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Conserved domains on  [gi|1622886769|ref|XP_014976253|]
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centromere protein J isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 908-1076 8.03e-09

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: 60.08  E-value: 8.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKElaRIEEfKKEEMRKLQKERKVFEKY----- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARlreie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  983 -STAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLR---SQIEMLVRENTDLREEIKVMERFRLDAWKRA 1058
Cdd:TIGR02169  819 qKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180
                   ....*....|....*....|...
gi 1622886769 1059 EAVER-----SLEVEKKDKLANT 1076
Cdd:TIGR02169  899 RELERkieelEAQIEKKRKRLSE 921
CUPID super family cl13287
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
 315-400 4.04e-03

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


The actual alignment was detected with superfamily member pfam11819:

Pssm-ID: 463360  Cd Length: 136  Bit Score: 38.83  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  315 DSSEVANIEERPIKAAIRERKQTfedyLEEQIRLEEQELKQKQLREAE--GPL----PIKAKPKKPFLKRGEGLARFTNA 388
Cdd:pfam11819   20 DSSTSSEKQKKEKTAALKKKQQA----LQERLELKLEELKKLCLREAEltGKLpkeyPLEPGEKPPQVRRRVGTAFKLDE 95

                           90
                   ....*....|..
gi 1622886769  389 KSKFQKGKESKL 400
Cdd:pfam11819   96 QHVLQYAEDPEL 107
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 908-1076 8.03e-09

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: 60.08  E-value: 8.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKElaRIEEfKKEEMRKLQKERKVFEKY----- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARlreie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  983 -STAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLR---SQIEMLVRENTDLREEIKVMERFRLDAWKRA 1058
Cdd:TIGR02169  819 qKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180
                   ....*....|....*....|...
gi 1622886769 1059 EAVER-----SLEVEKKDKLANT 1076
Cdd:TIGR02169  899 RELERkieelEAQIEKKRKRLSE 921
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
903-1060 1.79e-08

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 58.72  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLaklrierESALEKLRKEIADFEqqkakelARIEEFKKEEMRKLQKERKVfeky 982
Cdd:COG2433    406 RELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLE-------RELSEARSEERREIRKDREI---- 467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622886769  983 staartfpdKKEREEIQTLKQQIADLREDLKRKETKWSsthgRLRSQIEMLVRENTdlrEEIKVMERFRLDAWKRAEA 1060
Cdd:COG2433    468 ---------SRLDREIERLERELEEERERIEELKRKLE----RLKELWKLEHSGEL---VPVKVVEKFTKEAIRRLEE 529
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
925-1066 8.50e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  925 ENASLAKLRIER-----ESALEKLRKEIADFEQ-----------QKAKEL-ARIEEFkkEEMRKLQKERKvfekySTAAR 987
Cdd:PRK02224   169 ERASDARLGVERvlsdqRGSLDQLKAQIEEKEEkdlherlngleSELAELdEEIERY--EEQREQARETR-----DEADE 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  988 TFPDKKE-REEIQTLKQQIADLREDLKRKETKWSSTHGR---LRSQIEMLVRENTDLREE-------IKVMERFRLDAWK 1056
Cdd:PRK02224   242 VLEEHEErREELETLEAEIEDLRETIAETEREREELAEEvrdLRERLEELEEERDDLLAEaglddadAEAVEARREELED 321

                          170
                   ....*....|
gi 1622886769 1057 RAEAVERSLE 1066
Cdd:PRK02224   322 RDEELRDRLE 331
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
914-1062 4.56e-04

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 43.00  E-value: 4.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  914 ELETEIEKFKAENASLAKLRIERESA--LEKLRKEIADFEQQKAKELARIEEFKkEEMRKLQKERKVFEKYSTAAR---T 988
Cdd:NF033927     8 ALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNELA-EDRKVIIEAIDLIEKYNIADLfkdL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  989 FPDKKE-------REEIQTLKQQIadlrEDLKRKETKWSS---------THGRLRSQIEMLVRENTDLREEIKVMErFRL 1052
Cdd:NF033927    87 LPTAEEidslglpPPEKDLVKAAI----ERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKALA-GKL 161

                          170
                   ....*....|
gi 1622886769 1053 DAWKRAEAVE 1062
Cdd:NF033927   162 EELTAIAAID 171
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 910-1007 8.74e-04

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: 40.64  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  910 EKIIEletEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKYSTAARTF 989
Cdd:pfam03938    8 QKILE---ESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84

                           90
                   ....*....|....*...
gi 1622886769  990 PDKKEREEIQTLKQQIAD 1007
Cdd:pfam03938   85 LQKKQQELLQPIQDKINK 102
CUPID pfam11819
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
 315-400 4.04e-03

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


Pssm-ID: 463360  Cd Length: 136  Bit Score: 38.83  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  315 DSSEVANIEERPIKAAIRERKQTfedyLEEQIRLEEQELKQKQLREAE--GPL----PIKAKPKKPFLKRGEGLARFTNA 388
Cdd:pfam11819   20 DSSTSSEKQKKEKTAALKKKQQA----LQERLELKLEELKKLCLREAEltGKLpkeyPLEPGEKPPQVRRRVGTAFKLDE 95

                           90
                   ....*....|..
gi 1622886769  389 KSKFQKGKESKL 400
Cdd:pfam11819   96 QHVLQYAEDPEL 107
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 902-985 8.92e-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: 37.95  E-value: 8.92e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769   902 NARSQVLREKIIELETEIEKFKAENASL-AKLRIERESALEKLRKEIADFEQQKAKELARIEEfkkEEMRKLQKE-RKVF 979
Cdd:smart00935   28 KKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ---EELQKILDKiNKAI 104


                    ....*.
gi 1622886769   980 EKYSTA 985
Cdd:smart00935  105 KEVAKK 110
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 908-1076 8.03e-09

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: 60.08  E-value: 8.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKElaRIEEfKKEEMRKLQKERKVFEKY----- 982
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPE-IQAELSKLEEEVSRIEARlreie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  983 -STAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLR---SQIEMLVRENTDLREEIKVMERFRLDAWKRA 1058
Cdd:TIGR02169  819 qKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          170       180
                   ....*....|....*....|...
gi 1622886769 1059 EAVER-----SLEVEKKDKLANT 1076
Cdd:TIGR02169  899 RELERkieelEAQIEKKRKRLSE 921
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
903-1060 1.79e-08

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 58.72  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLaklrierESALEKLRKEIADFEqqkakelARIEEFKKEEMRKLQKERKVfeky 982
Cdd:COG2433    406 RELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLE-------RELSEARSEERREIRKDREI---- 467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622886769  983 staartfpdKKEREEIQTLKQQIADLREDLKRKETKWSsthgRLRSQIEMLVRENTdlrEEIKVMERFRLDAWKRAEA 1060
Cdd:COG2433    468 ---------SRLDREIERLERELEEERERIEELKRKLE----RLKELWKLEHSGEL---VPVKVVEKFTKEAIRRLEE 529
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 900-1081 3.80e-08

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: 57.76  E-value: 3.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  900 GDNARSQVL---REKIIELETEIEKFKAENAS----LAKLRIER---ESALEKLRKEIADFEQQKAKELARIEEFKKE-- 967
Cdd:TIGR02168  664 GSAKTNSSIlerRREIEELEEKIEELEEKIAElekaLAELRKELeelEEELEQLRKELEELSRQISALRKDLARLEAEve 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  968 ----EMRKLQKERKVFEKYSTAART-----FPDKKERE-EIQTLKQQIADLREDLKrketKWSSTHGRLRSQIEMLVREN 1037
Cdd:TIGR02168  744 qleeRIAQLSKELTELEAEIEELEErleeaEEELAEAEaEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEA 819

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622886769 1038 TDLREEIKVMERFRLDAWKRAEAVERSLEVEKKDKLANTSVRFQ 1081
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1085 4.41e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 4.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEK 981
Cdd:COG1196    287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 YSTAARTFPDKKE-----REEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKVMERFRLDAWK 1056
Cdd:COG1196    367 LLEAEAELAEAEEeleelAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                          170       180
                   ....*....|....*....|....*....
gi 1622886769 1057 RAEAVERSLEVEKKDKLANTSVRFQNNQI 1085
Cdd:COG1196    447 AAEEEAELEEEEEALLELLAELLEEAALL 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1084 4.81e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEK 981
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 YSTAARTfpDKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKvmerfRLDAWKRAEAV 1061
Cdd:COG1196    318 LEELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-----ELEELAEELLE 390

                          170       180
                   ....*....|....*....|...
gi 1622886769 1062 ERSLEVEKKDKLANTSVRFQNNQ 1084
Cdd:COG1196    391 ALRAAAELAAQLEELEEAEEALL 413
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
904-1049 6.82e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 6.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  904 RSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIAdfeQQKAKELARIEEFKKEEMRKLQKERKVFEKYS 983
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRRARLE 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622886769  984 TAART--FPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKVMER 1049
Cdd:COG4913    366 ALLAAlgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
891-1074 5.60e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 5.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  891 LNISQDQPPGDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESA---LEKLRKEIADFEQQKA-----KELARIE 962
Cdd:COG4717     59 FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLQllplyQELEALE 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  963 EFKKEEMRKLQKERKVFEKYSTAartfpdkkeREEIQTLKQQIADLREDLKRKETKWSSTHgrlRSQIEMLVRENTDLRE 1042
Cdd:COG4717    139 AELAELPERLEELEERLEELREL---------EEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAEELEELQQ 206

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622886769 1043 EIKVMERFRLDAWKRAEAVERSLEVEKKDKLA 1074
Cdd:COG4717    207 RLAELEEELEEAQEELEELEEELEQLENELEA 238
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 906-1044 1.92e-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: 50.31  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  906 QVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQ-----KAKELARIEefkkEEMRKLQKERKVFE 980
Cdd:COG1579     34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQ----KEIESLKRRISDLE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622886769  981 KystAARTFPDKKE--REEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEI 1044
Cdd:COG1579    110 D---EILELMERIEelEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 908-1048 2.28e-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: 49.92  E-value: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKK--------EEMRKLQKErkvf 979
Cdd:COG1579     22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnKEYEALQKE---- 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622886769  980 EKYSTAARTFPDKKERE---EIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKVME 1048
Cdd:COG1579     98 IESLKRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 903-1057 3.87e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFkKEEMRKLQKERKVFEKY 982
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL-EARLERLEDRRERLQQE 422

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622886769  983 STAARTFPDKKEREEIQ----TLKQQIADLREDLKRKETKWSsthgRLRSQIEMLVRENTDLREEIKVMeRFRLDAWKR 1057
Cdd:TIGR02168  423 IEELLKKLEEAELKELQaeleELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQL-QARLDSLER 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1075 4.74e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 4.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEK 981
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 YSTAARTFpdKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKVMERFRLDAWKRAEAV 1061
Cdd:TIGR02168  896 LEELSEEL--RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973

                          170
                   ....*....|....
gi 1622886769 1062 ERSLEvEKKDKLAN 1075
Cdd:TIGR02168  974 LKRLE-NKIKELGP 986
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 908-1066 8.01e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 8.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKakelarieEFKKEEMRKLQKERKVFEKYSTAAR 987
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK--------QILRERLANLERQLEELEAQLEELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  988 TFPDKKE------REEIQTLKQQIADLREDLKRKETKWSSTHGR---LRSQIEMLVRENTDLREEIKVMERFRLDAWKRA 1058
Cdd:TIGR02168  330 SKLDELAeelaelEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIERLEARL 409


                   ....*...
gi 1622886769 1059 EAVERSLE 1066
Cdd:TIGR02168  410 ERLEDRRE 417
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
925-1066 8.50e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  925 ENASLAKLRIER-----ESALEKLRKEIADFEQ-----------QKAKEL-ARIEEFkkEEMRKLQKERKvfekySTAAR 987
Cdd:PRK02224   169 ERASDARLGVERvlsdqRGSLDQLKAQIEEKEEkdlherlngleSELAELdEEIERY--EEQREQARETR-----DEADE 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  988 TFPDKKE-REEIQTLKQQIADLREDLKRKETKWSSTHGR---LRSQIEMLVRENTDLREE-------IKVMERFRLDAWK 1056
Cdd:PRK02224   242 VLEEHEErREELETLEAEIEDLRETIAETEREREELAEEvrdLRERLEELEEERDDLLAEaglddadAEAVEARREELED 321

                          170
                   ....*....|
gi 1622886769 1057 RAEAVERSLE 1066
Cdd:PRK02224   322 RDEELRDRLE 331
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
902-1081 9.07e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 9.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAkLRIERESALEKLrkeiADFEQQKAKELARIEEfKKEEMRKLQKERKvfek 981
Cdd:COG3206    181 EEQLPELRKELEEAEAALEEFRQKNGLVD-LSEEAKLLLQQL----SELESQLAEARAELAE-AEARLAALRAQLG---- 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 ysTAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTH---GRLRSQIEMLVRENTDLREEIKVMERFRLDAWKRA 1058
Cdd:COG3206    251 --SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328

                          170       180
                   ....*....|....*....|...
gi 1622886769 1059 EAVERSLEVEKKDKLANTSVRFQ 1081
Cdd:COG3206    329 EASLQAQLAQLEARLAELPELEA 351
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
908-1075 1.40e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEqQKAKELARIEEfKKEEMRKLQKERkvfEKYSTAAR 987
Cdd:PRK03918   236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKE-KAEEYIKLSEFY---EEYLDELR 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  988 TFPDKKER--EEIQTLKQQIADLREDLKRKEtkwssthgRLRSQIEMLVRENTDLREEIKVMERFRlDAWKRAEAVERSL 1065
Cdd:PRK03918   311 EIEKRLSRleEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRL 381

                          170
                   ....*....|
gi 1622886769 1066 EVEKKDKLAN 1075
Cdd:PRK03918   382 TGLTPEKLEK 391
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
900-1066 1.60e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  900 GDNARSQV--LREKIIELETEIEKFKAENASLAKLR---IERESALEKLRKeiADFEQQKAKELAR-IEEfKKEEMRKLQ 973
Cdd:COG4913    605 GFDNRAKLaaLEAELAELEEELAEAEERLEALEAELdalQERREALQRLAE--YSWDEIDVASAEReIAE-LEAELERLD 681

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  974 KERKVFEKYSTAArtfpdKKEREEIQTLKQQIADLREDLKRKETKWSsthgRLRSQIEMLVRENTDLREEIKVMERFRLD 1053
Cdd:COG4913    682 ASSDDLAALEEQL-----EELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLE 752

                          170
                   ....*....|...
gi 1622886769 1054 AWKRAEAVERSLE 1066
Cdd:COG4913    753 ERFAAALGDAVER 765
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 914-1070 1.68e-05

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: 49.30  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  914 ELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKE-RKVFEKYSTAARTFPDK 992
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622886769  993 KEREeiqtlkqqiadlrEDLKRKETKWSSTHGRLRSQIEMLVRENTDLR-EEIKVMERFRLDAWKRAEAVERSLEVEKK 1070
Cdd:TIGR02169  314 EREL-------------EDAEERLAKLEAEIDKLLAEIEELEREIEEERkRRDKLTEEYAELKEELEDLRAELEEVDKE 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1076 1.92e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEK 981
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 YSTAARtfpdkkereEIQTLKQQIADLREDLKRketkwssthgrLRSQIEMLVRENTDLREEIkvmeRFRLDAWKRAEAV 1061
Cdd:TIGR02168  381 LETLRS---------KVAQLELQIASLNNEIER-----------LEARLERLEDRRERLQQEI----EELLKKLEEAELK 436

                          170
                   ....*....|....*
gi 1622886769 1062 ERSLEVEKKDKLANT 1076
Cdd:TIGR02168  437 ELQAELEELEEELEE 451
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 890-1017 3.07e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  890 KLNISQDQPPgdnARSQVLREKIIELETEIEKFKAENASLAKLRieresaLEKLRKEIADFEQQKAKELARIEEfKKEEM 969
Cdd:COG0542    401 RVRMEIDSKP---EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALKARWEA-EKELI 470

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622886769  970 RKLQKERKVFEkystaartfpdkKEREEIQTLKQQIADLREDLKRKET 1017
Cdd:COG0542    471 EEIQELKEELE------------QRYGKIPELEKELAELEEELAELAP 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
903-1072 3.20e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELEtEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEF--KKEEMRKLQKERKVFE 980
Cdd:PRK03918   273 KEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeeKEERLEELKKKLKELE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  981 KysTAARTFPDKKEREEIQTLKQQIADLREDLKRKETkwssthGRLRSQIEMLVRENTDLREEIKVMERFRLDAWKRAEA 1060
Cdd:PRK03918   352 K--RLEELEERHELYEEAKAKKEELERLKKRLTGLTP------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423

                          170
                   ....*....|..
gi 1622886769 1061 VERSLEVEKKDK 1072
Cdd:PRK03918   424 LKKAIEELKKAK 435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
909-1079 5.05e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 5.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  909 REKIIELETEIEKFKAENASLAKlRIERESALEKLRKEIADFEQQKAKELARIEEFK---KEEMRKLQKERKVFEKYSTA 985
Cdd:PRK02224   474 RERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRetiEEKRERAEELRERAAELEAE 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  986 ARTfpdkkEREEIQTLKQQIADLREDLKRKETKWSSTHGRLRS--QIEMLVRENTDLREEIkvmERFRLdawKRAEAVER 1063
Cdd:PRK02224   553 AEE-----KREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEI---ERLRE---KREALAEL 621

                          170
                   ....*....|....*.
gi 1622886769 1064 slEVEKKDKLANTSVR 1079
Cdd:PRK02224   622 --NDERRERLAEKRER 635
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 914-1074 9.93e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 9.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  914 ELETEIEKFKAEnASLAKLRiERESALEKLRKEIADFEQQKAKELARIEEF--KKEEMR-KLQKERKVFEKYSTAARtfp 990
Cdd:COG1196    217 ELKEELKELEAE-LLLLKLR-ELEAELEELEAELEELEAELEELEAELAELeaELEELRlELEELELELEEAQAEEY--- 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  991 dkKEREEIQTLKQQIADLREDLKRKEtkwsSTHGRLRSQIEMLVRENTDLREEIKVMERFRLDAWKRAEAVERSLEVEKK 1070
Cdd:COG1196    292 --ELLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365


                   ....
gi 1622886769 1071 DKLA 1074
Cdd:COG1196    366 ALLE 369
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
908-1071 1.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLrierESALEKLRKEIADFEQQKAKELARIEEFK----KEEMRKLQKERKVFEKYS 983
Cdd:PRK03918   530 LKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYL 605

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  984 TAartfpdKKEREEIQTLKQQIADLREDLKRKETKWSSTHGR---LRSQIEMLVRENTD-----LREEI--KVMERFRLD 1053
Cdd:PRK03918   606 EL------KDAEKELEREEKELKKLEEELDKAFEELAETEKRleeLRKELEELEKKYSEeeyeeLREEYleLSRELAGLR 679

                          170
                   ....*....|....*...
gi 1622886769 1054 AwkRAEAVERSLEVEKKD 1071
Cdd:PRK03918   680 A--ELEELEKRREEIKKT 695
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
906-1066 1.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  906 QVLREKIIELETEIEKFKAENASLAKLRIER-ESALEKLRKEIADFeQQKAKELARIEEfKKEEMRKLQKE-RKVFEKYS 983
Cdd:COG4717     45 AMLLERLEKEADELFKPQGRKPELNLKELKElEEELKEAEEKEEEY-AELQEELEELEE-ELEELEAELEElREELEKLE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  984 TAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSsthgRLRSQIEMLVRENTDLREEI-KVMERFRLDAWKRAEAVE 1062
Cdd:COG4717    123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELeELLEQLSLATEEELQDLA 198


                   ....
gi 1622886769 1063 RSLE 1066
Cdd:COG4717    199 EELE 202
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 898-1066 1.83e-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: 45.83  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  898 PPGDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESAL-------EKLRKEIADFEQQKAKELARIEEfKKEEMR 970
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkiGEIEKEIEQLEQEEEKLKERLEE-LEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  971 KLQKERkvfekystaartfpdKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRL-RSQIEMLVRENTDLREEIKVMEr 1049
Cdd:TIGR02169  748 SLEQEI---------------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIE- 811

                          170
                   ....*....|....*..
gi 1622886769 1050 frldawKRAEAVERSLE 1066
Cdd:TIGR02169  812 ------ARLREIEQKLN 822
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
903-1023 2.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLAklriERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKY 982
Cdd:COG4717    132 QELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622886769  983 STAArtfpdkkeREEIQTLKQQIADLREDLKRKETKWSSTH 1023
Cdd:COG4717    208 LAEL--------EEELEEAQEELEELEEELEQLENELEAAA 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
908-1073 4.01e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEiADFEQQKAKELA-RIEEFKKEEmrklQKERKVFEKYSTAA 986
Cdd:PRK02224   263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEaRREELEDRD----EELRDRLEECRVAA 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  987 RTFPDKKE--REEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLvrenTDLREEIK-VMERFRLDAWKRAEAVER 1063
Cdd:PRK02224   338 QAHNEEAEslREDADDLEERAEELREEAAELESELEEAREAVEDRREEI----EELEEEIEeLRERFGDAPVDLGNAEDF 413

                          170
                   ....*....|.
gi 1622886769 1064 SLEV-EKKDKL 1073
Cdd:PRK02224   414 LEELrEERDEL 424
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 908-1074 4.13e-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: 44.67  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKL------RIERESALEKLR--KEIADFEQQKAKeLARIEEFKKEEMRKLQKE-RKV 978
Cdd:TIGR02169  249 LEEELEKLTEEISELEKRLEEIEQLleelnkKIKDLGEEEQLRvkEKIGELEAEIAS-LERSIAEKERELEDAEERlAKL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  979 FEKYSTAARTFPDKKER------------EEIQTLKQQIADLREDLKRKETKwsstHGRLRSQIEMLVRENTDLREEIKV 1046
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREieeerkrrdkltEEYAELKEELEDLRAELEEVDKE----FAETRDELKDYREKLEKLKREINE 403

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622886769 1047 MERFR---LDAWKRAEAVERSLEVEKKDKLA 1074
Cdd:TIGR02169  404 LKRELdrlQEELQRLSEELADLNAAIAGIEA 434
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
914-1062 4.56e-04

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 43.00  E-value: 4.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  914 ELETEIEKFKAENASLAKLRIERESA--LEKLRKEIADFEQQKAKELARIEEFKkEEMRKLQKERKVFEKYSTAAR---T 988
Cdd:NF033927     8 ALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNELA-EDRKVIIEAIDLIEKYNIADLfkdL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  989 FPDKKE-------REEIQTLKQQIadlrEDLKRKETKWSS---------THGRLRSQIEMLVRENTDLREEIKVMErFRL 1052
Cdd:NF033927    87 LPTAEEidslglpPPEKDLVKAAI----ERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKALA-GKL 161

                          170
                   ....*....|
gi 1622886769 1053 DAWKRAEAVE 1062
Cdd:NF033927   162 EELTAIAAID 171
PTZ00121 PTZ00121
MAEBL; Provisional
 910-1072 6.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  910 EKIIELETEIEKFKAENASLA---KLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEmrklqkERKVFEKYSTAA 986
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAeeaKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE------EENKIKAAEEAK 1668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  987 RTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHgRLRSQIEMLVRENTDLREEIKVMERFRLDAWKRAEAVERSLE 1066
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747


                   ....*.
gi 1622886769 1067 VEKKDK 1072
Cdd:PTZ00121  1748 EAKKDE 1753
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
903-1072 6.79e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKelarIEEFKKEEMRKLQKERKVFEKY 982
Cdd:PRK03918   186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKI 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  983 STAARTFpdKKEREEIQTLKQQIADLREdLKRKETKWSSTHG---RLRSQIEMLVRENTDLREEIKVMERfRLDawKRAE 1059
Cdd:PRK03918   262 RELEERI--EELKKEIEELEEKVKELKE-LKEKAEEYIKLSEfyeEYLDELREIEKRLSRLEEEINGIEE-RIK--ELEE 335

                          170
                   ....*....|...
gi 1622886769 1060 AVERSLEVEKKDK 1072
Cdd:PRK03918   336 KEERLEELKKKLK 348
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 910-1007 8.74e-04

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: 40.64  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  910 EKIIEletEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKYSTAARTF 989
Cdd:pfam03938    8 QKILE---ESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84

                           90
                   ....*....|....*...
gi 1622886769  990 PDKKEREEIQTLKQQIAD 1007
Cdd:pfam03938   85 LQKKQQELLQPIQDKINK 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 903-1045 9.07e-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: 43.52  E-value: 9.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKY 982
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622886769  983 STAARTFpdKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRlRSQIEMLVRENTDLREEIK 1045
Cdd:TIGR02169  458 EQLAADL--SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ-ARASEERVRGGRAVEEVLK 517
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 908-1050 9.46e-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: 43.52  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFK---KEEMRKLQKERKVFEKYST 984
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQ 469

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622886769  985 AARtfpdkKEREEIQTLKQQIADLREDLKRKET--KWSSTHGRLRSQIEMLVRENTD-----LREEIKVMERF 1050
Cdd:TIGR02169  470 ELY-----DLKEEYDRVEKELSKLQRELAEAEAqaRASEERVRGGRAVEEVLKASIQgvhgtVAQLGSVGERY 537
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 902-1060 1.27e-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: 42.44  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADF--EQQKAKELARIEE-FKKEEMRKLQKERKV 978
Cdd:COG4942     61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALlLSPEDFLDAVRRLQY 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  979 FEKYSTAARTFPD--KKEREEIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVRENTDLREEIKVMERfRLDAWK 1056
Cdd:COG4942    141 LKYLAPARREQAEelRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQ 219


                   ....
gi 1622886769 1057 RAEA 1060
Cdd:COG4942    220 QEAE 223
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 908-1052 1.30e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIE-----LETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQK-ERKVFEK 981
Cdd:PRK00409   499 LPENIIEeakklIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEaEKEAQQA 578

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622886769  982 YSTAartfpdKKEREE-IQTLKQQIADLREDLKRKETKwsSTHGRLRSQIEMLVRENTDLRE---EIKVMERFRL 1052
Cdd:PRK00409   579 IKEA------KKEADEiIKELRQLQKGGYASVKAHELI--EARKRLNKANEKKEKKKKKQKEkqeELKVGDEVKY 645
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 903-1108 1.39e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLRE-----KIIELETEIEKFKAENAS-----LAKLRIERESALEKLRKEiaDFEQQKAKELARIEEF----KKEE 968
Cdd:pfam17380  401 ARKVKILEeerqrKIQQQKVEMEQIRAEQEEarqreVRRLEEERAREMERVRLE--EQERQQQVERLRQQEEerkrKKLE 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  969 MRKLQKE--------RKVFEKYSTAARTFPDKKEREEiQTLKQQIADLREDLKRKETKWSSTHGRlRSQIEMLVRENTDL 1040
Cdd:pfam17380  479 LEKEKRDrkraeeqrRKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEER-RKQQEMEERRRIQE 556

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622886769 1041 REEIKVMERFRLDAWKRAEAVERSL-EVEKKDKlantsvrfqnnQISSGTQVEKYKKNYLPMQGTAQPP 1108
Cdd:pfam17380  557 QMRKATEERSRLEAMEREREMMRQIvESEKARA-----------EYEATTPITTIKPIYRPRISEYQPP 614
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 902-985 1.63e-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: 39.87  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELariEEFKKEEMRKLQKE-RKVFE 980
Cdd:pfam03938   29 KKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL---QKKQQELLQPIQDKiNKAIK 105


                   ....*
gi 1622886769  981 KYSTA 985
Cdd:pfam03938  106 EVAKE 110
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 903-975 2.00e-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: 40.20  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASL-AKLRIERESALEKLRKEIADFEQQKAKELARIEEfkkEEMRKLQKE 975
Cdd:COG2825     54 KRQAELQKLEKELQALQEKLQKEAATLsEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQ---ELLQPILEK 124
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 902-995 2.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  902 NARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADfEQQKAKELARIEEFKKEEMRKLQKERKVFEK 981
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE-LAAELAELQQEAEELEALIARLEAEAAAAAE 241

                           90
                   ....*....|....
gi 1622886769  982 ySTAARTFPDKKER 995
Cdd:COG4942    242 -RTPAAGFAALKGK 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 903-1049 2.14e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  903 ARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFK--KEEMRKLQKERKVFE 980
Cdd:COG1196    665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeqLEAEREELLEELLEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  981 KYSTAARTFPDKKEREEIQTLKQQIADLREDLKR------------KETKwsSTHGRLRSQIEMLVRENTDLREEIKVME 1048
Cdd:COG1196    745 EELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyEELE--ERYDFLSEQREDLEEARETLEEAIEEID 822


                   .
gi 1622886769 1049 R 1049
Cdd:COG1196    823 R 823
PTZ00121 PTZ00121
MAEBL; Provisional
 878-1084 2.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  878 KPKSDSHLGTEPKLNISQDqppgDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKeiadfeqqKAKE 957
Cdd:PTZ00121  1059 KAEAKAHVGQDEGLKPSYK----DFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKK--------KAED 1126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  958 LARIEEFKK-EEMRKLQKERKVFEkystaARTFPDKKEREEIQtlKQQIADLREDLKRKETKWSSTHGRLRSQiemlVRE 1036
Cdd:PTZ00121  1127 ARKAEEARKaEDARKAEEARKAED-----AKRVEIARKAEDAR--KAEEARKAEDAKKAEAARKAEEVRKAEE----LRK 1195

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622886769 1037 NTDLR---------EEIKVMERFRLDAWKRAEAVERSLEVEKKDKLANTSVRFQNNQ 1084
Cdd:PTZ00121  1196 AEDARkaeaarkaeEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 927-1035 2.72e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  927 ASLAKLRIERESALEKLRKEIadfeQQKAKELARIeefkKEEMRKLQKERKVFEKYSTAArtfpdkkeREEIQTLKQQIA 1006
Cdd:COG4942     16 AAQADAAAEAEAELEQLQQEI----AELEKELAAL----KKEEKALLKQLAALERRIAAL--------ARRIRALEQELA 79

                           90       100
                   ....*....|....*....|....*....
gi 1622886769 1007 DLREDLKRKETKWSSTHGRLRSQIEMLVR 1035
Cdd:COG4942     80 ALEAELAELEKEIAELRAELEAQKEELAE 108
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
909-1079 3.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  909 REKIIELETEIEKFKAENASLAKLR-------------IERESALEKLRKEIadfEQQKAKELARIEEFKKEEMRKLQKE 975
Cdd:PRK03918   147 REKVVRQILGLDDYENAYKNLGEVIkeikrrierlekfIKRTENIEELIKEK---EKELEEVLREINEISSELPELREEL 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  976 RKVFEKYSTAartfpdKKEREEIQTLKQQIADLREDLKRKETKWssthGRLRSQIEMLVRENTDLREEIKVMERFRLDAW 1055
Cdd:PRK03918   224 EKLEKEVKEL------EELKEEIEELEKELESLEGSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKELKEKAE 293

                          170       180
                   ....*....|....*....|....
gi 1622886769 1056 KRAEAVErsLEVEKKDKLANTSVR 1079
Cdd:PRK03918   294 EYIKLSE--FYEEYLDELREIEKR 315
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 897-1072 3.13e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  897 QPPGDNARSQVLREKIIELET----EIEKFKAENASLAKLRIERESALEKLRKEIADFE------QQKAKELARIEEFKK 966
Cdd:pfam17380  303 QEKEEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERMAMERERELERIRQEERKRElerirqEEIAMEISRMRELER 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  967 EEMRKLQKERKVFEKYSTAARTFPDKKERE-EIQTLKQQIADLR--------EDLKRKETKWSSTHGRLR-------SQI 1030
Cdd:pfam17380  383 LQMERQQKNERVRQELEAARKVKILEEERQrKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRleeqerqQQV 462

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622886769 1031 EMLVRENTDLREEIKVMERFRLDAWKRAEAVERSLEVEKKDK 1072
Cdd:pfam17380  463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 908-1071 3.18e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEE---MRKLQKERKVFEK--- 981
Cdd:COG4942     32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelRAELEAQKEELAEllr 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  982 --YSTAARTFP-------------------------DKKEREEIQTLKQQIADLREDLKRKETkwssthgRLRSQIEMLV 1034
Cdd:COG4942    112 alYRLGRQPPLalllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERA-------ELEALLAELE 184

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1622886769 1035 RENTDLREEIKVMERFRLDAWKRAEAVERSLEVEKKD 1071
Cdd:COG4942    185 EERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 930-1070 3.48e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  930 AKLRIERES---ALEKLRKEIADFEQQKakelariEEFKKEEmrklqkerkvfekystaartfpDKKEREEIQTLKQQIA 1006
Cdd:COG0542    400 ARVRMEIDSkpeELDELERRLEQLEIEK-------EALKKEQ----------------------DEASFERLAELRDELA 450

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622886769 1007 DLREDLKRKETKWSSTHGrlrsqiemLVRENTDLREEIKVMERFRLDAWKRAEAVERSLEVEKK 1070
Cdd:COG0542    451 ELEEELEALKARWEAEKE--------LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAP 506
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 910-1066 3.72e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  910 EKIIELETEIEKFKAENASLAKLR-----IERESALE-------KLRKEIAD-FEQQKAKELARIEEFKKEEM------- 969
Cdd:PRK05771   107 EEISELENEIKELEQEIERLEPWGnfdldLSLLLGFKyvsvfvgTVPEDKLEeLKLESDVENVEYISTDKGYVyvvvvvl 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  970 -RKLQKERKVFEKYSTAARTFPDKKE--------REEIQTLKQQIADLREDLKRKETKWSSThgrLRSQIEMLvrENTDL 1040
Cdd:PRK05771   187 kELSDEVEEELKKLGFERLELEEEGTpselireiKEELEEIEKERESLLEELKELAKKYLEE---LLALYEYL--EIELE 261

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1622886769 1041 REEIKVMER-----FRLDAW---KRAEAVERSLE 1066
Cdd:PRK05771   262 RAEALSKFLktdktFAIEGWvpeDRVKKLKELID 295
PTZ00121 PTZ00121
MAEBL; Provisional
 909-1072 3.86e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  909 REKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADfEQQKAKELARieefKKEEMRKLQKERKVFEKYSTAART 988
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKK----EAEEAKKAEELKKKEAEEKKKAEE 1720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  989 FpdKKEREEIQTLKQQIADLREDLKRKETKWSSTHGRlRSQIEMLVRENTDLREEIKVMERFRLDAWKRAEAVERSLEVE 1068
Cdd:PTZ00121  1721 L--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797


                   ....
gi 1622886769 1069 KKDK 1072
Cdd:PTZ00121  1798 KKIK 1801
CUPID pfam11819
Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune ...
 315-400 4.04e-03

Cytohesin Ubiquitin Protein Inducing Domain; C1ORF106 also known as INAVA (Innate Immune Activator), is identified as a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. INAVA carries CUPID (Cytohesin Ubiquitin Protein Inducing Domain). Three other human proteins contain CUPID: FRMD4A, FRMD4B, and CCDC120- proteins implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation.


Pssm-ID: 463360  Cd Length: 136  Bit Score: 38.83  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  315 DSSEVANIEERPIKAAIRERKQTfedyLEEQIRLEEQELKQKQLREAE--GPL----PIKAKPKKPFLKRGEGLARFTNA 388
Cdd:pfam11819   20 DSSTSSEKQKKEKTAALKKKQQA----LQERLELKLEELKKLCLREAEltGKLpkeyPLEPGEKPPQVRRRVGTAFKLDE 95

                           90
                   ....*....|..
gi 1622886769  389 KSKFQKGKESKL 400
Cdd:pfam11819   96 QHVLQYAEDPEL 107
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 908-1066 4.38e-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: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  908 LREKIIELETEIEKFKAENASLAK-------LRIERESALEKLRKEIADFEQQKAKELARIEEFKK------EEMRKLQK 974
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKeiqelqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrdleSRLGDLKK 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  975 ERKVFEKYSTAArtfpdkkeREEIQTLKQQIADLREDLKRKETKWSSTHGRLrSQIEMLVRENTDLREEIKVMErfrlDA 1054
Cdd:TIGR02169  890 ERDELEAQLREL--------ERKIEELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKGEDEEIPEEELSLE----DV 956

                          170
                   ....*....|..
gi 1622886769 1055 WKRAEAVERSLE 1066
Cdd:TIGR02169  957 QAELQRVEEEIR 968
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 940-1074 4.46e-03

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: 39.91  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  940 LEKLRKEIADFEQQKAKELARIEEFKKEemrkLQKERKVFEKYSTAArtfpdKKEREEIQTLKQQIADLREDLKRKETKw 1019
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDE----LAALEARLEAAKTEL-----EDLEKEIKRLELEIEEVEARIKKYEEQ- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622886769 1020 sstHGRLRSQIEM--LVRENTDLREEIKVMERFRLDAWKRAEAVERSLEvEKKDKLA 1074
Cdd:COG1579     82 ---LGNVRNNKEYeaLQKEIESLKRRISDLEDEILELMERIEELEEELA-ELEAELA 134
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
919-1071 7.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 7.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  919 IEKFKAENASLAKLRIERESALEKLRKEIADFEqqkaKELARIEEFKK-----EEMRKLQKERKVF--EKYSTAARTFPD 991
Cdd:PRK03918   454 LEEYTAELKRIEKELKEIEEKERKLRKELRELE----KVLKKESELIKlkelaEQLKELEEKLKKYnlEELEKKAEEYEK 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  992 KKER---------------EEIQTLKQQIADLREDLKRKETKWSSTHGRLRsqiEMLVRENTDLREEIKVMERFR----- 1051
Cdd:PRK03918   530 LKEKliklkgeikslkkelEKLEELKKKLAELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPFYneyle 606

                          170       180
                   ....*....|....*....|.
gi 1622886769 1052 -LDAWKRAEAVERSLEVEKKD 1071
Cdd:PRK03918   607 lKDAEKELEREEKELKKLEEE 627
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
 924-979 7.53e-03

Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ribosomal subunit S26 in eukaryotes


Pssm-ID: 464391 [Multi-domain]  Cd Length: 168  Bit Score: 38.76  E-value: 7.53e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622886769  924 AENASLAKLRIERESALEKLRKE-----IADFEQQKAKELARIEefkkEEMRKLQKERKVF 979
Cdd:pfam14943   82 EWNAEIAKLREERLAKEAEEREEeilerIEEKEEKEEEKKERAE----EEVRQEKEESKTF 138
FapA pfam03961
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ...
 883-982 7.68e-03

Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.


Pssm-ID: 461111 [Multi-domain]  Cd Length: 272  Bit Score: 39.59  E-value: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  883 SHLGTEPKLNISQDQPPgdnarsqvLREKIIELETEIEKFKAEnasLAKLrierESALEKLRKEI-ADFEQQKAKELARI 961
Cdd:pfam03961  137 SPAGTKTEIEVGVDFPE--------LKEKLEELEKELEELEEE---LEKL----KKRLKKLPKKArGQLPPEKREQLEKL 201

                           90       100
                   ....*....|....*....|....
gi 1622886769  962 EEFKK---EEMRKLQKERKVFEKY 982
Cdd:pfam03961  202 LETKNklsEELEELEEELKELKEE 225
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 907-975 7.86e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.43  E-value: 7.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622886769  907 VLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEI----ADFEQQKakelARIEEFKKE------EMRKLQKE 975
Cdd:pfam05911   89 ELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKsqaeAEIEALK----SRLESCEKEinslkyELHVLSKE 163
PTZ00121 PTZ00121
MAEBL; Provisional
 918-1072 8.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769  918 EIEKFKAENASLAKLRIERESALEKLRKEIADfEQQKAKELARIEEFKK-EEMRKLQKERKVFEKYSTAARTFPDKKERE 996
Cdd:PTZ00121  1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622886769  997 EIQTLKQQIADLREDLKRKETKWSSTHGRLRSQIEMLVREntdLREEIKVMERFRLDAWKRAEAVERSLEVEKKDK 1072
Cdd:PTZ00121  1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE---LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 902-985 8.92e-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: 37.95  E-value: 8.92e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622886769   902 NARSQVLREKIIELETEIEKFKAENASL-AKLRIERESALEKLRKEIADFEQQKAKELARIEEfkkEEMRKLQKE-RKVF 979
Cdd:smart00935   28 KKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ---EELQKILDKiNKAI 104


                    ....*.
gi 1622886769   980 EKYSTA 985
Cdd:smart00935  105 KEVAKK 110
 
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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