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Conserved domains on  [gi|1958969986|ref|WP_201503309|]
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MobA/MobL family protein, partial [Psychrobacter aquimaris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MobA_MobL super family cl37690
MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, ...
20-256 6.45e-39

MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, and the MobL protein from the Thiobacillus ferrooxidans plasmid PTF1. These sequences are mobilization proteins, which are essential for specific plasmid transfer.


The actual alignment was detected with superfamily member pfam03389:

Pssm-ID: 427275 [Multi-domain]  Cd Length: 217  Bit Score: 142.44  E-value: 6.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  20 SVVAKSAYNSGSKLVDEQSGVVHDYTSKakdkilnlvdsdgtkytqvveKNVVHTALITPTLAGDLAVTREGFWNDIERI 99
Cdd:pfam03389   2 SAVAAAAYRSGEKLHDERTGRTHDYTRK---------------------KGVVHSEILLPENAPEWAADRETLWNAVEAF 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 100 ETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQTLSDRYNVLVDVAIHRPHSHekhvgevevveltsrNFHAHILLSSR 179
Cdd:pfam03389  61 EKRKDAQLAREFEVALPRELSPEQRIELAREFVQENFVSKGMVADWAIHDPHPG---------------NPHAHIMLTTR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 180 EIVADVEGYALSARKNW----LQWSTEERLSKGLNGRgDELKYQRTLWADMANELLPKN---KTISEKSYRELGINRLPK 252
Cdd:pfam03389 126 PLDEDGFWGKKVRKEDEngekIRFKSGKIDTRDWNDK-EQLKEWREAWADLANQHLALAgidERIDHRSYAEQGIDLIPT 204

                  ....
gi 1958969986 253 MKLG 256
Cdd:pfam03389 205 IHEG 208
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
260-526 3.45e-03

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: 40.44  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  260 YKDILKGNRSVIHEYNETIDEINAYIEKnglvieyddkgrIDLESNEQEVNGVTIHYKK-RKPFARIELSnirfvdpAVE 338
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALND------------LEARLSHSRIPEIQAELSKlEEEVSRIEAR-------LRE 816
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  339 LEPAIpksNSQTHSDAANDHALDELLAISADFVSQKKMVRSA---LFSTIDALHEELAHQSKQIITIDKNIKSTQRFTEE 415
Cdd:TIGR02169  817 IEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  416 VGQDYSTSRQKMIELARQISTKEQ--SEALKTALVLVEEFRQ-DDTLQTGRAVTSLEKQLSQIDKIVLNNKAMLEKLIPL 492
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKrlSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958969986  493 NNEVIADYKGLKATLKPFAAKLNKLATGFKALDE 526
Cdd:TIGR02169  974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
 
Name Accession Description Interval E-value
MobA_MobL pfam03389
MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, ...
20-256 6.45e-39

MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, and the MobL protein from the Thiobacillus ferrooxidans plasmid PTF1. These sequences are mobilization proteins, which are essential for specific plasmid transfer.


Pssm-ID: 427275 [Multi-domain]  Cd Length: 217  Bit Score: 142.44  E-value: 6.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  20 SVVAKSAYNSGSKLVDEQSGVVHDYTSKakdkilnlvdsdgtkytqvveKNVVHTALITPTLAGDLAVTREGFWNDIERI 99
Cdd:pfam03389   2 SAVAAAAYRSGEKLHDERTGRTHDYTRK---------------------KGVVHSEILLPENAPEWAADRETLWNAVEAF 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 100 ETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQTLSDRYNVLVDVAIHRPHSHekhvgevevveltsrNFHAHILLSSR 179
Cdd:pfam03389  61 EKRKDAQLAREFEVALPRELSPEQRIELAREFVQENFVSKGMVADWAIHDPHPG---------------NPHAHIMLTTR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 180 EIVADVEGYALSARKNW----LQWSTEERLSKGLNGRgDELKYQRTLWADMANELLPKN---KTISEKSYRELGINRLPK 252
Cdd:pfam03389 126 PLDEDGFWGKKVRKEDEngekIRFKSGKIDTRDWNDK-EQLKEWREAWADLANQHLALAgidERIDHRSYAEQGIDLIPT 204

                  ....
gi 1958969986 253 MKLG 256
Cdd:pfam03389 205 IHEG 208
TraA_Ti TIGR02768
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ...
6-257 5.50e-36

Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.


Pssm-ID: 274289 [Multi-domain]  Cd Length: 744  Bit Score: 144.18  E-value: 5.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986   6 FHLSVSAVSKAKNHSVVAKSAYNSGSKLVDEQSGVVHDYTSKAkdkilnlvdsdgtkytqvvekNVVHTALITPTLAGDL 85
Cdd:TIGR02768   4 YHLSASIISRSSGRSAVAAAAYRSAARLVDERIGRVFDFTRKD---------------------GVAHSEIVLPDGAPDS 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  86 AVTREGFWNDIERIETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQTLSDRYNVLVDVAIHrphSHEKhvgevevvel 165
Cdd:TIGR02768  63 FLERAALWNAVEAAEKRKDAQLAREFEIALPRELNLEQNIELARRFVRDHFVEKGMVADWAIH---DDGD---------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 166 tsRNFHAHILLSSREIVADvegyALSARKNwLQWSTEERLSKGLNGRGDELKYQRTLWADMANELLPKNK---TISEKSY 242
Cdd:TIGR02768 130 --GNPHAHLLTTTRPLEEN----GFGAKKV-RVLGEDGQPYEFWAGSKEDLDYWREQWAELANEHLAEAGldlRIDHRSY 202
                         250
                  ....*....|....*
gi 1958969986 243 RELGINRLPKMKLGK 257
Cdd:TIGR02768 203 AEQGIDLIPTKHIGV 217
PRK13889 PRK13889
conjugal transfer relaxase TraA; Provisional
6-256 1.77e-17

conjugal transfer relaxase TraA; Provisional


Pssm-ID: 237546 [Multi-domain]  Cd Length: 988  Bit Score: 86.67  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986   6 FHLSVSAVSKAKNHSVVAKSAYNSGSKLVDEQSGVVHDYTSKAkdkilnlvdsdgtkytqvvekNVVHTALITPTLAGDL 85
Cdd:PRK13889    4 YHLHVKVIGRKAGSSAVASAAYRSASRLRDERLDRSHDFSAKR---------------------GVVHSEVMLPEGAPEA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  86 AVTREGFWNDIERIETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQ-TLSDRyNVLVDVAIHRphshekhvgevEVVE 164
Cdd:PRK13889   63 WSDRERLWNDVEAFEKRKDAQLAREVEFAIPREMTQAQGIELARDFVQaEFVDR-GMIADLNVHW-----------DIGE 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 165 LTSRNFHAHILLSSREIvaDVEGYALSARknwlQWSteerlskglngRGDELKYQRTLWADMANELLPK---NKTISEKS 241
Cdd:PRK13889  131 DGMAKPHAHVMLTMRAV--DENGFGAKVR----DWN-----------RTELVERWRERWAELANERLAEldiDARIDHRS 193
                         250
                  ....*....|....*
gi 1958969986 242 YRELGINRLPKMKLG 256
Cdd:PRK13889  194 LEAQGIALEPQSQIG 208
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
260-526 3.45e-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: 40.44  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  260 YKDILKGNRSVIHEYNETIDEINAYIEKnglvieyddkgrIDLESNEQEVNGVTIHYKK-RKPFARIELSnirfvdpAVE 338
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALND------------LEARLSHSRIPEIQAELSKlEEEVSRIEAR-------LRE 816
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  339 LEPAIpksNSQTHSDAANDHALDELLAISADFVSQKKMVRSA---LFSTIDALHEELAHQSKQIITIDKNIKSTQRFTEE 415
Cdd:TIGR02169  817 IEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  416 VGQDYSTSRQKMIELARQISTKEQ--SEALKTALVLVEEFRQ-DDTLQTGRAVTSLEKQLSQIDKIVLNNKAMLEKLIPL 492
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKrlSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958969986  493 NNEVIADYKGLKATLKPFAAKLNKLATGFKALDE 526
Cdd:TIGR02169  974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
383-549 4.66e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 383 STIDALHEELAHQSKQIITIDKNIKSTQRFTEEVGQDYSTSRQKMIELARQISTKEQSEALKTALvLVEEFRqdDTLQTG 462
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGERAR--ALYRSG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 463 RAVTSLE-----KQLSQidkiVLNNKAMLEKLIPLNNEVIADYKGLKATLKPFAAKL-NKLATGFKALDEIDIEKSDLSL 536
Cdd:COG3883   100 GSVSYLDvllgsESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEAAKAELEA 175
                         170
                  ....*....|...
gi 1958969986 537 QWDQAFADLQEID 549
Cdd:COG3883   176 QQAEQEALLAQLS 188
 
Name Accession Description Interval E-value
MobA_MobL pfam03389
MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, ...
20-256 6.45e-39

MobA/MobL family; This family includes of the MobA protein from the E. coli plasmid RSF1010, and the MobL protein from the Thiobacillus ferrooxidans plasmid PTF1. These sequences are mobilization proteins, which are essential for specific plasmid transfer.


Pssm-ID: 427275 [Multi-domain]  Cd Length: 217  Bit Score: 142.44  E-value: 6.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  20 SVVAKSAYNSGSKLVDEQSGVVHDYTSKakdkilnlvdsdgtkytqvveKNVVHTALITPTLAGDLAVTREGFWNDIERI 99
Cdd:pfam03389   2 SAVAAAAYRSGEKLHDERTGRTHDYTRK---------------------KGVVHSEILLPENAPEWAADRETLWNAVEAF 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 100 ETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQTLSDRYNVLVDVAIHRPHSHekhvgevevveltsrNFHAHILLSSR 179
Cdd:pfam03389  61 EKRKDAQLAREFEVALPRELSPEQRIELAREFVQENFVSKGMVADWAIHDPHPG---------------NPHAHIMLTTR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 180 EIVADVEGYALSARKNW----LQWSTEERLSKGLNGRgDELKYQRTLWADMANELLPKN---KTISEKSYRELGINRLPK 252
Cdd:pfam03389 126 PLDEDGFWGKKVRKEDEngekIRFKSGKIDTRDWNDK-EQLKEWREAWADLANQHLALAgidERIDHRSYAEQGIDLIPT 204

                  ....
gi 1958969986 253 MKLG 256
Cdd:pfam03389 205 IHEG 208
TraA_Ti TIGR02768
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ...
6-257 5.50e-36

Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.


Pssm-ID: 274289 [Multi-domain]  Cd Length: 744  Bit Score: 144.18  E-value: 5.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986   6 FHLSVSAVSKAKNHSVVAKSAYNSGSKLVDEQSGVVHDYTSKAkdkilnlvdsdgtkytqvvekNVVHTALITPTLAGDL 85
Cdd:TIGR02768   4 YHLSASIISRSSGRSAVAAAAYRSAARLVDERIGRVFDFTRKD---------------------GVAHSEIVLPDGAPDS 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  86 AVTREGFWNDIERIETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQTLSDRYNVLVDVAIHrphSHEKhvgevevvel 165
Cdd:TIGR02768  63 FLERAALWNAVEAAEKRKDAQLAREFEIALPRELNLEQNIELARRFVRDHFVEKGMVADWAIH---DDGD---------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 166 tsRNFHAHILLSSREIVADvegyALSARKNwLQWSTEERLSKGLNGRGDELKYQRTLWADMANELLPKNK---TISEKSY 242
Cdd:TIGR02768 130 --GNPHAHLLTTTRPLEEN----GFGAKKV-RVLGEDGQPYEFWAGSKEDLDYWREQWAELANEHLAEAGldlRIDHRSY 202
                         250
                  ....*....|....*
gi 1958969986 243 RELGINRLPKMKLGK 257
Cdd:TIGR02768 203 AEQGIDLIPTKHIGV 217
PRK13889 PRK13889
conjugal transfer relaxase TraA; Provisional
6-256 1.77e-17

conjugal transfer relaxase TraA; Provisional


Pssm-ID: 237546 [Multi-domain]  Cd Length: 988  Bit Score: 86.67  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986   6 FHLSVSAVSKAKNHSVVAKSAYNSGSKLVDEQSGVVHDYTSKAkdkilnlvdsdgtkytqvvekNVVHTALITPTLAGDL 85
Cdd:PRK13889    4 YHLHVKVIGRKAGSSAVASAAYRSASRLRDERLDRSHDFSAKR---------------------GVVHSEVMLPEGAPEA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  86 AVTREGFWNDIERIETRKNAQLGTEIDVMFPDGITADQRIVLVERYAQ-TLSDRyNVLVDVAIHRphshekhvgevEVVE 164
Cdd:PRK13889   63 WSDRERLWNDVEAFEKRKDAQLAREVEFAIPREMTQAQGIELARDFVQaEFVDR-GMIADLNVHW-----------DIGE 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 165 LTSRNFHAHILLSSREIvaDVEGYALSARknwlQWSteerlskglngRGDELKYQRTLWADMANELLPK---NKTISEKS 241
Cdd:PRK13889  131 DGMAKPHAHVMLTMRAV--DENGFGAKVR----DWN-----------RTELVERWRERWAELANERLAEldiDARIDHRS 193
                         250
                  ....*....|....*
gi 1958969986 242 YRELGINRLPKMKLG 256
Cdd:PRK13889  194 LEAQGIALEPQSQIG 208
PRK13826 PRK13826
Dtr system oriT relaxase; Provisional
7-128 8.43e-08

Dtr system oriT relaxase; Provisional


Pssm-ID: 237524 [Multi-domain]  Cd Length: 1102  Bit Score: 55.56  E-value: 8.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986    7 HLSVSAVSKAKNHSVVAKSAYNSGSKLVDEQSGVVHDYTSKakdkilnlvdsdgtkytqvveKNVVHTALITP------- 79
Cdd:PRK13826     5 HFSVSIVSRGSGRSAVLSAAYRHCAKMEYEREARTIDYTRK---------------------QGLLHEEFVLPadapewv 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958969986   80 -TLAGDLAVT--REGFWNDIERIETRKNAQLGTEIDVMFPDGITADQRIVLV 128
Cdd:PRK13826    64 rSMIADRSVSgaSEAFWNKVEAFEKRSDAQLAKDVTIALPLELTAEQNIALV 115
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
260-526 3.45e-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: 40.44  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  260 YKDILKGNRSVIHEYNETIDEINAYIEKnglvieyddkgrIDLESNEQEVNGVTIHYKK-RKPFARIELSnirfvdpAVE 338
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALND------------LEARLSHSRIPEIQAELSKlEEEVSRIEAR-------LRE 816
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  339 LEPAIpksNSQTHSDAANDHALDELLAISADFVSQKKMVRSA---LFSTIDALHEELAHQSKQIITIDKNIKSTQRFTEE 415
Cdd:TIGR02169  817 IEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986  416 VGQDYSTSRQKMIELARQISTKEQ--SEALKTALVLVEEFRQ-DDTLQTGRAVTSLEKQLSQIDKIVLNNKAMLEKLIPL 492
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKrlSELKAKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958969986  493 NNEVIADYKGLKATLKPFAAKLNKLATGFKALDE 526
Cdd:TIGR02169  974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
383-549 4.66e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 383 STIDALHEELAHQSKQIITIDKNIKSTQRFTEEVGQDYSTSRQKMIELARQISTKEQSEALKTALvLVEEFRqdDTLQTG 462
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGERAR--ALYRSG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958969986 463 RAVTSLE-----KQLSQidkiVLNNKAMLEKLIPLNNEVIADYKGLKATLKPFAAKL-NKLATGFKALDEIDIEKSDLSL 536
Cdd:COG3883   100 GSVSYLDvllgsESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEAAKAELEA 175
                         170
                  ....*....|...
gi 1958969986 537 QWDQAFADLQEID 549
Cdd:COG3883   176 QQAEQEALLAQLS 188
 
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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