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MobV family relaxase [Barnesiella intestinihominis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MobV NF041497
MobV family relaxase;
6-237 2.85e-48

MobV family relaxase;


:

Pssm-ID: 469385  Cd Length: 187  Bit Score: 165.05  E-value: 2.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939   6 KQAMHVEAGKSFGTAEANENERRWNDDKIdrknqepTNHYDKTRMKLNFEIGSDrkvhplGYQEKSLEVRLQERLTElGW 85
Cdd:NF041497    3 YAVLRVEKLKGGNLAGSQEHNERETENRT-------NPNADPSRTHLNFELVNG------PDGPIDYLEAIKERIAE-NA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  86 KPFKPDSKIQPNCCaKFIFGGNHDRTLEMAfgtqavnldkgaDNSHLqrcpeiEQWAKDVYDWCAKRYGQENIIGFQVHL 165
Cdd:NF041497   69 GIKRKIRKDAVRAV-EFILTGSPEFFKELA------------DPGEL------KEWFEDNYDFLADRYGEENIVSAVVHL 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796382939 166 DESSPHIHALIVPVGQRSKsgrecVMWSAKFGKNRyeygriLREMHTSLYEEVgSKYGLERGDSivGRNVQH 237
Cdd:NF041497  130 DETTPHIHATVVPITEDGR-----LSAKDVFGRKK------LSQLQDDYAEAM-KKYGLERGIS--GSEAKH 187
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-444 1.53e-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: 54.29  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  240 KRDYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRL-------KEIDEALASGKITLDRYEAQKADIQKLITEYQE 312
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  313 KLEDKSNKLHAKEHELEQLTKDAAKARSVIQPFRNHKVDftppqitekvplfgtdkwIERQNRLIAKQFTEIVRKIESLY 392
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ------------------LELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2796382939  393 RNDAARQVEAAQRNVLADYGELYQLRQENKILSDTNENLESELNTLLCQLAI 444
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
 
Name Accession Description Interval E-value
MobV NF041497
MobV family relaxase;
6-237 2.85e-48

MobV family relaxase;


Pssm-ID: 469385  Cd Length: 187  Bit Score: 165.05  E-value: 2.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939   6 KQAMHVEAGKSFGTAEANENERRWNDDKIdrknqepTNHYDKTRMKLNFEIGSDrkvhplGYQEKSLEVRLQERLTElGW 85
Cdd:NF041497    3 YAVLRVEKLKGGNLAGSQEHNERETENRT-------NPNADPSRTHLNFELVNG------PDGPIDYLEAIKERIAE-NA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  86 KPFKPDSKIQPNCCaKFIFGGNHDRTLEMAfgtqavnldkgaDNSHLqrcpeiEQWAKDVYDWCAKRYGQENIIGFQVHL 165
Cdd:NF041497   69 GIKRKIRKDAVRAV-EFILTGSPEFFKELA------------DPGEL------KEWFEDNYDFLADRYGEENIVSAVVHL 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796382939 166 DESSPHIHALIVPVGQRSKsgrecVMWSAKFGKNRyeygriLREMHTSLYEEVgSKYGLERGDSivGRNVQH 237
Cdd:NF041497  130 DETTPHIHATVVPITEDGR-----LSAKDVFGRKK------LSQLQDDYAEAM-KKYGLERGIS--GSEAKH 187
MobM_relaxase cd17242
relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a ...
 34-253 6.58e-34

relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site.


Pssm-ID: 410988  Cd Length: 196  Bit Score: 126.99  E-value: 6.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  34 IDRKNQEPTNHYDKTRMKLNFEIGSDRKvhplgyqeKSLEVRLQERLTELGW-KPFKPDSKIqpncCAKFIFGGNHDRTL 112
Cdd:cd17242    19 NERERETENPNIDPSRTHLNYELVGPGK--------KDYAEAIKERLEELGKkKKIRKDAVL----AVEFILTASPEFFE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 113 EMafgtqavnldkgadnshlqRCPEIEQWAKDVYDWCAKRYGQENIIGFQVHLDESSPHIHALIVPVGQRSKsgrecvmW 192
Cdd:cd17242    87 GL-------------------DPEEIEEFFKDALEFLKERFGEENIVSAVVHLDETTPHLHAVVVPITEDGR-------L 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796382939 193 SAK-FGKNRYEygriLREMHTSLYEEVGSKYGLERGdsIVGRNVQHLHKRDYIRKLAKEAKQ 253
Cdd:cd17242   141 SAKeLFGGRKK----LRELQDDYAEAVAKKGGLERG--IKGSKAKHKTKEKELKAKHEELKE 196
Mob_Pre pfam01076
Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific ...
 137-243 2.94e-09

Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre. Pre is a plasmid recombination enzyme. This protein is also known as Mob (conjugative mobilization). This family is also known as Mob-V. One of the family members, MobM, is encoded by a promiscuous plasmid actively involved in the spread of antibiotic resistance. Homologs of MobM are found in many plasmids and other mobile genetic elements of pathogenic bacteria, including S. aureus. MobM is a metal-dependent nuclease that uses histidine nitrogen for the nucleophilic attack on the scissile phosphate. Furthermore, in contrast to other DNA-processing enzymes, MobM is a histidine relaxase, a DNA-breaking and -joining enzyme, that operates through a phosphorus-nitrogen protein-DNA adduct for cell-to-cell DNA transfer. Mutational analysis indicate that the H(N/D)(Q/E)R N-terminal motif of MobM plays a crucial role in the cleavage and generation of stable DNA-protein adducts.


Pssm-ID: 395854  Cd Length: 195  Bit Score: 56.95  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 137 EIEQWAKDVYDWCAKRYGQENIIGFQVHLDESSPHIHALIVPVGQRSKSgrecvmwSAK-FGKNRYEygriLREMHTSLY 215
Cdd:pfam01076  98 EAKEFFETAFQFFEERYGKENVLYAVVHLDEATPHMHMGVVPGTEDGRL-------SAKaIFGNRKE----LIALQDRFP 166

                          90       100
                  ....*....|....*....|....*....
gi 2796382939 216 EEVGSK-YGLERGdsIVGRNVQHLHKRDY 243
Cdd:pfam01076 167 EYMGLKgFDLERG--EPGSERKHLGTNEY 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-444 1.53e-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: 54.29  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  240 KRDYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRL-------KEIDEALASGKITLDRYEAQKADIQKLITEYQE 312
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  313 KLEDKSNKLHAKEHELEQLTKDAAKARSVIQPFRNHKVDftppqitekvplfgtdkwIERQNRLIAKQFTEIVRKIESLY 392
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ------------------LELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2796382939  393 RNDAARQVEAAQRNVLADYGELYQLRQENKILSDTNENLESELNTLLCQLAI 444
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 249-342 1.67e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 249 KEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLED-KSNK-LHAKEH 326
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKeYEALQK 96

                          90
                  ....*....|....*.
gi 2796382939 327 ELEQLTKDAAKARSVI 342
Cdd:COG1579    97 EIESLKRRISDLEDEI 112
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 242-343 7.67e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 242 DYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALA------SGKITLDRYEAQKADIQKLITEYQEKLE 315
Cdd:cd22656   121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKdlltdeGGAIARKEIKDLQKELEKLNEEYAAKLK 200

                          90       100
                  ....*....|....*....|....*...
gi 2796382939 316 DKSNKLHAKEHELEQLTKDAAKARSVIQ 343
Cdd:cd22656   201 AKIDELKALIADDEAKLAAALRLIADLT 228
PRK12472 PRK12472
hypothetical protein; Provisional
 246-338 8.43e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.78  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 246 KLAKEAKQA----EKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEA----QKADIQKliTEYQEKLEDK 317
Cdd:PRK12472  204 RAADEAKTAaaaaAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAeerqQKAAQQA--AEAATQLDTA 281

                          90       100
                  ....*....|....*....|.
gi 2796382939 318 SNKLHAKEHELEQlTKDAAKA 338
Cdd:PRK12472  282 KADAEAKRAAAAA-TKEAAKA 301
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 250-344 2.86e-03

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 40.13  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 250 EAKQAEKalkgLQAMIRKL-EREMLAGRnRLKEIDEalasgkitldRYEAQKADIQKLITEYQEKLEDKSNKLHAKEHEL 328
Cdd:pfam12004 383 ELKQAEK----YEQEISKLkERLRVSNR-KLEEYER----------RLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEK 447

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2796382939 329 ---------------EQLTKDAAKARSVIQP 344
Cdd:pfam12004 448 dsqmksiisrlmaveEELKKDHAEMQAVIDS 478
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 244-330 9.69e-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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.79  E-value: 9.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQK--ADIQKLITEYQEKLEDKSNKL 321
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKkeKELQKKVQEFQRKQQKLQQDL 85


                   ....*....
gi 2796382939  322 HAKEHELEQ 330
Cdd:smart00935  86 QKRQQEELQ 94
 
Name Accession Description Interval E-value
MobV NF041497
MobV family relaxase;
6-237 2.85e-48

MobV family relaxase;


Pssm-ID: 469385  Cd Length: 187  Bit Score: 165.05  E-value: 2.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939   6 KQAMHVEAGKSFGTAEANENERRWNDDKIdrknqepTNHYDKTRMKLNFEIGSDrkvhplGYQEKSLEVRLQERLTElGW 85
Cdd:NF041497    3 YAVLRVEKLKGGNLAGSQEHNERETENRT-------NPNADPSRTHLNFELVNG------PDGPIDYLEAIKERIAE-NA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  86 KPFKPDSKIQPNCCaKFIFGGNHDRTLEMAfgtqavnldkgaDNSHLqrcpeiEQWAKDVYDWCAKRYGQENIIGFQVHL 165
Cdd:NF041497   69 GIKRKIRKDAVRAV-EFILTGSPEFFKELA------------DPGEL------KEWFEDNYDFLADRYGEENIVSAVVHL 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796382939 166 DESSPHIHALIVPVGQRSKsgrecVMWSAKFGKNRyeygriLREMHTSLYEEVgSKYGLERGDSivGRNVQH 237
Cdd:NF041497  130 DETTPHIHATVVPITEDGR-----LSAKDVFGRKK------LSQLQDDYAEAM-KKYGLERGIS--GSEAKH 187
MobM_relaxase cd17242
relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a ...
 34-253 6.58e-34

relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site.


Pssm-ID: 410988  Cd Length: 196  Bit Score: 126.99  E-value: 6.58e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  34 IDRKNQEPTNHYDKTRMKLNFEIGSDRKvhplgyqeKSLEVRLQERLTELGW-KPFKPDSKIqpncCAKFIFGGNHDRTL 112
Cdd:cd17242    19 NERERETENPNIDPSRTHLNYELVGPGK--------KDYAEAIKERLEELGKkKKIRKDAVL----AVEFILTASPEFFE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 113 EMafgtqavnldkgadnshlqRCPEIEQWAKDVYDWCAKRYGQENIIGFQVHLDESSPHIHALIVPVGQRSKsgrecvmW 192
Cdd:cd17242    87 GL-------------------DPEEIEEFFKDALEFLKERFGEENIVSAVVHLDETTPHLHAVVVPITEDGR-------L 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796382939 193 SAK-FGKNRYEygriLREMHTSLYEEVGSKYGLERGdsIVGRNVQHLHKRDYIRKLAKEAKQ 253
Cdd:cd17242   141 SAKeLFGGRKK----LRELQDDYAEAVAKKGGLERG--IKGSKAKHKTKEKELKAKHEELKE 196
Mob_Pre pfam01076
Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific ...
 137-243 2.94e-09

Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre. Pre is a plasmid recombination enzyme. This protein is also known as Mob (conjugative mobilization). This family is also known as Mob-V. One of the family members, MobM, is encoded by a promiscuous plasmid actively involved in the spread of antibiotic resistance. Homologs of MobM are found in many plasmids and other mobile genetic elements of pathogenic bacteria, including S. aureus. MobM is a metal-dependent nuclease that uses histidine nitrogen for the nucleophilic attack on the scissile phosphate. Furthermore, in contrast to other DNA-processing enzymes, MobM is a histidine relaxase, a DNA-breaking and -joining enzyme, that operates through a phosphorus-nitrogen protein-DNA adduct for cell-to-cell DNA transfer. Mutational analysis indicate that the H(N/D)(Q/E)R N-terminal motif of MobM plays a crucial role in the cleavage and generation of stable DNA-protein adducts.


Pssm-ID: 395854  Cd Length: 195  Bit Score: 56.95  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 137 EIEQWAKDVYDWCAKRYGQENIIGFQVHLDESSPHIHALIVPVGQRSKSgrecvmwSAK-FGKNRYEygriLREMHTSLY 215
Cdd:pfam01076  98 EAKEFFETAFQFFEERYGKENVLYAVVHLDEATPHMHMGVVPGTEDGRL-------SAKaIFGNRKE----LIALQDRFP 166

                          90       100
                  ....*....|....*....|....*....
gi 2796382939 216 EEVGSK-YGLERGdsIVGRNVQHLHKRDY 243
Cdd:pfam01076 167 EYMGLKgFDLERG--EPGSERKHLGTNEY 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-444 1.53e-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: 54.29  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  240 KRDYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRL-------KEIDEALASGKITLDRYEAQKADIQKLITEYQE 312
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanlerqlEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  313 KLEDKSNKLHAKEHELEQLTKDAAKARSVIQPFRNHKVDftppqitekvplfgtdkwIERQNRLIAKQFTEIVRKIESLY 392
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ------------------LELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2796382939  393 RNDAARQVEAAQRNVLADYGELYQLRQENKILSDTNENLESELNTLLCQLAI 444
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 249-342 1.67e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.15  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 249 KEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLED-KSNK-LHAKEH 326
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKeYEALQK 96

                          90
                  ....*....|....*.
gi 2796382939 327 ELEQLTKDAAKARSVI 342
Cdd:COG1579    97 EIESLKRRISDLEDEI 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 242-443 7.16e-06

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: 48.22  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 242 DYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLEDKSNKL 321
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 322 HAKEHELEQLTKDAAKARSVIQPfrnhKVDFTPPQITEKVPLFgtdKWIERQNRLIAKQFTEIVRKIESLyrnDAARQVE 401
Cdd:COG4942   100 EAQKEELAELLRALYRLGRQPPL----ALLLSPEDFLDAVRRL---QYLKYLAPARREQAEELRADLAEL---AALRAEL 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2796382939 402 AAQRNvladygELYQLRQENKILSDTNENLESELNTLLCQLA 443
Cdd:COG4942   170 EAERA------ELEALLAELEEERAALEALKAERQKLLARLE 205
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-343 1.92e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 244 IRKLAKEAKQAEKALKgLQAMIRKLEREMLAgrNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLEDKSNKLHA 323
Cdd:COG1196   202 LEPLERQAEKAERYRE-LKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                          90       100
                  ....*....|....*....|
gi 2796382939 324 KEHELEQLTKDAAKARSVIQ 343
Cdd:COG1196   279 LELELEEAQAEEYELLAELA 298
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-438 2.76e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  244 IRKLAKEAKQAEKaLKGLQAMIRKLEREMLAgrNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLEDKSNKLHA 323
Cdd:TIGR02168  202 LKSLERQAEKAER-YKELKAELRELELALLV--LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  324 KEHELEQLTK---------DAAKARSVIQPFRNHKVDFTPPQITEKVPLFGTDKwIERQNRL--IAKQFTEIVRKIESL- 391
Cdd:TIGR02168  279 LEEEIEELQKelyalaneiSRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELaeLEEKLEELKEELESLe 357

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2796382939  392 --------YRNDAARQVEAAQRNVLADYGELYQLRQENKILSDTNENLESELNTL 438
Cdd:TIGR02168  358 aeleeleaELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 250-442 2.65e-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: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  250 EAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQ-------EKLEDKSNKLH 322
Cdd:TIGR02169  288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrdkltEEYAELKEELE 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  323 AKEHELEQLTKDAAKARSVIQPFRNHKVDFTppqiTEKVPLFGT-DKWIERQNRLIAKQfTEIVRKIESLY--------- 392
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLK----REINELKRElDRLQEELQRLSEEL-ADLNAAIAGIEakineleee 442

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2796382939  393 RNDAARQVEAAQRN------VLADY-GELYQLRQENKILSDTNENLESELNTLLCQL 442
Cdd:TIGR02169  443 KEDKALEIKKQEWKleqlaaDLSKYeQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-435 6.81e-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: 42.36  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  240 KRDYIRKLAKEAKQA-----------EKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLIT 308
Cdd:TIGR02169  696 ELRRIENRLDELSQElsdasrkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  309 EYQEKLEDKSNKLhaKEHELEQLTKDAAKARSVIQPFRN---------HKVDFTPPQITEKVplfgtdKWIERQNRLIAK 379
Cdd:TIGR02169  776 KLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEArlreieqklNRLTLEKEYLEKEI------QELQEQRIDLKE 847

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2796382939  380 QFTEIVRKIESLYRNDAARQVEAAQRNvladyGELYQLRQENKILSDTNENLESEL 435
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELE-----AALRDLESRLGDLKKERDELEAQL 898
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 242-343 7.67e-04

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 242 DYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALA------SGKITLDRYEAQKADIQKLITEYQEKLE 315
Cdd:cd22656   121 ALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKdlltdeGGAIARKEIKDLQKELEKLNEEYAAKLK 200

                          90       100
                  ....*....|....*....|....*...
gi 2796382939 316 DKSNKLHAKEHELEQLTKDAAKARSVIQ 343
Cdd:cd22656   201 AKIDELKALIADDEAKLAAALRLIADLT 228
PRK12472 PRK12472
hypothetical protein; Provisional
 246-338 8.43e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.78  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 246 KLAKEAKQA----EKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEA----QKADIQKliTEYQEKLEDK 317
Cdd:PRK12472  204 RAADEAKTAaaaaAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAeerqQKAAQQA--AEAATQLDTA 281

                          90       100
                  ....*....|....*....|.
gi 2796382939 318 SNKLHAKEHELEQlTKDAAKA 338
Cdd:PRK12472  282 KADAEAKRAAAAA-TKEAAKA 301
PRK00106 PRK00106
ribonuclease Y;
239-336 1.47e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 41.01  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 239 HKRDYIRKLAKEAKQAEKALKGLQAM--IRK----LEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQE 312
Cdd:PRK00106   53 RDAEHIKKTAKRESKALKKELLLEAKeeARKyreeIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQ 132

                          90       100
                  ....*....|....*....|....
gi 2796382939 313 KLEDKSNKLHAKEHELEQLTKDAA 336
Cdd:PRK00106  133 SLTDKSKHIDEREEQVEKLEEQKK 156
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 244-338 1.98e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 40.70  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKI-----TLDRYEAQKADIQKLITEYQEKLEDKS 318
Cdd:PRK05035  438 IRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKdavaaALARVKAKKAAATQPIVIKAGARPDNS 517

                          90       100
                  ....*....|....*....|
gi 2796382939 319 NKLHAKEHELEQLTKDAAKA 338
Cdd:PRK05035  518 AVIAAREARKAQARARQAEK 537
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-435 2.09e-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: 40.82  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  240 KRDYIRKLAKEAKQAEKaLKGLQAMIRKLEremlaGRNRLKEIDEALASgkitLDRYEAQKADIQKLITEYQEKLEDKSN 319
Cdd:TIGR02169  196 KRQQLERLRREREKAER-YQALLKEKREYE-----GYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  320 KLHAKEHELEQLTKDAAKARSVIQpfrnhkvdftpPQITEKVPLFGTDkwIERQNRLIA------KQFTEIVRKIESLYR 393
Cdd:TIGR02169  266 RLEEIEQLLEELNKKIKDLGEEEQ-----------LRVKEKIGELEAE--IASLERSIAekerelEDAEERLAKLEAEID 332

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2796382939  394 NdAARQVEAAQRNVLADYGELYQLRQENKILSDTNENLESEL 435
Cdd:TIGR02169  333 K-LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
241-406 2.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 241 RDYIRKLAKEAKQAEKALKGLQAmIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEK---LEDK 317
Cdd:PRK03918  265 EERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEEL 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 318 SNKLHAKEHELEQLTKDA---AKARSVIQPFRNHKVDFTPPQITEkvplfgtdkwIERQNRLIAKQFTEIVRKIESLYRN 394
Cdd:PRK03918  344 KKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLTPEK----------LEKELEELEKAKEEIEEEISKITAR 413

                         170
                  ....*....|..
gi 2796382939 395 DAARQVEAAQRN 406
Cdd:PRK03918  414 IGELKKEIKELK 425
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 250-344 2.86e-03

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 40.13  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 250 EAKQAEKalkgLQAMIRKL-EREMLAGRnRLKEIDEalasgkitldRYEAQKADIQKLITEYQEKLEDKSNKLHAKEHEL 328
Cdd:pfam12004 383 ELKQAEK----YEQEISKLkERLRVSNR-KLEEYER----------RLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEK 447

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2796382939 329 ---------------EQLTKDAAKARSVIQP 344
Cdd:pfam12004 448 dsqmksiisrlmaveEELKKDHAEMQAVIDS 478
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 244-330 6.41e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 37.51  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITL--DRYEAQKADIQKLITEYQEKLEDKSNKL 321
Cdd:COG2825    31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLseEERQKKERELQKKQQELQRKQQEAQQDL 110


                  ....*....
gi 2796382939 322 HAKEHELEQ 330
Cdd:COG2825   111 QKRQQELLQ 119
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-339 6.48e-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: 39.27  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQKADIQKLITEYQEKLEDKSNKLHA 323
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870

                           90
                   ....*....|....*.
gi 2796382939  324 KEHELEQLTKDAAKAR 339
Cdd:TIGR02168  871 LESELEALLNERASLE 886
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 244-343 6.68e-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: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKE---------------------------IDEALASGKIT---L 293
Cdd:COG3883    53 YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgsesfsdfLDRLSALSKIAdadA 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2796382939 294 DRYEAQKADIQKLiTEYQEKLEDKSNKLHAKEHELEQLTKDAAKARSVIQ 343
Cdd:COG3883   133 DLLEELKADKAEL-EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 240-340 7.34e-03

Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.


Pssm-ID: 398808 [Multi-domain]  Cd Length: 180  Bit Score: 37.54  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939 240 KRDYIRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASG---------------------KITLDRYEA 298
Cdd:pfam05335  36 KNQLADKALQAAKAAEAALAGKQQIVEQLEQELREAEAVVQEESASLQQSqananaaqraaqqaqqqlealTAALKAAQA 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2796382939 299 QKADIQKLITEYQEKLEDKSNKLHAKEHELEQLTKDAAKARS 340
Cdd:pfam05335 116 NLENAEQVAAGAQQELAEKTQLLEAAKKRVERLQRQLAEARA 157
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 244-330 9.69e-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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.79  E-value: 9.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796382939  244 IRKLAKEAKQAEKALKGLQAMIRKLEREMLAGRNRLKEIDEALASGKITLDRYEAQK--ADIQKLITEYQEKLEDKSNKL 321
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKkeKELQKKVQEFQRKQQKLQQDL 85


                   ....*....
gi 2796382939  322 HAKEHELEQ 330
Cdd:smart00935  86 QKRQQEELQ 94
 
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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