AP----GFKVYSTYCSNYPKALKLLKkllkknpkfRAFLEELEANPEcrgldlNSFLIK---PVQRIPRYPLLLKELLKH 150

                         170       180
                  ....*....|....*....|....
gi 2024395567 425 TEQEHPDYYLLLVCVQRLRVFISH 448
Cdd:pfam00621 151 TPPDHPDYEDLKKALEAIKEVAKQ 174
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-140 4.48e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567   29 QSCDWAAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKE---ELSDAKSMI 105
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKL 332

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024395567  106 EEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQK 140
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAEL 367
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 281-448 9.12e-16

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 75.80  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 281 IALELLESERKYVINLSLILKIKATLQGPDVKRSTKE-RSFFPNsLRYLVQQHVDLLhaLQERVLSWPRQGILGDIFLKL 359
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEiKTIFSN-IEEIYELHRQLL--LEELLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 360 TNdennFLDYYVAYLRDLPECISLIH---------VVILKEVEEEIK------SDLYILffhIVQRIPEYLIHLQNVLKF 424
Cdd:pfam00621  78 AP----GFKVYSTYCSNYPKALKLLKkllkknpkfRAFLEELEANPEcrgldlNSFLIK---PVQRIPRYPLLLKELLKH 150

                         170       180
                  ....*....|....*....|....
gi 2024395567 425 TEQEHPDYYLLLVCVQRLRVFISH 448
Cdd:pfam00621 151 TPPDHPDYEDLKKALEAIKEVAKQ 174
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 281-457 1.13e-13

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 70.02  E-value: 1.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  281 IALELLESERKYVINLSLILKI-KATLQGPDVKRSTKE-RSFFPNSLRyLVQQHVDLLHALQERVLSWPRQG-ILGDIFL 357
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVfLKPLKKELKLLSPNElETLFGNIEE-IYEFHRDFLDELEERIEEWDDSVeRIGDVFL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  358 KLtndeNNFLDYYVAYLRDLPECISLIH--------VVILKEVEEEIKSDLYILFFHI---VQRIPEYLIHLQNVLKFTE 426
Cdd:smart00325  80 KL----EEFFKIYSEYCSNHPDALELLKklkknprfQKFLKEIESSPQCRRLTLESLLlkpVQRLTKYPLLLKELLKHTP 155

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024395567  427 QEHPDYYLLLVCVQRLRvfishySLLFQCNE 457
Cdd:smart00325 156 EDHEDREDLKKALKAIK------ELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 278-448 1.19e-13

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 70.02  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 278 RQNIALELLESERKYVINLSLILKI-KATLQGPDVKRSTKER-SFFPNsLRYLVQQHVDLLHALQERVLSWPRQG-ILGD 354
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDKELLPLSPEEVeLLFGN-IEEIYEFHRIFLKSLEERVEEWDKSGpRIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 355 IFLKLtndeNNFLDYYVAYLRDLPECISLIH---------VVILKEVEEE-IKSDLYILFFHIVQRIPEYLIHLQNVLKF 424
Cdd:cd00160    80 VFLKL----APFFKIYSEYCSNHPDALELLKklkkfnkffQEFLEKAESEcGRLKLESLLLKPVQRLTKYPLLLKELLKH 155

                         170       180
                  ....*....|....*....|....
gi 2024395567 425 TEQEHPDYYLLLVCVQRLRVFISH 448
Cdd:cd00160   156 TPDGHEDREDLKKALEAIKEVASQ 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-140 4.48e-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: 43.89  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567   29 QSCDWAAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKE---ELSDAKSMI 105
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKL 332

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024395567  106 EEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQK 140
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAEL 367
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
18-146 1.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  18 PATQISQMAPSQSCDWAAERLGALQALASELKAGFTEAMQELSRIQhgeyALEEKVKSCRCAMEEKVAEMKNSLNTFKEE 97
Cdd:COG4372    20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEELNEQLQAAQAE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2024395567  98 LSDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQKDDHSSQ 146
Cdd:COG4372    96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 41-138 2.34e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  41 LQALASELKAGFTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQKIE 120
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111

                          90
                  ....*....|....*...
gi 2024395567 121 QLQQEKRRESRKVKAKRA 138
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEA 129
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 281-448 9.12e-16

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 75.80  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 281 IALELLESERKYVINLSLILKIKATLQGPDVKRSTKE-RSFFPNsLRYLVQQHVDLLhaLQERVLSWPRQGILGDIFLKL 359
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEiKTIFSN-IEEIYELHRQLL--LEELLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 360 TNdennFLDYYVAYLRDLPECISLIH---------VVILKEVEEEIK------SDLYILffhIVQRIPEYLIHLQNVLKF 424
Cdd:pfam00621  78 AP----GFKVYSTYCSNYPKALKLLKkllkknpkfRAFLEELEANPEcrgldlNSFLIK---PVQRIPRYPLLLKELLKH 150

                         170       180
                  ....*....|....*....|....
gi 2024395567 425 TEQEHPDYYLLLVCVQRLRVFISH 448
Cdd:pfam00621 151 TPPDHPDYEDLKKALEAIKEVAKQ 174
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 281-457 1.13e-13

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 70.02  E-value: 1.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  281 IALELLESERKYVINLSLILKI-KATLQGPDVKRSTKE-RSFFPNSLRyLVQQHVDLLHALQERVLSWPRQG-ILGDIFL 357
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVfLKPLKKELKLLSPNElETLFGNIEE-IYEFHRDFLDELEERIEEWDDSVeRIGDVFL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  358 KLtndeNNFLDYYVAYLRDLPECISLIH--------VVILKEVEEEIKSDLYILFFHI---VQRIPEYLIHLQNVLKFTE 426
Cdd:smart00325  80 KL----EEFFKIYSEYCSNHPDALELLKklkknprfQKFLKEIESSPQCRRLTLESLLlkpVQRLTKYPLLLKELLKHTP 155

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024395567  427 QEHPDYYLLLVCVQRLRvfishySLLFQCNE 457
Cdd:smart00325 156 EDHEDREDLKKALKAIK------ELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 278-448 1.19e-13

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 70.02  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 278 RQNIALELLESERKYVINLSLILKI-KATLQGPDVKRSTKER-SFFPNsLRYLVQQHVDLLHALQERVLSWPRQG-ILGD 354
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDKELLPLSPEEVeLLFGN-IEEIYEFHRIFLKSLEERVEEWDKSGpRIGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567 355 IFLKLtndeNNFLDYYVAYLRDLPECISLIH---------VVILKEVEEE-IKSDLYILFFHIVQRIPEYLIHLQNVLKF 424
Cdd:cd00160    80 VFLKL----APFFKIYSEYCSNHPDALELLKklkkfnkffQEFLEKAESEcGRLKLESLLLKPVQRLTKYPLLLKELLKH 155

                         170       180
                  ....*....|....*....|....
gi 2024395567 425 TEQEHPDYYLLLVCVQRLRVFISH 448
Cdd:cd00160   156 TPDGHEDREDLKKALEAIKEVASQ 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-140 4.48e-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: 43.89  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567   29 QSCDWAAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKE---ELSDAKSMI 105
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEleaQLEELESKL 332

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2024395567  106 EEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQK 140
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAEL 367
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-142 5.12e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567   58 ELSRIQHGEYALEEKVKSCRcameEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQKIEQLQQ---EKRRESRKVK 134
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQ----SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLE 750


                   ....*...
gi 2024395567  135 AKRAQKDD 142
Cdd:TIGR02169  751 QEIENVKS 758
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
18-146 1.46e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  18 PATQISQMAPSQSCDWAAERLGALQALASELKAGFTEAMQELSRIQhgeyALEEKVKSCRCAMEEKVAEMKNSLNTFKEE 97
Cdd:COG4372    20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEELNEQLQAAQAE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2024395567  98 LSDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQKDDHSSQ 146
Cdd:COG4372    96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
69-127 2.03e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 38.41  E-value: 2.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  69 LEEKVKSCRCAMEEKVAEMKNSLNTFKEELSD-AKSMIEEISAKQEEMQQKIEQLQQEKR 127
Cdd:COG4980    47 AEDLKDELKEKASELSEEAKEKLDELIEEIKEkIEELKEEVEPKIEELKEEAEKLQKEVE 106
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 41-138 2.34e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  41 LQALASELKAGFTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQKIE 120
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111

                          90
                  ....*....|....*...
gi 2024395567 121 QLQQEKRRESRKVKAKRA 138
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEA 129
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 69-139 2.40e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024395567  69 LEEKVKscrcAMEEKVAEMKNSLNTFKEEL-SDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQ 139
Cdd:pfam03938  24 LEKKFK----KRQAELEAKQKELQKLYEELqKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
34-142 2.44e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  34 AAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVKscrcAMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQE 113
Cdd:COG4372    50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ----AAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                          90       100
                  ....*....|....*....|....*....
gi 2024395567 114 EMQQKIEQLQQEKRRESRKVKAKRAQKDD 142
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKE 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 34-142 2.62e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  34 AAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVkscrcameekvAEMKNSLNTFKEELSDAKSMIEEISAKQE 113
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-----------ARLEQDIARLEERRRELEERLEELEEELA 326

                          90       100
                  ....*....|....*....|....*....
gi 2024395567 114 EMQQKIEQLQQEKRRESRKVKAKRAQKDD 142
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEE 355
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 35-140 2.84e-03

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: 41.21  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567   35 AERLGALQALASELkagfteaMQELSRIQHGEYALEEKVKSCrcamEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEE 114
Cdd:TIGR02169  680 RERLEGLKRELSSL-------QSELRRIENRLDELSQELSDA----SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100
                   ....*....|....*....|....*.
gi 2024395567  115 MQQKIEQLQQEKRRESRKVKAKRAQK 140
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDL 774
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 69-135 3.88e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 36.87  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024395567  69 LEEKVKScrcaMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKA 135
Cdd:COG3074     9 LEAKVQQ----AVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRS 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-146 7.89e-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: 40.04  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567    2 DTNKQEGETESVPVSTPATQISQMAPSQScdwaaERLGALQALASELKAGFTEAMQELSRiqhgeyaLEEKVKSCRCAME 81
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLLNEEAANLRERLES-------LERRIAATERRLE 841

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024395567   82 EKVAEMKNSlntfKEELSDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQKDDHSSQ 146
Cdd:TIGR02168  842 DLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 38-139 8.03e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  38 LGALQALASELKAgfTEAMQELSRIQHGEYALEEKVKscrcAMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQ 117
Cdd:COG4942    10 LLALAAAAQADAA--AEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83

                          90       100
                  ....*....|....*....|..
gi 2024395567 118 KIEQLQQEKRRESRKVKAKRAQ 139
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEE 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 19-156 8.48e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  19 ATQISQMAPSQscdwaAERLGALQALASELKAGFTEAMQELSRIQHGEYALEEKVKscrcAMEEKVAEMKNSLNTFKEEL 98
Cdd:COG3883   121 LSALSKIADAD-----ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA----ELEAQQAEQEALLAQLSAEE 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024395567  99 SDAKSMIEEISAKQEEMQQKIEQLQQEKRRESRKVKAKRAQKDDHSSQTVPTPLQGSP 156
Cdd:COG3883   192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 52-141 9.74e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024395567  52 FTEAMQELSRIQHGEYALEEKVKSCRCAMEEKVAEMKNSLNTFKEELSDAKSMIEEISAKQEEMQQKIEQLQQEKRRESR 131
Cdd:COG3883   117 FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196

                          90
                  ....*....|
gi 2024395567 132 KVKAKRAQKD 141
Cdd:COG3883   197 QLAELEAELA 206
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH