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Conserved domains on  [gi|2024505059|ref|XP_040529043|]
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ras association domain-containing protein 8 isoform X1 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.48e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


:

Pssm-ID: 340552  Cd Length: 83  Bit Score: 178.98  E-value: 2.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505059  81 GPS 83
Cdd:cd16135    81 GPS 83
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-351 1.48e-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: 60.70  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHGDTLEtdlRLWEHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQER 245
Cdd:COG4913    241 HEALEDAREQIELLEPIRELAERYA---AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 VRSLRASLEEYTQRIYELS-ARTEALQKEIQWEMAERAKRG----------KEIPVPSPTDLEDMAAkMKRDLEAKVKQG 314
Cdd:COG4913    318 LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA-LRAEAAALLEAL 396

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024505059  315 TQLEnnlASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG4913    397 EEEL---EALEEALAEAEAALRDLRRELRELEAEIAS 430
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.48e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 178.98  E-value: 2.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505059  81 GPS 83
Cdd:cd16135    81 GPS 83
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.24e-10

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 57.69  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059    1 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL-REKERQLLPLECPLESLAKCGQYANDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2024505059   74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 1.50e-10

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 57.73  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   1 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL--REKERQLLPLECPLESLAKCGQYAN 71
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2024505059  72 DVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-351 1.48e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHGDTLEtdlRLWEHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQER 245
Cdd:COG4913    241 HEALEDAREQIELLEPIRELAERYA---AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 VRSLRASLEEYTQRIYELS-ARTEALQKEIQWEMAERAKRG----------KEIPVPSPTDLEDMAAkMKRDLEAKVKQG 314
Cdd:COG4913    318 LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA-LRAEAAALLEAL 396

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024505059  315 TQLEnnlASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG4913    397 EEEL---EALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-356 1.04e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  190 ETDLRLW------EHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLE----KECERERQERVRSLRASLEEYTQR 259
Cdd:TIGR02168  224 ELELALLvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  260 IYELSARTEALQKEIQWEMAERAKRGKeipvpSPTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQN 339
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170
                   ....*....|....*..
gi 2024505059  340 QELEELNKELRQCNLQQ 356
Cdd:TIGR02168  379 EQLETLRSKVAQLELQI 395
PRK12705 PRK12705
hypothetical protein; Provisional
 227-351 2.12e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 227 FWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVpsptdledmaaKMKRD 306
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV-----------QKEEQ 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2024505059 307 LEAKVKQGTQLENNLasvekalEEAERSLQAQNQELEELNKELRQ 351
Cdd:PRK12705   93 LDARAEKLDNLENQL-------EEREKALSARELELEELEKQLDN 130
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 164-345 2.08e-04

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: 43.95  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  164 SKEELFKTVLRQQE-----QLHSLEAHGDTLETDLRlwEHGRasSQEDEILYLEHLVRRNDTELGE-----EEFWQS--- 230
Cdd:pfam15921  299 SQLEIIQEQARNQNsmymrQLSDLESTVSQLRSELR--EAKR--MYEDKIEELEKQLVLANSELTEarterDQFSQEsgn 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  231 -----------------ELRLEKECERERQER-------VRSLRASLEEYTQRIYELSARTEALQKEIQWEMAER--AKR 284
Cdd:pfam15921  375 lddqlqklladlhkrekELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaAIQ 454

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024505059  285 GKEIPVPSPTDL-------EDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEEL 345
Cdd:pfam15921  455 GKNESLEKVSSLtaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 257-365 3.08e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  257 TQRIYELSARTEALQKEIQwemAERAKRGKEipvpsptdLEDMAAKMKRDLEAKVKQGTQL-ENNLASVEKALEEAERSL 335
Cdd:smart00935   6 VQKILQESPAGKAAQKQLE---KEFKKRQAE--------LEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEF 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024505059  336 QAQNQELEELNKELRQCNLQQFIQQTGATV 365
Cdd:smart00935  75 QRKQQKLQQDLQKRQQEELQKILDKINKAI 104
 
Name Accession Description Interval E-value
RA_RASSF7 cd16135
Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); ...
 1-83 2.48e-55

Ras-associating (RA) domain found in N-terminal Ras-association domain family 7 (RASSF7); RASSF7, also termed HRAS1-related cluster protein 1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF protein family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF7 is a potential Ras effector as its function has been linked to some key biological processes including the regulation of cell death and proliferation; for example, RASSF7 is up-regulated in pancreatic cancer.


Pssm-ID: 340552  Cd Length: 83  Bit Score: 178.98  E-value: 2.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRT 80
Cdd:cd16135     1 MELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRYVLIQKLRDKERQLLANECPLEALAKCGQYANDVQFILRRT 80


                  ...
gi 2024505059  81 GPS 83
Cdd:cd16135    81 GPS 83
RA_RASSF8 cd16134
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ...
 2-83 1.79e-43

Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.


Pssm-ID: 340551  Cd Length: 82  Bit Score: 147.97  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILRRTG 81
Cdd:cd16134     1 ELKVWVDGIQRVVCGVTEVTTCQEVVIALAQATGRTGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTG 80


                  ..
gi 2024505059  82 PS 83
Cdd:cd16134    81 PS 82
RA_RASSF7_like cd16123
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ...
 2-79 5.07e-34

Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.


Pssm-ID: 340540  Cd Length: 81  Bit Score: 122.74  E-value: 5.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARAIGQ---TGRYVLVQKLREKERQLLPLECPLESLAKCGQYANDVQFILR 78
Cdd:cd16123     1 ELKVWVDGEERVVSGVTERTTCQDVIYALAQATGQtndTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLR 80


                  .
gi 2024505059  79 R 79
Cdd:cd16123    81 R 81
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-81 1.24e-10

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 57.69  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059    1 MELKVWVD---GIQRVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL-REKERQLLPLECPLESLAKCGQYANDV 73
Cdd:smart00314   3 FVLRVYVDdlpGGTYKTLRVSSRTTARDVIQQLLEKFHLTDdpeEYVLVEVLpDGKERVLPDDENPLQLQKLWPRRGPNL 82


                   ....*...
gi 2024505059   74 QFILRRTG 81
Cdd:smart00314  83 RFVLRKRD 90
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
 1-79 1.50e-10

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 57.73  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   1 MELKVWVDGIQ----RVVCGVSEQTTCQEVVIALARAIGQTG---RYVLVQKL--REKERQLLPLECPLESLAKCGQYAN 71
Cdd:pfam00788   3 GVLKVYTEDGKpgttYKTILVSSSTTAEEVIEALLEKFGLEDdprDYVLVEVLerGGGERRLPDDECPLQIQLQWPRDAS 82


                  ....*...
gi 2024505059  72 DVQFILRR 79
Cdd:pfam00788  83 DSRFLLRK 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
 3-79 8.23e-10

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 55.40  E-value: 8.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   3 LKVWVDGIQ-----RVVCgVSEQTTCQEVVIALARAIG---QTGRYVLVQKL--REKERQLLPLECPLESLAKCGQYAND 72
Cdd:cd17043     2 LKVYDDDLApgsayKSIL-VSSTTTAREVVQLLLEKYGleeDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80


                  ....*..
gi 2024505059  73 VQFILRR 79
Cdd:cd17043    81 FRFVLKR 87
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-351 1.48e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHGDTLEtdlRLWEHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQER 245
Cdd:COG4913    241 HEALEDAREQIELLEPIRELAERYA---AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 VRSLRASLEEYTQRIYELS-ARTEALQKEIQWEMAERAKRG----------KEIPVPSPTDLEDMAAkMKRDLEAKVKQG 314
Cdd:COG4913    318 LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERErrrarleallAALGLPLPASAEEFAA-LRAEAAALLEAL 396

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024505059  315 TQLEnnlASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG4913    397 EEEL---EALEEALAEAEAALRDLRRELRELEAEIAS 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 174-351 7.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 174 RQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEilyLEHLVRRNDTELGEEEFWQSELrlEKECERERQERVRsLRASL 253
Cdd:COG1196   210 EKAERYRELKEELKELEAELLLLKLRELEAELEE---LEAELEELEAELEELEAELAEL--EAELEELRLELEE-LELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 254 EEYTQRIYELSARTEALQKEIQWEMAERAkrgkeipvpsptDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAER 333
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRR------------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         170
                  ....*....|....*...
gi 2024505059 334 SLQAQNQELEELNKELRQ 351
Cdd:COG1196   352 ELEEAEAELAEAEEALLE 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-356 1.04e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  190 ETDLRLW------EHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLE----KECERERQERVRSLRASLEEYTQR 259
Cdd:TIGR02168  224 ELELALLvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  260 IYELSARTEALQKEIQWEMAERAKRGKeipvpSPTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQN 339
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170
                   ....*....|....*..
gi 2024505059  340 QELEELNKELRQCNLQQ 356
Cdd:TIGR02168  379 EQLETLRSKVAQLELQI 395
RA_RASSF9 cd16133
Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, ...
 2-77 2.02e-06

Ras-associating (RA) domain of N-terminal Ras-association domain family 9 (RASSF9); RASSF9, also termed PAM COOH-terminal interactor protein 1 (P-CIP1), or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor, is a member of N-terminus RASSF7-10 protein family. RASSF7-10 has an RA domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of the N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF9 was formerly known as PAM COOH-terminal interactor-1 (P-CIP1) because of its interaction with peptidylglycine alpha-amidating mono-oxygenase (PAM) and possibility of its role in regulating the trafficking of integral membrane PAM. RASSF9 is widely expressed in multiple organs such as testis, kidney, skeletal muscle, liver, lung, brain, and heart. Cloned RASSF9 showed preferential binding to N-Ras and K-Ras.


Pssm-ID: 340550  Cd Length: 93  Bit Score: 45.99  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059   2 ELKVWVDGIQRVVCGVSEQTTCQEVVIALARA-----------IGQTGRYVLVQKLREKERQLLPLECPLESLAKCGQYA 70
Cdd:cd16133     1 EIVVWVCQEEKVVCGLTKHTTCADVIQALLEEheatfgekrflLGQPSDYCIVEKWRGFERVLPPLTKILRLWKAWGDEQ 80


                  ....*..
gi 2024505059  71 NDVQFIL 77
Cdd:cd16133    81 PNLQFVL 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-374 1.50e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  217 RNDTELGEEEFWQSELRLE--KECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIpvpspT 294
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL-----T 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  295 DLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKELRQcnLQQFIQQTGATVTVGQARSEE 374
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL--LNEEAANLRERLESLERRIAA 835
PRK12705 PRK12705
hypothetical protein; Provisional
 227-351 2.12e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 227 FWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVpsptdledmaaKMKRD 306
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV-----------QKEEQ 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2024505059 307 LEAKVKQGTQLENNLasvekalEEAERSLQAQNQELEELNKELRQ 351
Cdd:PRK12705   93 LDARAEKLDNLENQL-------EEREKALSARELELEELEKQLDN 130
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-351 3.64e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 3.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  165 KEELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEILYLEHLVRRNDTELGEEEFW----------QSELRL 234
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqieqlKEELKA 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  235 EKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQwEMAERAKRGKEIPV---PSPTDLEDMAAKMKRDLEAKV 311
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIEslaAEIEELEELIEELESELEALL 879

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024505059  312 KQGTQLENNLASVEKALEEaersLQAQNQELEELNKELRQ 351
Cdd:TIGR02168  880 NERASLEEALALLRSELEE----LSEELRELESKRSELRR 915
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 146-346 5.79e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.71  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  146 RQHAwEGMDLKDGGAGQPSKEELFKT---VLRQQEQLHSLEAHGDTLETDLRLWEHgRASSQEDEILYLEHLVRR----- 217
Cdd:COG3096    472 RQFE-KAYELVCKIAGEVERSQAWQTareLLRRYRSQQALAQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRigqql 549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  218 NDTELGEEEFWQSELRLEkECE---RERQERVRSLRASLEEYTQRIYELSARTEAlqkeiqW-EMAERAKRGKEIPVPSP 293
Cdd:COG3096    550 DAAEELEELLAELEAQLE-ELEeqaAEAVEQRSELRQQLEQLRARIKELAARAPA------WlAAQDALERLREQSGEAL 622

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024505059  294 TDLEDMAAKMKRDLEaKVKQGTQLENNLASVEKALE-EAERSLQAQNQELEELN 346
Cdd:COG3096    623 ADSQEVTAAMQQLLE-REREATVERDELAARKQALEsQIERLSQPGGAEDPRLL 675
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 171-351 6.57e-05

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: 44.15  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 171 TVLRQQEQLHSLEAhgdtLETDLRLWEHGRASSQEdEILYLEHLVRRNDTELGEEEFWQSELRLEKeceRERQERVRSLR 250
Cdd:COG1579     1 AMPEDLRALLDLQE----LDSELDRLEHRLKELPA-ELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEEVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 251 ASLEEYTQRIyeLSART----EALQKEIqwEMAERAKRgkeipvpsptDLEDMAAKMKRDLEAKVKQGTQLENNLASVEK 326
Cdd:COG1579    73 ARIKKYEEQL--GNVRNnkeyEALQKEI--ESLKRRIS----------DLEDEILELMERIEELEEELAELEAELAELEA 138

                         170       180
                  ....*....|....*....|....*
gi 2024505059 327 ALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG1579   139 ELEEKKAELDEELAELEAELEELEA 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-349 6.75e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 6.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHgRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQER 245
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 VRSLRASLEE----YTQRIYELSARTEALQKEIQWEMAERAkrgkeipvpsptDLEDMAAKMKRDLEAKVKQGTQLENNL 321
Cdd:TIGR02168  780 AEAEIEELEAqieqLKEELKALREALDELRAELTLLNEEAA------------NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180
                   ....*....|....*....|....*...
gi 2024505059  322 ASVEKALEEAERSLQAQNQELEELNKEL 349
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESEL 875
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-382 8.36e-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: 45.44  E-value: 8.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  164 SKEELFKTVLRQQEQLHSLEAHGDTLETDLRlweHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQ 243
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEARLS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  244 ERVRSLRASLEEytqRIYELSARTEALQkeiqwemaerakrgkeipvpspTDLEDMAAKMKRdLEAKVKQgtqLENNLAS 323
Cdd:TIGR02169  836 QELQEQRIDLKE---QIKSIEKEIENLN----------------------GKKEELEEELEE-LEAALRD---LESRLGD 886

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024505059  324 VEKALEEAERSLQAQNQELEELNKELRQCNLQQFIQQTGATVTVGQARSEEDAQPELSP 382
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 233-351 9.03e-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: 45.06  E-value: 9.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  233 RLEKEceRERQERVRSLRASLEEYtqRIYELSARTEALQKEIQWEMAERAKRGKEIPvPSPTDLEDMAAKMK------RD 306
Cdd:TIGR02169  202 RLRRE--REKAERYQALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELEKRLEeieqllEE 276

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024505059  307 LEAKVKQGT-----QLENNLASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:TIGR02169  277 LNKKIKDLGeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-382 1.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEilyLEHLVRRNDTELGEEEFWQSELRLEKEcERERQER 245
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAEELLEALRA-AAELAAQ 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 246 VRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEipvpsptdledmAAKMKRDLEAKVKQGTQLENNLASVE 325
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA------------LEEAAEEEAELEEEEEALLELLAELL 469

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024505059 326 KALEEAERSLQAQNQELEELNKELRQcnLQQFIQQTGATVTVGQARSEEDAQPELSP 382
Cdd:COG1196   470 EEAALLEAALAELLEELAEAAARLLL--LLEAEADYEGFLEGVKAALLLAGLRGLAG 524
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 241-379 1.12e-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: 44.37  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 241 ERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKR-------GKEIPVP------SPTDLEDMAAKMKRDL 307
Cdd:COG4942    66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlGRQPPLAlllspeDFLDAVRRLQYLKYLA 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024505059 308 EAKVKQGTQLENNLAsvekALEEAERSLQAQNQELEELNKELRQCNLQQFIQQTGATVTVGQARSEEDAQPE 379
Cdd:COG4942   146 PARREQAEELRADLA----ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-351 1.17e-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: 44.66  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  165 KEELFKTVLRQQEQLHSLEAHGDTLETDLRLWEhgrasSQEDEILYLEHLVRRNDTELgEEEFWQSELRLEKECE----- 239
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEEL-KEELESLEAELEELEAeleel 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  240 ----RERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVPSPTDLEDMAAKMKRDLEAKVKQGT 315
Cdd:TIGR02168  371 esrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024505059  316 QLENNLASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 233-344 1.20e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  233 RLEK-ECERERQ-ERVRSLRASLEEYTQRIYELSARTEALQKEIQwemaERAKRGKEIPVPSPTDLEDMAAKMKRDLEAK 310
Cdd:COG3096    992 RLEQaEEARREArEQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ----ELEQELEELGVQADAEAEERARIRRDELHEE 1067

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024505059  311 V-----------KQGTQLENNLASVEKALEEAERSLQAQNQELEE 344
Cdd:COG3096   1068 LsqnrsrrsqleKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
166-364 1.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 166 EELFKTVLRQQEQLHSLEAHGDTLETDLRlwehgrasSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERErQER 245
Cdd:COG4717    77 EEELKEAEEKEEEYAELQEELEELEEELE--------ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL-PER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 246 VRSLRASLEEYTqriyELSARTEALQKEIQWEMAERAKRGKEIPVPSPTDLEDMAAKMKRdleakvkqgtqLENNLASVE 325
Cdd:COG4717   148 LEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE-----------LQQRLAELE 212

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2024505059 326 KALEEAERSLQAQNQELEELNKELRQCNLQQFIQQTGAT 364
Cdd:COG4717   213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-351 1.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEILYLE---HLVRRNDTELGEEEFWQSELRLEKECERER 242
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 243 QERVRSLRASLEEYTQRIYELSARTEALQKEI-QWEMAERAKRGKEIpvpsptDLEDMAAKMKRDLEAKVKQGTQLENNL 321
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELL------EALRAAAELAAQLEELEEAEEALLERL 416

                         170       180       190
                  ....*....|....*....|....*....|
gi 2024505059 322 ASVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEALEE 446
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 164-345 2.08e-04

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: 43.95  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  164 SKEELFKTVLRQQE-----QLHSLEAHGDTLETDLRlwEHGRasSQEDEILYLEHLVRRNDTELGE-----EEFWQS--- 230
Cdd:pfam15921  299 SQLEIIQEQARNQNsmymrQLSDLESTVSQLRSELR--EAKR--MYEDKIEELEKQLVLANSELTEarterDQFSQEsgn 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  231 -----------------ELRLEKECERERQER-------VRSLRASLEEYTQRIYELSARTEALQKEIQWEMAER--AKR 284
Cdd:pfam15921  375 lddqlqklladlhkrekELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaAIQ 454

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024505059  285 GKEIPVPSPTDL-------EDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEEL 345
Cdd:pfam15921  455 GKNESLEKVSSLtaqlestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
177-350 3.28e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 177 EQLHSLEAHGDTLETDLRLWEHGRASSQE-----DEILYlEHLVRRNDTELGEEEFwqSELRLEK-ECERERQ---ERVR 247
Cdd:PRK02224  206 ERLNGLESELAELDEEIERYEEQREQAREtrdeaDEVLE-EHEERREELETLEAEI--EDLRETIaETEREREelaEEVR 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 248 SLRASLEEYTQRIYELSARTE---ALQKEIQWEMAERAKRGKEIP------VPSPTDLEDMAAKMKRDLEAKVKQGTQLE 318
Cdd:PRK02224  283 DLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRdrleecRVAAQAHNEEAESLREDADDLEERAEELR 362

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2024505059 319 NNLASVEKALEEAERSLQAQNQELEELNKELR 350
Cdd:PRK02224  363 EEAAELESELEEAREAVEDRREEIEELEEEIE 394
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
164-360 3.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 164 SKEELFK----TVLRQQEQLHSLEAHGDTLETDLRLWEhgrasSQEDEILYLEHLVRRNDTELGEeefWQSELR-LEKEC 238
Cdd:COG4717    54 EADELFKpqgrKPELNLKELKELEEELKEAEEKEEEYA-----ELQEELEELEEELEELEAELEE---LREELEkLEKLL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 239 E-RERQERVRSLRASLEEYTQRIYELSARTEAL-QKEIQWEMAERAKRGKEipvpsptdlEDMAAKMKRDLEAKVKQGTQ 316
Cdd:COG4717   126 QlLPLYQELEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQ---------EELEELLEQLSLATEEELQD 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2024505059 317 LENNLASVEKALEEAERSLQAQNQELEELNKELRQCNLQQFIQQ 360
Cdd:COG4717   197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
166-348 6.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEHGRASSQEdEILYLEHLVRRNdTELGEEEFWQSELR------LEKECE 239
Cdd:PRK03918  234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK-EIEELEEKVKEL-KELKEKAEEYIKLSefyeeyLDELRE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 240 RE-RQERVRSLRASLEEYTQRIYELSARTEALQKEIqwemaERAKRGKEIPVPSPTDLEDMAAKMKR--DLEAKVKQGT- 315
Cdd:PRK03918  312 IEkRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----KELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTp 386

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2024505059 316 -QLENNLASVEKALEEAERSLQAQNQELEELNKE 348
Cdd:PRK03918  387 eKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
226-356 8.65e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  226 EFWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERakrgkEIpvpspTDLEDMaakmKR 305
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-----EI-----AELEAE----LE 678

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024505059  306 DLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKELRQCNLQQ 356
Cdd:COG4913    679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 219-355 1.31e-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: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 219 DTELGEEefwQSELR-LEKECERERQE------RVRSLRASLEEYTQ-------RIYELSARTEALQKEIQWEMAERAKR 284
Cdd:TIGR04523 362 QRELEEK---QNEIEkLKKENQSYKQEiknlesQINDLESKIQNQEKlnqqkdeQIKKLQQEKELLEKEIERLKETIIKN 438

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024505059 285 GKEIpvpspTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKELRQCNLQ 355
Cdd:TIGR04523 439 NSEI-----KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 158-348 1.39e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  158 GGAGQPSKEELFKT-----VLRQQEQLHSLEAHGDTLETDLRlwehgrasSQEDEILYLEHLVRRNDTELGEEEFWQSEL 232
Cdd:TIGR02169  657 GGSRAPRGGILFSRsepaeLQRLRERLEGLKRELSSLQSELR--------RIENRLDELSQELSDASRKIGEIEKEIEQL 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  233 RLEKECERERQErvrSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIpvpspTDLEDMAAKMKrdLEAKVK 312
Cdd:TIGR02169  729 EQEEEKLKERLE---ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSR--IPEIQA 798

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024505059  313 QGTQLENNLASVEKALEEAERSLQAQNQELEELNKE 348
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
PRK12704 PRK12704
phosphodiesterase; Provisional
 234-345 1.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 234 LEKECERERQERVRSLRASLE-EYTQRIYELSARTEAL-QKEiqwemaERAKRGKEipvpsptDLEdmaaKMKRDLEAKV 311
Cdd:PRK12704   54 IKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLlQKE------ENLDRKLE-------LLE----KREEELEKKE 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2024505059 312 KQGTQLENNLasvEKALEEAERSLQAQNQELEEL 345
Cdd:PRK12704  117 KELEQKQQEL---EKKEEELEELIEEQLQELERI 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 199-351 2.96e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 199 GRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQWEM 278
Cdd:COG1196   665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024505059 279 AERAKRGKEIPVPSPTDLEDMAAKMKRdLEAKVKqgtQLEN-NLASVE--KALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG1196   745 EELLEEEALEELPEPPDLEELERELER-LEREIE---ALGPvNLLAIEeyEELEERYDFLSEQREDLEEARETLEE 816
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 257-365 3.08e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  257 TQRIYELSARTEALQKEIQwemAERAKRGKEipvpsptdLEDMAAKMKRDLEAKVKQGTQL-ENNLASVEKALEEAERSL 335
Cdd:smart00935   6 VQKILQESPAGKAAQKQLE---KEFKKRQAE--------LEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEF 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024505059  336 QAQNQELEELNKELRQCNLQQFIQQTGATV 365
Cdd:smart00935  75 QRKQQKLQQDLQKRQQEELQKILDKINKAI 104
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 189-351 3.23e-03

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 39.77  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 189 LETDLRLWEHGRASSQEDEILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTE 268
Cdd:COG4251   122 LLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLL 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 269 ALQKEIQWEMAERAKRGKEIPVPSPTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKE 348
Cdd:COG4251   202 LLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEE 281


                  ...
gi 2024505059 349 LRQ 351
Cdd:COG4251   282 LEQ 284
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 257-351 3.40e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.94  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 257 TQRIYELSARTEALQKEIQwemAERAKRGKEipvpsptdLEDMAAKMKRDLEAKVKQGTQLENNLASVEKALEEAERSLQ 336
Cdd:pfam03938   7 MQKILEESPEGKAAQAQLE---KKFKKRQAE--------LEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQ 75

                          90
                  ....*....|....*....
gi 2024505059 337 ----AQNQELEELNKELRQ 351
Cdd:pfam03938  76 qlqqKAQQELQKKQQELLQ 94
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
241-351 3.41e-03

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 40.13  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 241 ERQERVRSLRASLEEYTQRIYELSARTEALQKEiqwemaerakrgkeipvpsptdledmAAKMKRDLEAKVKQGTQLENN 320
Cdd:COG1193   511 EESIDVEKLIEELERERRELEEEREEAERLREE--------------------------LEKLREELEEKLEELEEEKEE 564

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024505059 321 LasVEKALEEAERSLQAQNQELEELNKELRQ 351
Cdd:COG1193   565 I--LEKAREEAEEILREARKEAEELIRELRE 593
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 165-360 4.04e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 165 KEELFKTVLRQQEQLHSLEAHGDTLETDLRlwehgrasSQEDEILYLEHLVRRNDTELGEEEFWQSELR-----LEKECE 239
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEkeiaeLRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 240 RERQERVRSLRA-----------------SLEEYTQRIYELSARTEALQKEIQwEMAERAKRGKEIPvpspTDLEDMAAK 302
Cdd:COG4942   101 AQKEELAELLRAlyrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALR----AELEAERAE 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024505059 303 MKRDLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKELRQcnLQQFIQQ 360
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE--LEALIAR 231
46 PHA02562
endonuclease subunit; Provisional
 241-350 4.89e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 241 ERQERVRSLRASLEEYTQRIYELS-ARTEALQKEIQWEMAERAKRGkeipvpsptdledmaakMKRDLEAKVKQGTQLEN 319
Cdd:PHA02562  296 EGPDRITKIKDKLKELQHSLEKLDtAIDELEEIMDEFNEQSKKLLE-----------------LKNKISTNKQSLITLVD 358

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024505059 320 NLASVEKALEEAERSLQAQNQELEELNKELR 350
Cdd:PHA02562  359 KAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
PTZ00121 PTZ00121
MAEBL; Provisional
 166-348 5.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHgdTLETDLRLWEHGRASSQEDeiLYLEHLVRRNDTELGEEEFWQSELRLEKECERERQER 245
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEA--RIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 VRSLRASLEEYTQRIYELSARTEALQKEIQ-WEMAERAKRGKEIPVPSPTDLEDMAAKMKRDLEAKVKQGTQLENNLASV 324
Cdd:PTZ00121  1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728

                          170       180
                   ....*....|....*....|....
gi 2024505059  325 EKALEEAERSLQAQNQELEELNKE 348
Cdd:PTZ00121  1729 KIKAEEAKKEAEEDKKKAEEAKKD 1752
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
174-380 5.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 174 RQQEQLHSLEAHGDTLETDLRLWEHGRASSQEDEILYLEHLVRRNDtELGEEEFWQSELRLEKECERERQERVRSLRA-- 251
Cdd:COG4717   302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEag 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 252 --SLEEYTQRIYELSARTEALQK--EIQWEMAERAK-RGKEIPVPSPTDLEDMAAKMKRDLEAKVKQGTQLENNLASVEK 326
Cdd:COG4717   381 veDEEELRAALEQAEEYQELKEEleELEEQLEELLGeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024505059 327 ALEEAERS--LQAQNQELEELNKELRQCNLQQFIQQTGATVtVGQARS--EEDAQPEL 380
Cdd:COG4717   461 ELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALEL-LEEAREeyREERLPPV 517
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-335 5.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  166 EELFKTVLRQQEQLHSLEAHGDTLETDLRLWEH-GRASSQEDEILYLEHLVRRNDTELGEEEFWQSELR-LEKEcERERQ 243
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAaLEEQ-LEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  244 ERVRSLRASLEEYTQRIYELSARTEALQKEIQWEMAERAKRGKEIPVPSPTDLEDM-AAKMKRDLEAKVKQgtQLENNLA 322
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRE--NLEERID 776

                          170
                   ....*....|...
gi 2024505059  323 SVEKALEEAERSL 335
Cdd:COG4913    777 ALRARLNRAEEEL 789
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
243-385 6.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  243 QERVRSLRASLEEYTQRIYELSARTEALQKEIQwEMAERAKRGKEIPVPSPTDLE-DMAAKMKRDLEAKVKQGTQLENNL 321
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDL 687

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024505059  322 ASVEKALEEAERSLQAQNQELEELNKELRQCNLqqfiQQTGATVTVGQARSEEDAQPELSPREL 385
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGRLEK----ELEQAEEELDELQDRLEAAEDLARLEL 747
mukB PRK04863
chromosome partition protein MukB;
175-346 7.40e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  175 QQEQLHSLEAHGDTLETDLRLWE---------HGRASSQEDEILYLEHLVRRNDTELgeeefwqSELRLEKECERERQEr 245
Cdd:PRK04863   511 LAEQLQQLRMRLSELEQRLRQQQraerllaefCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERRM- 582

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059  246 vrSLRASLEEYTQRIYELSARtealqkEIQWEMA-ERAKRGKEIPVPSPTDLEDMAAKMKRDLEaKVKQGTQLENNLASV 324
Cdd:PRK04863   583 --ALRQQLEQLQARIQRLAAR------APAWLAAqDALARLREQSGEEFEDSQDVTEYMQQLLE-RERELTVERDELAAR 653

                          170       180
                   ....*....|....*....|...
gi 2024505059  325 EKALE-EAERSLQAQNQELEELN 346
Cdd:PRK04863   654 KQALDeEIERLSQPGGSEDPRLN 676
MlaD COG1463
Periplasmic subunit MlaD of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 279-366 8.00e-03

Periplasmic subunit MlaD of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441072 [Multi-domain]  Cd Length: 260  Bit Score: 38.15  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 279 AERAKRGKEIPVPSPTDLEDMAAKMKR-----DLEAKVKQGTQLENNLASVEKALEEAERSLQAQNQELEELNKELRQC- 352
Cdd:COG1463   118 GPPLADGDVIPLESPVDLEDLLSQLSPllealDPGALLDNLNTLTDTLADAAAQLDALLDNLNTLSDTLAERRDDLRALl 197

                          90
                  ....*....|....*
gi 2024505059 353 -NLQQFIQQTGATVT 366
Cdd:COG1463   198 aSLNALSAQLDGLLA 212
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
207-351 8.20e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024505059 207 EILYLEHLVRRNDTELGEEEFWQSELRLEKECERERQERVRSLRASLEEYTQRIYELSARTEALQKEIQwEMAERAKRGK 286
Cdd:PRK03918  208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELK 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024505059 287 EIPvPSPTDLEDMAAKMKRDLEAKV---KQGTQLENNLASVEKALEEAERslqaQNQELEELNKELRQ 351
Cdd:PRK03918  287 ELK-EKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKE 349
 
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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