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Conserved domains on  [gi|568987340|ref|XP_006518912|]
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centromere protein J isoform X1 [Mus musculus]

Protein Classification

T-complex 10 C-terminal domain-containing protein( domain architecture ID 10537651)

T-complex 10 C-terminal domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1151-1179 3.23e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.98  E-value: 3.23e-11
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1151 EISHPDGKVEKIYKNGRRVVLFPNGTRKE 1179
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1260-1288 5.94e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.94e-10
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1260 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1288
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
872-1039 9.60e-09

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.93  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  872 DSHLENESKLNLSQDQppGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKA----RE 947
Cdd:COG4913   262 ERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  948 LARIEEYRKEETRKLQKERKVFEKYTAAART--FPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVK 1025
Cdd:COG4913   340 LEQLEREIERLERELEERERRRARLEALLAAlgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                         170
                  ....*....|....
gi 568987340 1026 ENTDLREEIKVMER 1039
Cdd:COG4913   420 ELRELEAEIASLER 433
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1224-1252 4.01e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 4.01e-05
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1224 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1252
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1295-1324 1.00e-04

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


:

Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568987340  1295 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1324
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
 
Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1151-1179 3.23e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.98  E-value: 3.23e-11
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1151 EISHPDGKVEKIYKNGRRVVLFPNGTRKE 1179
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1260-1288 5.94e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.94e-10
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1260 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1288
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
872-1039 9.60e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.93  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  872 DSHLENESKLNLSQDQppGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKA----RE 947
Cdd:COG4913   262 ERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  948 LARIEEYRKEETRKLQKERKVFEKYTAAART--FPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVK 1025
Cdd:COG4913   340 LEQLEREIERLERELEERERRRARLEALLAAlgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                         170
                  ....*....|....
gi 568987340 1026 ENTDLREEIKVMER 1039
Cdd:COG4913   420 ELRELEAEIASLER 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 875-1039 1.36e-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: 59.69  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   875 LENESKLNLSQDQPPGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEY 954
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   955 RKEETRkLQKERKVFEKYTAAARTFPDKKEREEIQA----LKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDL 1030
Cdd:TIGR02168  406 EARLER-LEDRRERLQQEIEELLKKLEEAELKELQAeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484

                          170
                   ....*....|..
gi 568987340  1031 RE---EIKVMER 1039
Cdd:TIGR02168  485 AQlqaRLDSLER 496
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
898-1041 3.22e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqQKARELARIEEYrKEETRKLQKERkvfEKYTAAAR 977
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEK-AEEYIKLSEFY---EEYLDELR 310

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987340  978 TFPDKKER--EEIQALKQQIADLQEDLKRKEtkwsstqsRLRSQIEMLVKENTDLREEIKVMERFR 1041
Cdd:PRK03918  311 EIEKRLSRleEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERHELYEEAK 368
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1224-1252 4.01e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 4.01e-05
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1224 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1252
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1295-1324 1.00e-04

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568987340  1295 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1324
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 894-1064 5.56e-04

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: 44.34  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   894 RSQVLREKVTELES-EIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKAReLARIEEYRKEETRKLQKE------- 965
Cdd:pfam17380  411 RQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER-LRQQEEERKRKKLELEKEkrdrkra 489

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   966 ----RKVFEKYTAAARTFPDKKEREEiQALKQQIADLQEDLKRKETKWSSTQSRlRSQIEMlvKENTDLREEIKVM--ER 1039
Cdd:pfam17380  490 eeqrRKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEER-RKQQEM--EERRRIQEQMRKAteER 565

                          170       180       190
                   ....*....|....*....|....*....|
gi 568987340  1040 FRLDAWKRAEAM-----ENSPKACQYMMAT 1064
Cdd:pfam17380  566 SRLEAMEREREMmrqivESEKARAEYEATT 595
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 898-1034 1.35e-03

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: 42.36  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESAL-EKLRKEIADFEQQKAREL-ARIEEYRKEETRKLqkerkvfekytaa 975
Cdd:cd22656   133 YQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKEIKDLqKELEKLNEEYAAKL------------- 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340  976 artfpdkkeREEIQALKQQIADLQEDLKRKEtkwsstqsRLRSQIEMLVKENTDLREEI 1034
Cdd:cd22656   200 ---------KAKIDELKALIADDEAKLAAAL--------RLIADLTAADTDLDNLLALI 241
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
898-1054 3.45e-03

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 40.69  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESA--LEKLRKEIADFEQQKARELARIEEyRKEETRKLQKERKVFEKYTAA 975
Cdd:NF033927    2 LSNVIAALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNE-LAEDRKVIIEAIDLIEKYNIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  976 AR---TFPDKKE-------REEIQALKQQIadlqEDLKRKETKWSS---------TQSRLRSQIEMLVKENTDLREEIKV 1036
Cdd:NF033927   81 DLfkdLLPTAEEidslglpPPEKDLVKAAI----ERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKA 156

                         170
                  ....*....|....*...
gi 568987340 1037 MErFRLDAWKRAEAMENS 1054
Cdd:NF033927  157 LA-GKLEELTAIAAIDEE 173
 
Name Accession Description Interval E-value
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1151-1179 3.23e-11

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 58.98  E-value: 3.23e-11
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1151 EISHPDGKVEKIYKNGRRVVLFPNGTRKE 1179
Cdd:pfam07202    2 EIIFPDGTVERVYSDGDKVIEFPNGTREI 30
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1260-1288 5.94e-10

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 55.52  E-value: 5.94e-10
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1260 EESIFPDGTIVRVQRDGNKIIEFNNGQRE 1288
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
872-1039 9.60e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.93  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  872 DSHLENESKLNLSQDQppGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKA----RE 947
Cdd:COG4913   262 ERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  948 LARIEEYRKEETRKLQKERKVFEKYTAAART--FPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVK 1025
Cdd:COG4913   340 LEQLEREIERLERELEERERRRARLEALLAAlgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419

                         170
                  ....*....|....
gi 568987340 1026 ENTDLREEIKVMER 1039
Cdd:COG4913   420 ELRELEAEIASLER 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 875-1039 1.36e-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: 59.69  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   875 LENESKLNLSQDQPPGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEY 954
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   955 RKEETRkLQKERKVFEKYTAAARTFPDKKEREEIQA----LKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDL 1030
Cdd:TIGR02168  406 EARLER-LEDRRERLQQEIEELLKKLEEAELKELQAeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484

                          170
                   ....*....|..
gi 568987340  1031 RE---EIKVMER 1039
Cdd:TIGR02168  485 AQlqaRLDSLER 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 898-1054 1.99e-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: 58.91  E-value: 1.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETR------KLQKERKVFEK 971
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   972 YTAAARTFPDkKEREEIQALKQQIADLQEDLKRKE---TKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAWKRA 1048
Cdd:TIGR02168  762 EIEELEERLE-EAEEELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840


                   ....*.
gi 568987340  1049 EAMENS 1054
Cdd:TIGR02168  841 EDLEEQ 846
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 898-1053 2.02e-08

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: 58.93  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARElaRIEEYRkEETRKLQKERKVFEKYTAA-- 975
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQ-AELSKLEEEVSRIEARLREie 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   976 ----ARTFPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLR---SQIEMLVKENTDLREEIKVMERFRLDAWKRA 1048
Cdd:TIGR02169  819 qklnRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleEELEELEAALRDLESRLGDLKKERDELEAQL 898


                   ....*
gi 568987340  1049 EAMEN 1053
Cdd:TIGR02169  899 RELER 903
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 896-1050 2.14e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAA 975
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987340  976 ARTfpDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERfRLDAWKRAEA 1050
Cdd:COG1196   315 EER--LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAE 386
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
896-1050 4.87e-08

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 57.56  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAENTSLaklrierESALEKLRKEIADFEqqkarelARIEEYRKEETRKLQKERKVfekytaa 975
Cdd:COG2433   409 TEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIERLE-------RELSEARSEERREIRKDREI------- 467

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987340  976 artfpdKKEREEIQALKQQIADLQEDLKRKETKwsstQSRLRSQIEMLVKENTdlrEEIKVMERFRLDAWKRAEA 1050
Cdd:COG2433   468 ------SRLDREIERLERELEEERERIEELKRK----LERLKELWKLEHSGEL---VPVKVVEKFTKEAIRRLEE 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 894-1044 1.00e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  894 RSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERkvfekyt 973
Cdd:COG1196   254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA------- 326

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987340  974 aaartfpdkKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDA 1044
Cdd:COG1196   327 ---------ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 898-1038 2.04e-07

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: 53.39  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKE-ETRKLQKERKVFEK---YT 973
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYEALQKeieSL 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987340  974 AAARTFPDKKERE---EIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVME 1038
Cdd:COG1579   102 KRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
871-1047 5.22e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.00  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  871 LDSHLENESK--LNLSQDQPPGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESA---LEKLRKEIADFEQQKA 945
Cdd:COG4717    47 LLERLEKEADelFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  946 -----RELARIEEYRKEETRKLQKERKVFEKYTAAartfpdkkeREEIQALKQQIADLQEDLKRKETKWSSTQsrlRSQI 1020
Cdd:COG4717   127 llplyQELEALEAELAELPERLEELEERLEELREL---------EEELEELEAELAELQEELEELLEQLSLAT---EEEL 194

                         170       180
                  ....*....|....*....|....*..
gi 568987340 1021 EMLVKENTDLREEIKVMERfRLDAWKR 1047
Cdd:COG4717   195 QDLAEELEELQQRLAELEE-ELEEAQE 220
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 898-1052 1.16e-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: 53.14  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKA----------RELARIEEYRKEETRKlqKERK 967
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlanleRQLEELEAQLEELESK--LDEL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   968 VFEKYTAAARTFPDKKE-----------REEIQALKQQIADLQE----------DLKRKETKWSSTQSRLRSQIEMLVKE 1026
Cdd:TIGR02168  336 AEELAELEEKLEELKEElesleaeleelEAELEELESRLEELEEqletlrskvaQLELQIASLNNEIERLEARLERLEDR 415

                          170       180
                   ....*....|....*....|....*.
gi 568987340  1027 NTDLREEIKVMERFRLDAWKRAEAME 1052
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAE 441
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
898-1037 1.64e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 52.71  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAEN--------------------TSLAKLRIER---ESALEKLRKEIADFEQQKARELA--RIE 952
Cdd:COG3206   187 LRKELEEAEAALEEFRQKNglvdlseeaklllqqlseleSQLAEARAELaeaEARLAALRAQLGSGPDALPELLQspVIQ 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  953 EYRKEETRKLQKERKVFEKYTAAArtfPDkkereeIQALKQQIADLQEDLKRKETK-WSSTQSR---LRSQIEMLVKENT 1028
Cdd:COG3206   267 QLRAQLAELEAELAELSARYTPNH---PD------VIALRAQIAALRAQLQQEAQRiLASLEAEleaLQAREASLQAQLA 337


                  ....*....
gi 568987340 1029 DLREEIKVM 1037
Cdd:COG3206   338 QLEARLAEL 346
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
898-1041 3.22e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqQKARELARIEEYrKEETRKLQKERkvfEKYTAAAR 977
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEK-AEEYIKLSEFY---EEYLDELR 310

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987340  978 TFPDKKER--EEIQALKQQIADLQEDLKRKEtkwsstqsRLRSQIEMLVKENTDLREEIKVMERFR 1041
Cdd:PRK03918  311 EIEKRLSRleEEINGIEERIKELEEKEERLE--------ELKKKLKELEKRLEELEERHELYEEAK 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 894-1035 4.02e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  894 RSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYT 973
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987340  974 AAARTfpDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIK 1035
Cdd:COG1196   390 EALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 892-1050 8.26e-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: 8.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   892 SVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEyrkeetrkLQKERKVFEK 971
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA--------LLNERASLEE 887

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   972 YTAAARTFPDKKERE------EIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAW 1045
Cdd:TIGR02168  888 ALALLRSELEELSEElrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967


                   ....*
gi 568987340  1046 KRAEA 1050
Cdd:TIGR02168  968 EEARR 972
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 900-1054 1.29e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  900 EKVTELESEIEKFKAEntsLAKLRIE-RESALEKLRKEIADFEQQKARELARIEEYRKEETR---KLQKERKVFEKYTAA 975
Cdd:COG1196   213 ERYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEElrlELEELELELEEAQAE 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340  976 ARtfpdkKEREEIQALKQQIADLQEDLKRKEtkwsSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENS 1054
Cdd:COG1196   290 EY-----ELLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 898-1059 1.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAAR 977
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  978 TF-PDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFrLDAWKRAEAMENSPK 1056
Cdd:COG1196   443 ALeEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF-LEGVKAALLLAGLRG 521


                  ...
gi 568987340 1057 ACQ 1059
Cdd:COG1196   522 LAG 524
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 876-1035 1.58e-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: 49.68  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   876 ENESKLNLSQDQPPGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYr 955
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL- 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   956 keETRKLQKERKVFEKYTAAARTFPD-KKEREEIQALKQQIADLQEDLKRKETKWSSTQSRlRSQIEMLVKENTDLREEI 1034
Cdd:TIGR02169  440 --EEEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ-ARASEERVRGGRAVEEVL 516


                   .
gi 568987340  1035 K 1035
Cdd:TIGR02169  517 K 517
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
896-1049 1.81e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAENTSLAKLRIER-ESALEKLRKEIADFeQQKARELARIEEYRKEETRKLQKERKVFEKYTA 974
Cdd:COG4717    45 AMLLERLEKEADELFKPQGRKPELNLKELKElEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987340  975 AARTFPDKKEREEIQALKQQIADLQEDLKRKETKWsstqSRLRSQIEMLVKENTDLREEI-KVMERFRLDAWKRAE 1049
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELeELLEQLSLATEEELQ 195
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
915-1033 2.30e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  915 ENTSLAKLRIER-----ESALEKLRKEIADFEQQKARE-LARIEEYRKEETRKL-----QKERKVFEKYTAAARTFPDKK 983
Cdd:PRK02224  169 ERASDARLGVERvlsdqRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIeryeeQREQARETRDEADEVLEEHEE 248

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568987340  984 EREEIQALKQQIADLQEDLKRKETKWSSTQSR---LRSQIEMLVKENTDLREE 1033
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEvrdLRERLEELEEERDDLLAE 301
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1224-1252 4.01e-05

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 41.65  E-value: 4.01e-05
                           10        20
                   ....*....|....*....|....*....
gi 568987340  1224 EVLHFSSGQIEKHFPDGRKEITFPDQTIK 1252
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTRE 29
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
891-1041 6.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  891 DSVRSQVLREKVTELESEIEKFKAENTSLAKLrierESALEKLRKEIADFEQQKArelARIEEYRKEETRKLQKERKVfE 970
Cdd:COG4913   659 DEIDVASAEREIAELEAELERLDASSDDLAAL----EEQLEELEAELEELEEELD---ELKGEIGRLEKELEQAEEEL-D 730

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987340  971 KYTAAARTFPDKKEREEIQALKQQIADLQEDLKRKEtkwssTQSRLRSQIEMLVKENTDLREEI-KVMERFR 1041
Cdd:COG4913   731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERE-----LRENLEERIDALRARLNRAEEELeRAMRAFN 797
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
899-1057 7.24e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  899 REKVTELESEIEKFKAEntsLAKLrierESALEKLRKEIADFEQQKaRELARIEEYRKEETRKLQKERKVFEK---YTAA 975
Cdd:COG4913   609 RAKLAALEAELAELEEE---LAEA----EERLEALEAELDALQERR-EALQRLAEYSWDEIDVASAEREIAELeaeLERL 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  976 ARTFPDKKE-REEIQALKQQIADLQEDLKRKETKWSSTQSRLRsQIEMLVKENTDLREEIKVME----RFRLDAWKRAEA 1050
Cdd:COG4913   681 DASSDDLAAlEEQLEELEAELEELEEELDELKGEIGRLEKELE-QAEEELDELQDRLEAAEDLArlelRALLEERFAAAL 759


                  ....*..
gi 568987340 1051 MENSPKA 1057
Cdd:COG4913   760 GDAVERE 766
Tcp10_C pfam07202
T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the ...
 1295-1324 1.00e-04

T-complex protein 10 C-terminus; This entry represents a repeating unit commonly found in the C terminus of the eukaryotic T-complex protein 10. The T-complex is involved in spermatogenesis in mice. The repeating unit is commonly found 3-4 times, but there is often a gap between the first and second repeats, which is big enough to accommodate another repeat unit. However, the score is insufficient to be included, and could be a degenerate repeat.


Pssm-ID: 462118  Cd Length: 30  Bit Score: 40.49  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 568987340  1295 KRREYPDGTVKTVYANGHQETKYTSGRVRV 1324
Cdd:pfam07202    1 EEIIFPDGTVERVYSDGDKVIEFPNGTREI 30
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
898-1072 1.18e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIEresaLEKLRKEIADFEQQKARELARIEEYRKEEtRKLQKERKVFEKYTaaar 977
Cdd:PRK03918  219 LREELEKLEKEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELK---- 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  978 tfPDKKEREEIQALKQQIADLQEDLKRKETKWSStqsrLRSQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENSPKA 1057
Cdd:PRK03918  290 --EKAEEYIKLSEFYEEYLDELREIEKRLSRLEE----EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL 363

                         170
                  ....*....|....*
gi 568987340 1058 cqYMMATKKDESMNS 1072
Cdd:PRK03918  364 --YEEAKAKKEELER 376
PTZ00121 PTZ00121
MAEBL; Provisional
 899-1093 1.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  899 REKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEiadfEQQKARELARIEEYRK-EETRKLQKERKVFEkyTAAAR 977
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE----EAKKADEAKKAEEAKKaDEAKKAEEKKKADE--LKKAE 1555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  978 TFPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENSPKA 1057
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568987340 1058 CQymMATKKDESMNSSFQFQKSHVSSGVQVEKYKKK 1093
Cdd:PTZ00121 1636 EQ--LKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 898-1104 1.57e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEET---RKLQKERKVFEKYTA 974
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelrAELEAQKEELAELLR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  975 AA---------------RTFPD----------------------KKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLR 1017
Cdd:COG4942   112 ALyrlgrqpplalllspEDFLDavrrlqylkylaparreqaeelRADLAELAALRAELEAERAELEALLAELEEERAALE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340 1018 SQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENSPKACQYMMATKKDESMNSSFqfqkshvssgvqvEKYKKKY-LP 1096
Cdd:COG4942   192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF-------------AALKGKLpWP 258


                  ....*...
gi 568987340 1097 AQGNLSRR 1104
Cdd:COG4942   259 VSGRVVRR 266
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
878-1017 2.88e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  878 ESKLNLSQDQPP--GDSVRSQVLREKVTELESEIEKFKAENTslaklriERESALEKLRKEIADFEQQKARELARIEEYR 955
Cdd:COG3206   246 RAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSARYT-------PNHPDVIALRAQIAALRAQLQQEAQRILASL 318

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987340  956 KEETRKLQKERKVFEKYTAAArtfpdKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLR 1017
Cdd:COG3206   319 EAELEALQAREASLQAQLAQL-----EARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 923-1048 2.93e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   923 RIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAARTFPD-----KKEREEIQALKQQIAD 997
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlARLEAEVEQLEERIAQ 751

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568987340   998 LQEDLKRKETKWSSTQSRL---RSQIEMLVKENTDLREEIKVMERfRLDAWKRA 1048
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLeeaEEELAEAEAEIEELEAQIEQLKE-ELKALREA 804
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 888-1038 3.40e-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: 45.06  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   888 PPGDSVRSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEqqkaRELARIEEYRKEETRKLqKERK 967
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE----KEIEQLEQEEEKLKERL-EELE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987340   968 VFEKYTAAARTfpdkKEREEIQALKQQIADLQEDLKRKETKWSSTQSRL-RSQIEMLVKENTDLREEIKVME 1038
Cdd:TIGR02169  744 EDLSSLEQEIE----NVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIE 811
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 894-1044 3.47e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   894 RSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETR------KLQKERK 967
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaaNLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   968 VFEKYTAAARTFPD------KKEREEIQALKQQIADLQEDLKRKE---TKWSSTQSRLRSQIEMLVKENTDLREEIKVME 1038
Cdd:TIGR02168  828 SLERRIAATERRLEdleeqiEELSEDIESLAAEIEELEELIEELEselEALLNERASLEEALALLRSELEELSEELRELE 907


                   ....*.
gi 568987340  1039 RFRLDA 1044
Cdd:TIGR02168  908 SKRSEL 913
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
891-1044 4.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  891 DSVRSQVLREkVTELE---------SEIEK-FKAENTSLAKLrIERESALEKLRKEIADFEQQKARELARIEEYRKEETR 960
Cdd:PRK03918  144 DESREKVVRQ-ILGLDdyenayknlGEVIKeIKRRIERLEKF-IKRTENIEELIKEKEKELEEVLREINEISSELPELRE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  961 KLQKERKVFEKYtaaartfpdKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRlrsqIEMLVKENTDLREEIKVMERF 1040
Cdd:PRK03918  222 ELEKLEKEVKEL---------EELKEEIEELEKELESLEGSKRKLEEKIRELEER----IEELKKEIEELEEKVKELKEL 288


                  ....
gi 568987340 1041 RLDA 1044
Cdd:PRK03918  289 KEKA 292
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
894-1039 5.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  894 RSQVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKAR--ELARIEEYRKEETRKLQKERKVFEK 971
Cdd:PRK03918  187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieELEKELESLEGSKRKLEEKIRELEE 266

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987340  972 YTaaartfpdKKEREEIQALKQQIADLQEdLKRKETKW---SSTQSRLRSQIEMLVKENTDLREEIKVMER 1039
Cdd:PRK03918  267 RI--------EELKKEIEELEEKVKELKE-LKEKAEEYiklSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 896-1050 5.52e-04

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: 43.98  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAENTSLaklrierESALEKLRKEIAD-----------------FEQQKARELAR-------I 951
Cdd:COG4942    72 RALEQELAALEAELAELEKEIAEL-------RAELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRrlqylkyL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  952 EEYRKEETRKLQKERKVFEKYTAAARTFPDKKE--REEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTD 1029
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEalLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                         170       180
                  ....*....|....*....|.
gi 568987340 1030 LREEIKVMERFRLDAWKRAEA 1050
Cdd:COG4942   225 LEALIARLEAEAAAAAERTPA 245
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 894-1064 5.56e-04

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: 44.34  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   894 RSQVLREKVTELES-EIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKAReLARIEEYRKEETRKLQKE------- 965
Cdd:pfam17380  411 RQRKIQQQKVEMEQiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER-LRQQEEERKRKKLELEKEkrdrkra 489

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   966 ----RKVFEKYTAAARTFPDKKEREEiQALKQQIADLQEDLKRKETKWSSTQSRlRSQIEMlvKENTDLREEIKVM--ER 1039
Cdd:pfam17380  490 eeqrRKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEER-RKQQEM--EERRRIQEQMRKAteER 565

                          170       180       190
                   ....*....|....*....|....*....|
gi 568987340  1040 FRLDAWKRAEAM-----ENSPKACQYMMAT 1064
Cdd:pfam17380  566 SRLEAMEREREMmrqivESEKARAEYEATT 595
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 920-1025 5.72e-04

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: 43.98  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  920 AKLRIERESALEKLRKEIADFEQQKARElarieeyrKEETRKLQKERKVFEKYTAAArtfpdkkeREEIQALKQQIADLQ 999
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAAL--------KKEEKALLKQLAALERRIAAL--------ARRIRALEQELAALE 82

                          90       100
                  ....*....|....*....|....*.
gi 568987340 1000 EDLKRKETKWSSTQSRLRSQIEMLVK 1025
Cdd:COG4942    83 AELAELEKEIAELRAELEAQKEELAE 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
898-1013 6.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAklriERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAAr 977
Cdd:COG4717   137 LEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL- 211

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568987340  978 tfpdkkeREEIQALKQQIADLQEDLKRKETKWSSTQ 1013
Cdd:COG4717   212 -------EEELEEAQEELEELEEELEQLENELEAAA 240
PTZ00121 PTZ00121
MAEBL; Provisional
 899-1093 7.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  899 REKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADfEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAART 978
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  979 FPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEmlVKENTDLREEIKVMERFRLDAWKRAEAmENSPKAC 1058
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE--EKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAA 1664

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568987340 1059 QymMATKKDESMNSSFQFQKSHVSSGVQVEKYKKK 1093
Cdd:PTZ00121 1665 E--EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
900-1041 8.70e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  900 EKVTELESEIEKFKAENTSLAKLRiERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAARTF 979
Cdd:COG1340   140 EKIKELEKELEKAKKALEKNEKLK-ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987340  980 PDKKE-----REEIQALKQQIADLQEDLKRKETKWSSTQSRlrsqiemlvKENTDLREEIK-VMERFR 1041
Cdd:COG1340   219 VEAQEkadelHEEIIELQKELRELRKELKKLRKKQRALKRE---------KEKEELEEKAEeIFEKLK 277
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 918-1042 1.30e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  918 SLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAArtfpdKKEREE-IQALKQQIA 996
Cdd:PRK00409  524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEA-----KKEADEiIKELRQLQK 598

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568987340  997 DLQEDLKRKETKwsSTQSRLRSQIEML---VKENTDLREEIKVMERFRL 1042
Cdd:PRK00409  599 GGYASVKAHELI--EARKRLNKANEKKekkKKKQKEKQEELKVGDEVKY 645
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 898-1034 1.35e-03

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: 42.36  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESAL-EKLRKEIADFEQQKAREL-ARIEEYRKEETRKLqkerkvfekytaa 975
Cdd:cd22656   133 YQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKEIKDLqKELEKLNEEYAAKL------------- 199

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340  976 artfpdkkeREEIQALKQQIADLQEDLKRKEtkwsstqsRLRSQIEMLVKENTDLREEI 1034
Cdd:cd22656   200 ---------KAKIDELKALIADDEAKLAAAL--------RLIADLTAADTDLDNLLALI 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
896-1034 1.42e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAEntsLAKLRIERESA----LEKLRKEIADFEQQKARELARIEEYRkEETRKLQ----KERK 967
Cdd:COG4913   305 ARLEAELERLEARLDALREE---LDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLE-ALLAALGlplpASAE 380

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987340  968 VFEKYTAAARTFPDKKE------REEIQALKQQIADLQEDLKRKETKWSSTQSRlRSQIEmlvKENTDLREEI 1034
Cdd:COG4913   381 EFAALRAEAAALLEALEeelealEEALAEAEAALRDLRRELRELEAEIASLERR-KSNIP---ARLLALRDAL 449
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 896-1039 1.50e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAE----NTSLAKLRIERESALEKLRKEIADFEQQKARE---------------------LAR 950
Cdd:COG3883    47 EELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRSGGSVsyldvllgsesfsdfldrlsaLSK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  951 IEEYRKEETRKLQKERKVFEKYTAAARtfpdkKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDL 1030
Cdd:COG3883   127 IADADADLLEELKADKAELEAKKAELE-----AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201


                  ....*....
gi 568987340 1031 REEIKVMER 1039
Cdd:COG3883   202 EAELAAAEA 210
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
891-1053 1.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  891 DSVRSQVLREKVTELESEIEKFKAENTslaklriERESALEKLRKEIADFEQQKA-----RE--------LARIEEYRKE 957
Cdd:PRK02224  535 KRERAEELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAelkerIEslerirtlLAAIADAEDE 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  958 ETRKLQKERKVFEKYTAAARTFPDKKER-------------EEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEML- 1023
Cdd:PRK02224  608 IERLREKREALAELNDERRERLAEKRERkreleaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVe 687

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568987340 1024 --VKENTDLREEIKVME--RFRLDA-WKRAEAMEN 1053
Cdd:PRK02224  688 neLEELEELRERREALEnrVEALEAlYDEAEELES 722
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
894-1038 1.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  894 RSQVLREKVTELESEIEKFKAE-------NTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRK------EETR 960
Cdd:PRK02224  280 EVRDLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREdaddleERAE 359

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987340  961 KLQKERKVFEKYTAAARTFPDKKeREEIQALKQQIADLQEDLKRKETKWSSTQSRLrsqiEMLVKENTDLREEIKVME 1038
Cdd:PRK02224  360 ELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAPVDLGNAEDFL----EELREERDELREREAELE 432
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 903-1044 2.16e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   903 TELESEIEKFKAEN-TSLAKLRIErESALEKLRKEIADFEqqkaRELARIEEYRKEETR--KLQKERKVFEKYTAAARTf 979
Cdd:pfam12128  743 SGAKAELKALETWYkRDLASLGVD-PDVIAKLKREIRTLE----RKIERIAVRRQEVLRyfDWYQETWLQRRPRLATQL- 816

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987340   980 pdKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDA 1044
Cdd:pfam12128  817 --SNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA 879
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 907-997 2.27e-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: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   907 SEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAARTFPDKKERE 986
Cdd:pfam03938   12 EESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91

                           90
                   ....*....|.
gi 568987340   987 EIQALKQQIAD 997
Cdd:pfam03938   92 LLQPIQDKINK 102
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 879-1020 2.33e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  879 SKLNLSQDQPPgdsvrsqvlrEKVTELESEIEKfkaentslakLRIEREsALEKlRKEIADFE--QQKARELARIEEYRK 956
Cdd:COG0542   400 ARVRMEIDSKP----------EELDELERRLEQ----------LEIEKE-ALKK-EQDEASFErlAELRDELAELEEELE 457

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987340  957 EETRKLQKERKVFEKYTAAartfpdkkeREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQI 1020
Cdd:COG0542   458 ALKARWEAEKELIEEIQEL---------KEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
PTZ00121 PTZ00121
MAEBL; Provisional
 900-1092 2.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  900 EKVTELESEIEKFKAEN---TSLAKLRIERESALEKLRKEIADFEQQKARELARIEEYRKEEtrklqkERKVFEKYTAAA 976
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE------EENKIKAAEEAK 1668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  977 RTFPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQsRLRSQIEMLVKENTDLREEIKVmERFRLDAWKRaEAMENSPK 1056
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKK-EAEEDKKK 1745

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568987340 1057 ACQymmATKKDESMNSSFQFQKSHVSSGVQVEKYKK 1092
Cdd:PTZ00121 1746 AEE---AKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 899-1035 2.72e-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: 42.36  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   899 REKVTELESEIEKFKA----ENTSLAKLRIERESALE--KLRKEIADFEQ-QKARELARIEEYRKEETRKLQKERKVFEK 971
Cdd:TIGR02169  176 LEELEEVEENIERLDLiideKRQQLERLRREREKAERyqALLKEKREYEGyELLKEKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987340   972 YTAAArtfPDKKER-----EEIQALKQQIADLQED----LKRKETKWSSTQSRLRSQIEMLVKENTDLREEIK 1035
Cdd:TIGR02169  256 LTEEI---SELEKRleeieQLLEELNKKIKDLGEEeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
898-1035 3.26e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIE---RESALEKLRKEIADFEQqkarelarieEYRKEETRKLQKERKVFEKYTA 974
Cdd:PRK03918  607 LKDAEKELEREEKELKKLEEELDKAFEElaeTEKRLEELRKELEELEK----------KYSEEEYEELREEYLELSRELA 676

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987340  975 AARtfpdkKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSqIEMLVKENTDLREEIK 1035
Cdd:PRK03918  677 GLR-----AELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
PRK12704 PRK12704
phosphodiesterase; Provisional
 933-1039 3.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  933 LRKEIADFEQQKARELAR--IEEYRKE-ETRKLQKERKVFEKYTAAARTFPD--KKEREEIQALKQQIADLQEDLKRKET 1007
Cdd:PRK12704   24 VRKKIAEAKIKEAEEEAKriLEEAKKEaEAIKKEALLEAKEEIHKLRNEFEKelRERRNELQKLEKRLLQKEENLDRKLE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568987340 1008 KWSSTQSRLRSQIEMLVKENTDLREEIKVMER 1039
Cdd:PRK12704  104 LLEKREEELEKKEKELEQKQQELEKKEEELEE 135
alph_xenorhab_B NF033927
alpha-xenorhabdolysin family binary toxin subunit B;
898-1054 3.45e-03

alpha-xenorhabdolysin family binary toxin subunit B;


Pssm-ID: 411488 [Multi-domain]  Cd Length: 223  Bit Score: 40.69  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAENTSLAKLRIERESA--LEKLRKEIADFEQQKARELARIEEyRKEETRKLQKERKVFEKYTAA 975
Cdd:NF033927    2 LSNVIAALRKSAAKIANKLDDLSQINLREATLdlLAQLQEQIAELEAQIAALESKLNE-LAEDRKVIIEAIDLIEKYNIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  976 AR---TFPDKKE-------REEIQALKQQIadlqEDLKRKETKWSS---------TQSRLRSQIEMLVKENTDLREEIKV 1036
Cdd:NF033927   81 DLfkdLLPTAEEidslglpPPEKDLVKAAI----ERLKKLLGKISEgltyidlveARDKLRDRINALLAESRTLDKDIKA 156

                         170
                  ....*....|....*...
gi 568987340 1037 MErFRLDAWKRAEAMENS 1054
Cdd:NF033927  157 LA-GKLEELTAIAAIDEE 173
46 PHA02562
endonuclease subunit; Provisional
 870-1034 4.12e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  870 KLDSHLENESKLNLSQDQppgdsvRSQVLREKVTELESEIEKFKAE----NTSLAKLRIERE---SALEKLRKEIADFEQ 942
Cdd:PHA02562  196 QIKTYNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEieelTDELLNLVMDIEdpsAALNKLNTAAAKIKS 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  943 QKARelarieeyrkeetrkLQKERKVFEKY-TAAARTFPDKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLrSQIE 1021
Cdd:PHA02562  270 KIEQ---------------FQKVIKMYEKGgVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM-DEFN 333

                         170
                  ....*....|...
gi 568987340 1022 MLVKENTDLREEI 1034
Cdd:PHA02562  334 EQSKKLLELKNKI 346
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 897-965 4.15e-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: 41.58  E-value: 4.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340   897 VLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEI----ADFEQQKarelARIEEYRKE------ETRKLQKE 965
Cdd:pfam05911   89 ELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKsqaeAEIEALK----SRLESCEKEinslkyELHVLSKE 163
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 920-1068 4.30e-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: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  920 AKLRIERES---ALEKLRKEIADFEQQKARelarieeyrkeetrkLQKERkvfekytaaartfpDKKEREEIQALKQQIA 996
Cdd:COG0542   400 ARVRMEIDSkpeELDELERRLEQLEIEKEA---------------LKKEQ--------------DEASFERLAELRDELA 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987340  997 DLQEDLKRKETKWSSTQSrlrsqiemLVKENTDLREEIKVMERFRLDAWKRAEAMENSPKACQYMMATKKDE 1068
Cdd:COG0542   451 ELEEELEALKARWEAEKE--------LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 896-985 5.16e-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: 40.90  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  896 QVLREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADfEQQKARELARIEEYRKEETRKLQKERKVFEKYTAA 975
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE-LAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                          90
                  ....*....|
gi 568987340  976 ArTFPDKKER 985
Cdd:COG4942   246 A-GFAALKGK 254
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
898-1044 5.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  898 LREKVTELESEIEKFKAEntsLAKLRIERESALEKLRKEIADFEQQKARelariEEYRKEETRKLQKERKVFEKYTAAAr 977
Cdd:COG4372    50 LREELEQAREELEQLEEE---LEQARSELEQLEEELEELNEQLQAAQAE-----LAQAQEELESLQEEAEELQEELEEL- 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987340  978 tfpdKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDA 1044
Cdd:COG4372   121 ----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 919-1109 5.79e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.76  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   919 LAKLRIERESALEKlRKEIADFEQQKARELARIEEYRKEETRKLQKERKVFEKYTAAARTFPDKKEREEIQALKQ----- 993
Cdd:pfam05262  183 VEALREDNEKGVNF-RRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEaknlp 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   994 QIADLQEDLKRKETKWSSTQSRLRSQIEmlVKENTDlrEEIKVMERFRLDAWKRAEAMENspkacqymMATKKDESMnss 1073
Cdd:pfam05262  262 KPADTSSPKEDKQVAENQKREIEKAQIE--IKKNDE--EALKAKDHKAFDLKQESKASEK--------EAEDKELEA--- 326

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 568987340  1074 fQFQKSHVSSGVQVEKYKKKYLPAQGNLSRRIKSAP 1109
Cdd:pfam05262  327 -QKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNP 361
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 903-1039 5.81e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.88  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   903 TELESEIEKFKAENTSLAKLRiERESALEKLRKEIADFEQQKARELARIEEYRKEETRKLQKERKV---FEKYTAAARTF 979
Cdd:pfam05557   41 RQLDRESDRNQELQKRIRLLE-KREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREViscLKNELSELRRQ 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   980 PDKKErEEIQALKQQIADLQEDLKRKETKWSSTqSRLRSQIEMLVKENTDLREEIKVMER 1039
Cdd:pfam05557  120 IQRAE-LELQSTNSELEELQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAEQRIKELEF 177
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 898-1035 6.14e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELArieeyrKEETRKLQKE-RKVFEKYTAAa 976
Cdd:TIGR04523  508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL------EKEIDEKNKEiEELKQTQKSL- 580

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340   977 rtfpdKKEREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIK 1035
Cdd:TIGR04523  581 -----KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 898-965 6.24e-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: 39.05  E-value: 6.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987340  898 LREKVTELESEIEKFKAENTSL-AKLRIERESALEKLRKEIADFEQQKARELARIeeyRKEETRKLQKE 965
Cdd:COG2825    59 LQKLEKELQALQEKLQKEAATLsEEERQKKERELQKKQQELQRKQQEAQQDLQKR---QQELLQPILEK 124
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
900-1034 6.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340  900 EKVTELESEIEKFKAENTSLAKLriERESALEKLRKEI--------ADFEQQKARELARIEEYRKEETRKLQKERKV--- 968
Cdd:COG4717   337 EELLELLDRIEELQELLREAEEL--EEELQLEELEQEIaallaeagVEDEEELRAALEQAEEYQELKEELEELEEQLeel 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987340  969 FEKYTAAARTFPDKKEREEIQALKQQIADLQEDLKRKETKwsstQSRLRSQIEMLVKENT--DLREEI 1034
Cdd:COG4717   415 LGELEELLEALDEEELEEELEELEEELEELEEELEELREE----LAELEAELEQLEEDGElaELLQEL 478
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 895-1054 7.36e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.28  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   895 SQVLREKVTELESEIEkfkAENTSLAKLRIERESALEKLRKEIAdfeQQKARElarieeyrKEETRKLQKERKVFEKYTA 974
Cdd:pfam04012    6 GRLVRANIHEGLDKAE---DPEKMLEQAIRDMQSELVKARQALA---QTIARQ--------KQLERRLEQQTEQAKKLEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   975 AARTFPDKKEREEIQALKQQIADLQEDLKRKETKWS---STQSRLRSQIEMLVKENTDLREEIKVMeRFRLDAWKRAEAM 1051
Cdd:pfam04012   72 KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAqqrSAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAV 150


                   ...
gi 568987340  1052 ENS 1054
Cdd:pfam04012  151 QTS 153
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
 891-969 7.71e-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: 7.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   891 DSVRSQVLREKVTELESEIEKFKA----ENTSLAKLRIERESALEKLRKE-----IADFEQQKARELARIEeyrkEETRK 961
Cdd:pfam14943   55 YEEELGSESEEEAEEEEEHRELMAwneeWNAEIAKLREERLAKEAEEREEeilerIEEKEEKEEEKKERAE----EEVRQ 130


                   ....*...
gi 568987340   962 LQKERKVF 969
Cdd:pfam14943  131 EKEESKTF 138
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 898-965 7.77e-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: 38.33  E-value: 7.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987340   898 LREKVTELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKARELARIeeyRKEETRKLQKE 965
Cdd:pfam03938   35 LEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKK---QQELLQPIQDK 99
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 904-1076 8.63e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 8.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   904 ELESEIEKFKAENTSLAKLRIERESALEKLRKEIADFEQQKAReLARIEEYRKEETRKLQKERKVFEKYTaaartfpdKK 983
Cdd:pfam15921  594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK-LVNAGSERLRAVKDIKQERDQLLNEV--------KT 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987340   984 EREEIQALKQQIADLQEDLKRKETKWSSTQSRLRSQIEMLVKENTDLREEIKVMERFRLDAWKRAEAMENspkacQYMMA 1063
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK-----QITAK 739

                          170
                   ....*....|...
gi 568987340  1064 TKKDESMNSSFQF 1076
Cdd:pfam15921  740 RGQIDALQSKIQF 752
 
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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