NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1719041701|ref|WP_145393562|]
View 

DUF1640 domain-containing protein [Pantoea sp. SJZ147]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-257 5.55e-15

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: 72.65  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 102 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKT--- 178
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnke 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 179 ------DVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG1579    91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREE 167


                  ....*
gi 1719041701 253 LKTDV 257
Cdd:COG1579   168 LAAKI 172
CCDC90-like super family cl06708
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 6-152 1.87e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


The actual alignment was detected with superfamily member pfam07798:

Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 44.04  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   6 MNTHKAFKRLQRAGINDRQAEAMVAIFSELQQDNA-------LSRADVMRAFQFQNQHIMMLSTQLKKAE----SDLRTE 74
Cdd:pfam07798   1 FDTHAFVRQLEEAGFTEEQAEAIMKALRDLLNDSLenvskdlVTKEDLENETYLQKADLAELRSELQILEksefAALRSE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1719041701  75 TGDVAKGVEVLQTDndvFRTDIVELKTDVA-ELKTDVAELKTDVAELKTDVAELKTdvaELKTDVAKLKTDVDELKTDV 152
Cdd:pfam07798  81 NEKLRRELEKLKQR---LREEITKLKADVRlDLNLEKGRIREELKAQELKIQETNN---KIDTEIANLRTQIESVKWDV 153
 
Name Accession Description Interval E-value
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-257 5.55e-15

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: 72.65  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 102 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKT--- 178
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnke 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 179 ------DVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG1579    91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREE 167


                  ....*
gi 1719041701 253 LKTDV 257
Cdd:COG1579   168 LAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-264 7.87e-15

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: 74.71  E-value: 7.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   60 LSTQLKKAES--DLRTETGDVAKGVEVLqtDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 137
Cdd:TIGR02168  205 LERQAEKAERykELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  138 VAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAE 217
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1719041701  218 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
60-263 1.39e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRTETGDVAKGVEVLQTDNDVF------RTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 133
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEADEVLeeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 134 LKTD---------------------VAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKK 192
Cdd:PRK02224  291 LEEErddllaeaglddadaeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1719041701 193 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 112-254 4.14e-09

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 56.56  E-value: 4.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  112 ELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKtdvaELKKDVAELKTdvaelkTDVAILKTDVAELK 191
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDP------TELDRAKEKLKKLL 217

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1719041701  192 KDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK----TDVAELKTDVAELK 254
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQ 284
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 88-254 5.41e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 50.66  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  88 DNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVA 167
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 168 ELKTDVAELKTDVAILKTDVaelKKDVAELKTDVAELKTDVAELKTDVAELKTdvaeLKTDVAELKTDVAELKTDVAELK 247
Cdd:pfam07888 140 TLTQRVLERETELERMKERA---KKAGAQRKEEEAERKQLQAKLQQTEEELRS----LSKEFQELRNSLAQRDTQVLQLQ 212


                  ....*..
gi 1719041701 248 TDVAELK 254
Cdd:pfam07888 213 DTITTLT 219
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 6-152 1.87e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 44.04  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   6 MNTHKAFKRLQRAGINDRQAEAMVAIFSELQQDNA-------LSRADVMRAFQFQNQHIMMLSTQLKKAE----SDLRTE 74
Cdd:pfam07798   1 FDTHAFVRQLEEAGFTEEQAEAIMKALRDLLNDSLenvskdlVTKEDLENETYLQKADLAELRSELQILEksefAALRSE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1719041701  75 TGDVAKGVEVLQTDndvFRTDIVELKTDVA-ELKTDVAELKTDVAELKTDVAELKTdvaELKTDVAKLKTDVDELKTDV 152
Cdd:pfam07798  81 NEKLRRELEKLKQR---LREEITKLKADVRlDLNLEKGRIREELKAQELKIQETNN---KIDTEIANLRTQIESVKWDV 153
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 106-260 2.28e-05

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 44.71  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 106 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAelkTDVAELKKDVAELKTDVAELKTdvaiLKT 185
Cdd:cd21116    82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLD---DDSRNLQTDATKAQAQVAVLNA----LKN 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1719041701 186 DVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVaelktDVAELKTDVAELKTDVAELKTDVAELKTDVGNL 260
Cdd:cd21116   155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDL-----EDAESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 87-234 2.78e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 38.82  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  87 TDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDV-AELKTDVAKLKTDVDE--LKTDVAELKTDVAELK 163
Cdd:NF033928  116 PLSSDDKEIVKELKEILEDLKNDIKDYQQKADDVKKELDDFENDLrEELLPQLKLKKKLYDDnlGSDSIEELREKIDQLE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 164 KDVAELKTDVAELKTDV---------------AILKTDVAELKKDVAELKtdvAELKTDVAELKTDVAeLKTDVAELKTD 228
Cdd:NF033928  196 KEIEQLNKEYDDYVKLSftglaggpiglaitgGIFGSKAEKIRKEKNALI---QEIDELQEQLKKKNA-LLGSLERLQTS 271


                  ....*.
gi 1719041701 229 VAELKT 234
Cdd:NF033928  272 LDDILT 277
 
Name Accession Description Interval E-value
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 102-257 5.55e-15

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: 72.65  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 102 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKT--- 178
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnke 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 179 ------DVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG1579    91 yealqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREE 167


                  ....*
gi 1719041701 253 LKTDV 257
Cdd:COG1579   168 LAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-264 7.87e-15

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: 74.71  E-value: 7.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   60 LSTQLKKAES--DLRTETGDVAKGVEVLqtDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 137
Cdd:TIGR02168  205 LERQAEKAERykELKAELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  138 VAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAE 217
Cdd:TIGR02168  283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1719041701  218 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 94-252 1.77e-14

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: 71.11  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELK--KDVAELKT 171
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 172 DVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVAELKTDVAELKTDVA 251
Cdd:COG1579    97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIP 173


                  .
gi 1719041701 252 E 252
Cdd:COG1579   174 P 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 105-271 5.65e-14

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: 72.01  E-value: 5.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  105 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILK 184
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  185 TDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833


                   ....*..
gi 1719041701  265 CWVKRLM 271
Cdd:TIGR02168  834 AATERRL 840
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-261 8.57e-14

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: 71.63  E-value: 8.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   96 IVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAE 175
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  176 LKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831


                   ....*.
gi 1719041701  256 DVGNLK 261
Cdd:TIGR02168  832 RIAATE 837
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-253 4.77e-13

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: 69.32  E-value: 4.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   60 LSTQLKKAESDL---RTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 136
Cdd:TIGR02168  258 LTAELQELEEKLeelRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  137 DVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVA 216
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1719041701  217 ELKTDVAEL-----KTDVAELKTDVAELKTDVAELKTDVAEL 253
Cdd:TIGR02168  418 RLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERL 459
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 90-245 6.78e-13

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: 66.49  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKT--DVAELKKDVA 167
Cdd:COG1579    20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1719041701 168 ELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVAELKTDVAELKTDVAE 245
Cdd:COG1579   100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPP 174
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 109-261 1.40e-12

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: 65.72  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 109 DVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKT--D 186
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkE 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1719041701 187 VAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAELKTDVGNLK 261
Cdd:COG1579    91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELE 162
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 93-263 2.75e-12

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: 66.33  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  93 RTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAEL--- 169
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlra 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 ---------------KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 234
Cdd:COG4942   113 lyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192

                         170       180
                  ....*....|....*....|....*....
gi 1719041701 235 DVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:COG4942   193 LKAERQKLLARLEKELAELAAELAELQQE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-260 3.03e-12

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: 67.00  E-value: 3.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   50 FQFQNQHIMMLSTQLKKAESDLRTETgdvakgvevlqtdndvfrTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKT 129
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELT------------------AELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  130 DVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVA 209
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1719041701  210 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNL 260
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 94-263 5.84e-12

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 65.24  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAEL---- 169
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaral 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 ---------------KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 234
Cdd:COG3883    96 yrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                         170       180
                  ....*....|....*....|....*....
gi 1719041701 235 DVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
94-262 9.91e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 65.32  E-value: 9.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAE-----LKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAE 168
Cdd:COG4913    255 EPIRELAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  169 LKTD-VAELKTDVAILKTDVAELKKDVAELKTDVAELK----TDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 243
Cdd:COG4913    335 NGGDrLEQLEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414

                          170
                   ....*....|....*....
gi 1719041701  244 AELKTDVAELKTDVGNLKN 262
Cdd:COG4913    415 RDLRRELRELEAEIASLER 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-253 1.44e-11

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: 64.69  E-value: 1.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701    7 NTHKAFKRLQRAGINDRQAEAMVAIFSELQQDNALSRADVMRAFQFQNQHIMMLSTQLKKAESDL---RTETGDVAKGVE 83
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaEAEIEELEAQIE 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   84 VLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDV-------AELKTDVAKLKTDVDELKTDVAELK 156
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedleeqiEELSEDIESLAAEIEELEELIEELE 872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  157 TDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAEL---- 232
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEyslt 952

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1719041701  233 -----------KTDVAELKTDVAELKTDVAEL 253
Cdd:TIGR02168  953 leeaealenkiEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-261 2.41e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  62 TQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKL 141
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 142 KTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTD 221
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1719041701 222 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-263 2.41e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  98 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELK 177
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 178 TDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 257
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395


                  ....*.
gi 1719041701 258 GNLKND 263
Cdd:COG1196   396 AELAAQ 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-262 3.06e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAEL 169
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 249
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170
                  ....*....|...
gi 1719041701 250 VAELKTDVGNLKN 262
Cdd:COG1196   395 AAELAAQLEELEE 407
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 70-256 3.32e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  70 DLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELK 149
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 150 TDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 229
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                         170       180
                  ....*....|....*....|....*..
gi 1719041701 230 AELKTDVAELKTDVAELKTDVAELKTD 256
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEE 422
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-264 3.48e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRtetgdvAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVA 139
Cdd:COG1196   218 LKEELKELEAELL------LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 140 KLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELK 219
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1719041701 220 TDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:COG1196   372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 60-252 9.40e-11

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: 61.70  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRTETGDVAKGVEVLQTDNDvfrtDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVA 139
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 140 KL------------------KTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDV 201
Cdd:COG4942   108 ELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1719041701 202 AELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG4942   188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-240 1.35e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   93 RTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTD-VDELKTDVAELKTDVAELKKDVAELKT 171
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEA 366

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1719041701  172 DVAELKTDVAilkTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK 240
Cdd:COG4913    367 LLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 116-263 2.15e-10

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: 59.55  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 116 DVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELK--KD 193
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKE 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 194 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELktdVAELKTDVGNLKND 263
Cdd:COG1579    91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAE 157
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
60-263 1.39e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 58.51  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRTETGDVAKGVEVLQTDNDVF------RTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 133
Cdd:PRK02224  211 LESELAELDEEIERYEEQREQARETRDEADEVLeeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 134 LKTD---------------------VAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKK 192
Cdd:PRK02224  291 LEEErddllaeaglddadaeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1719041701 193 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PRK02224  371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 63-253 3.16e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 3.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   63 QLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVA------------ELKTDVAELKTDVAELKTDVAELKTD 130
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  131 VAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAE 210
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1719041701  211 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAEL 253
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
25-250 3.22e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.33  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  25 AEAMVAIFseLQQDNALSRADVMRAFQFQNQHIMMLSTQLKKAESDL---RTETGDVAKGVEVLQTDNDV--FRTDIVEL 99
Cdd:COG3206   154 ANALAEAY--LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLSEEAKLLLQQLseLESQLAEA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 100 KTDVAELKTDVAELKTDVAELKTDVAELKTD--VAELKTDVAKLKTDVDELKT-------DVAELKTDVAELKKDV-AEL 169
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEA 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELktdvAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 249
Cdd:COG3206   312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYESLLQRLEEARLAEALTVGN 387


                  .
gi 1719041701 250 V 250
Cdd:COG3206   388 V 388
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 112-254 4.14e-09

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 56.56  E-value: 4.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  112 ELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKtdvaELKKDVAELKTdvaelkTDVAILKTDVAELK 191
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDP------TELDRAKEKLKKLL 217

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1719041701  192 KDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK----TDVAELKTDVAELK 254
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQ 284
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
103-264 7.77e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 7.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  103 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLK--TDVDELKTDVAELKTDVAELKKDVAELKT---DVAELK 177
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  178 TDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAEL-----KTDVAELKTDVAELKTD------VAEL 246
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALGDaverelRENL 771

                          170
                   ....*....|....*...
gi 1719041701  247 KTDVAELKTDVGNLKNDM 264
Cdd:COG4913    772 EERIDALRARLNRAEEEL 789
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 109-264 1.09e-08

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: 55.54  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 109 DVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVA 188
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 189 ELKKDVAEL------------------KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 250
Cdd:COG4942   101 AQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170
                  ....*....|....
gi 1719041701 251 AELKTDVGNLKNDM 264
Cdd:COG4942   181 AELEEERAALEALK 194
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-238 1.54e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 110 VAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAE 189
Cdd:PRK02224  316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1719041701 190 LKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 238
Cdd:PRK02224  396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
104-264 1.83e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.43  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 104 AELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAIL 183
Cdd:PRK02224  233 RETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 184 KTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PRK02224  313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392


                  .
gi 1719041701 264 M 264
Cdd:PRK02224  393 I 393
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 54-266 3.19e-08

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: 54.26  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  54 NQHIMMLSTQLKKAESD---LRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTD 130
Cdd:TIGR04523 341 NEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 131 VAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAE 210
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1719041701 211 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDMCW 266
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
69-245 4.51e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  69 SDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVA--------------ELKTDVAELKTDVAEL 134
Cdd:PRK02224  254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeavearreELEDRDEELRDRLEEC 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 135 KTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTD 214
Cdd:PRK02224  334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1719041701 215 VAELKTDVAELKTDVAELKTDVAELKTDVAE 245
Cdd:PRK02224  414 LEELREERDELREREAELEATLRTARERVEE 444
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-264 6.65e-08

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: 53.23  E-value: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 116 DVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVA 195
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 196 ELKTDVAEL---------------------------------------KTDVAELKTDVAELKTDVAELKTDVAELKTDV 236
Cdd:COG4942   101 AQKEELAELlralyrlgrqpplalllspedfldavrrlqylkylaparREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180
                  ....*....|....*....|....*...
gi 1719041701 237 AELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKEL 208
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
69-261 1.05e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.76  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  69 SDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKT--DVAELKTDVAELKTDVAELKTDVAKLKTDVD 146
Cdd:PRK03918  241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 147 ELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVaELKKDVAELKTDVAELKTDVAELKTDvaELKTDVAELK 226
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELE 397

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1719041701 227 TDVAELKTDVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 98-233 1.13e-07

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 51.94  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   98 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKtdvdELKTDVAELK-TDVAELKKDVAELKTDVAEL 176
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDpTELDRAKEKLKKLLQEIMIK 223

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1719041701  177 KTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELK----TDVAELKTDVAELK 233
Cdd:smart00787 224 VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQ 284
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
64-231 1.22e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.73  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  64 LKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKT 143
Cdd:PRK02224  277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 144 DVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVA 223
Cdd:PRK02224  357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436


                  ....*...
gi 1719041701 224 ELKTDVAE 231
Cdd:PRK02224  437 TARERVEE 444
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
59-256 1.46e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  59 MLSTQLKKAESDLRTETGdvaKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKtdvaELKTDVAELKTDVAELKTDV 138
Cdd:COG4717    46 MLLERLEKEADELFKPQG---RKPELNLKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREEL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 139 AKLKTDVD--ELKTDVAELKTDVAELKKDVAELKTDVAELKTdvaiLKTDVAELKKDVAELKTDVAELKTDV-AELKTDV 215
Cdd:COG4717   119 EKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLsLATEEEL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1719041701 216 AELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 256
Cdd:COG4717   195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
PTZ00121 PTZ00121
MAEBL; Provisional
 98-254 2.35e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   98 ELKTDVAELKTDVAEL-KTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAEL 176
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1719041701  177 KTDVAILKtdvAELKKDVAELKTDVAELKTDVAELKTDVAElKTDVAELKTDvAELKTDVAELKTDvAELKTDVAELK 254
Cdd:PTZ00121  1379 KADAAKKK---AEEKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKK-AEEKKKADEAKKK-AEEAKKADEAK 1450
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 94-226 2.53e-07

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 51.17  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvaKLKTDVDELK-TDVAELKTDVAELKKDVAELKTD 172
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKK 226

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1719041701  173 VAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELK----TDVAELKTDVAELK 226
Cdd:smart00787 227 LEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQ 284
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 146-263 3.42e-07

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 50.79  E-value: 3.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  146 DELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKkdvaELKTDVAELK-TDVAELKTDVAELKTDVAE 224
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDpTELDRAKEKLKKLLQEIMI 222

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1719041701  225 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 62-262 5.36e-07

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: 50.79  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  62 TQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKL 141
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 142 KTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTD 221
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1719041701 222 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKN 262
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 88-254 5.41e-07

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 50.66  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  88 DNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVA 167
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 168 ELKTDVAELKTDVAILKTDVaelKKDVAELKTDVAELKTDVAELKTDVAELKTdvaeLKTDVAELKTDVAELKTDVAELK 247
Cdd:pfam07888 140 TLTQRVLERETELERMKERA---KKAGAQRKEEEAERKQLQAKLQQTEEELRS----LSKEFQELRNSLAQRDTQVLQLQ 212


                  ....*..
gi 1719041701 248 TDVAELK 254
Cdd:pfam07888 213 DTITTLT 219
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
100-255 6.35e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 100 KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKT--DVAELKTDVAELKKDVAELKTDVAELK 177
Cdd:COG4717   336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELL 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 178 TDVAIL--KTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD--VAELKTDVAELKTDVAELKTDVAEL 253
Cdd:COG4717   416 GELEELleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAAL 495


                  ..
gi 1719041701 254 KT 255
Cdd:COG4717   496 KL 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
63-253 1.09e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   63 QLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIvelktDVAELKTDVAELKTDVAELKTDVAELktdvAELKTDVAKLK 142
Cdd:COG4913    628 EAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDDL----AALEEQLEELE 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  143 TDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAIL-----KTDVAELKKDVAELKTDVAElKTDVAELKTDVAE 217
Cdd:COG4913    699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALGDAVE-RELRENLEERIDA 777

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1719041701  218 LKTDVAELKTDVAELKTD-VAELKTDVAELKTDVAEL 253
Cdd:COG4913    778 LRARLNRAEEELERAMRAfNREWPAETADLDADLESL 814
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 84-209 1.11e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 49.34  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  84 VLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELK 163
Cdd:TIGR04320 230 FVNFNDSYIADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQ 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1719041701 164 KDVAEL-KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVA 209
Cdd:TIGR04320 310 AQALQTaQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
PTZ00121 PTZ00121
MAEBL; Provisional
 105-257 1.21e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  105 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDvAELKTDVAILK 184
Cdd:PTZ00121  1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEELK 1708

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1719041701  185 TDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAElKTDVAELKTDVAELKTDVAELKTDV 257
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAV 1780
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 102-262 1.78e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.74  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 102 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVA 181
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 182 ILKTDVAELKKDVAELKTDVaelKTDVAELKTDVAELKTDVAELKTDVAELK---TDVAELKTDVAELKTDVAELKTDVG 258
Cdd:pfam07888 140 TLTQRVLERETELERMKERA---KKAGAQRKEEEAERKQLQAKLQQTEEELRslsKEFQELRNSLAQRDTQVLQLQDTIT 216


                  ....
gi 1719041701 259 NLKN 262
Cdd:pfam07888 217 TLTQ 220
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 114-230 1.78e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 48.57  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 114 KTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAilktdvAELKKD 193
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQAL------QTAQNN 319

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1719041701 194 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVA 230
Cdd:TIGR04320 320 LATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
63-233 2.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  63 QLKKAESDLRtetgDVAKGVEVLQTDNDVFRTdIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLK 142
Cdd:PRK03918  270 ELKKEIEELE----EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 143 TDVDELKTDVAELKTDVaELKKDVAELKTDVAELKTDVAILKTDvaELKKDVAELKTDVAELKTDVAELKTDVAELKTDV 222
Cdd:PRK03918  345 KKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEI 421

                         170
                  ....*....|.
gi 1719041701 223 AELKTDVAELK 233
Cdd:PRK03918  422 KELKKAIEELK 432
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 88-262 2.02e-06

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: 48.86  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  88 DNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVA 167
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 168 ELKTDVAELKTDVA-----ILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 242
Cdd:TIGR04523 292 QLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371

                         170       180
                  ....*....|....*....|
gi 1719041701 243 VAELKTDVAELKTDVGNLKN 262
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLES 391
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 98-262 2.40e-06

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: 48.48  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  98 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELK 177
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 178 TDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 257
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470


                  ....*
gi 1719041701 258 GNLKN 262
Cdd:TIGR04523 471 KVLSR 475
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 135-244 2.42e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 48.18  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 135 KTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAEL-KTDVAELKT 213
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQA 325

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1719041701 214 DVAELKTDVAELKTDVAELKTDVAELKTDVA 244
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLNADLAKKQAALD 356
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
64-260 2.53e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  64 LKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLK- 142
Cdd:PRK02224  319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRe 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 143 ------TDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVA 216
Cdd:PRK02224  399 rfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVE 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1719041701 217 ELKTDVAELKTDVAELKTDVAELKtDVAELKTDVAELKTDVGNL 260
Cdd:PRK02224  479 ELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDL 521
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 76-255 2.71e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  76 GDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAEL 155
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 156 KTDVAELKKDVAELKTDVAELKTDV----AILKTDVAELKKDVAELKTDVAELK---TDVAELKTDVAELKTDVAELKTD 228
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAkkagAQRKEEEAERKQLQAKLQQTEEELRslsKEFQELRNSLAQRDTQVLQLQDT 214

                         170       180
                  ....*....|....*....|....*..
gi 1719041701 229 VAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:pfam07888 215 ITTLTQKLTTAHRKEAENEALLEELRS 241
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
90-260 3.28e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAE-----LKTDVAELKTDVAELKTDVAELKT--DVAELKTDVAKLKTDVDELKTDVAELKTDVAEL 162
Cdd:COG3206   159 EAYLEQNLELRREEARkalefLEEQLPELRKELEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 163 KKDVAELKTDVAELKTDVAILKTD--VAELKKDVAELKTDVAELKT-------DVAELKTDVAELKTDV-AELKTDVAEL 232
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILASL 318

                         170       180
                  ....*....|....*....|....*...
gi 1719041701 233 KTDVAELKTDVAELKTDVAELKTDVGNL 260
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAEL 346
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-262 3.46e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  62 TQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELK-----TDVAElKT 136
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG-SP 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 137 DVAKLKTD---VDELKTDVAELKTDVAELKKDVAELKtDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKT 213
Cdd:PRK02224  466 HVETIEEDrerVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1719041701 214 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKN 262
Cdd:PRK02224  545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 63-219 3.65e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  63 QLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAEL--------------- 127
Cdd:COG3883    27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyld 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 128 ----KTDVAELKTDVAKLKT-------DVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAE 196
Cdd:COG3883   107 vllgSESFSDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186

                         170       180
                  ....*....|....*....|...
gi 1719041701 197 LKTDVAELKTDVAELKTDVAELK 219
Cdd:COG3883   187 LSAEEAAAEAQLAELEAELAAAE 209
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 53-264 4.14e-06

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: 48.09  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  53 QNQHIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFR---TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKT 129
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKeleEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 130 DVAELKTDVAK--LKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTD 207
Cdd:TIGR04523 546 ELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1719041701 208 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
96-252 4.35e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  96 IVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAE 175
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1719041701 176 LKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 142-251 4.39e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 47.41  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 142 KTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAEL-KTDVAELKT 220
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQA 325

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1719041701 221 DVAELKTDVAELKTDVAELKTDVAELKTDVA 251
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLNADLAKKQAALD 356
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 111-260 4.42e-06

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: 48.14  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  111 AELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAEL 190
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1719041701  191 KKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVA-----ELKTDVAELKTDVAELKTDVAELKTDVGNL 260
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
110-263 4.98e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 110 VAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAE 189
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1719041701 190 LKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 156-261 7.62e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 46.64  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 156 KTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAEL-KTDVAELKT 234
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQA 325

                          90       100
                  ....*....|....*....|....*..
gi 1719041701 235 DVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLNADLAKKQ 352
PTZ00121 PTZ00121
MAEBL; Provisional
 63-261 7.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 7.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   63 QLKKAESD--LRTETGDVAKGVEVLQTDnDVFRTDIVELKTDVAELKTDvAELKTDVAELKTDvAELKTDVAELKTDVAK 140
Cdd:PTZ00121  1568 EAKKAEEDknMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKA-EEEKKKVEQLKKKEAE 1644

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  141 LKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDvailktdvAELKKDVAELKTDVAELKTDVAELKTDVAELKT 220
Cdd:PTZ00121  1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1719041701  221 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:PTZ00121  1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
63-261 8.24e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  63 QLKKAESDLRtetgdvAKGVEVLQTDNDVFRtdivELKTDVAELKTDVAELKTDV---AELKTDVAELKTDVAELKTDVA 139
Cdd:PRK03918  504 QLKELEEKLK------KYNLEELEKKAEEYE----KLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELA 573

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 140 KLKTDVDELK-TDVAELKTDVAELK---KDVAELKTDVAEL---KTDVAILKTDVAELKKDVAELKTDVAELKTDVAELK 212
Cdd:PRK03918  574 ELLKELEELGfESVEELEERLKELEpfyNEYLELKDAEKELereEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1719041701 213 T-----DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:PRK03918  654 KkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-260 8.93e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 103 VAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELK--KDVAELKTDVAELKTDV 180
Cdd:PRK03918  226 LEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEY 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 181 AILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVaELKTDVAELKTDVAELKTDVGNL 260
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGL 384
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 149-255 9.64e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 46.26  E-value: 9.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 149 KTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAEL-KTDVAELKT 227
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQA 325

                          90       100
                  ....*....|....*....|....*...
gi 1719041701 228 DVAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLNADLAKKQA 353
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-253 1.09e-05

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: 46.30  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 164 KDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 243
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90
                  ....*....|
gi 1719041701 244 AELKTDVAEL 253
Cdd:COG4942   100 EAQKEELAEL 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-254 1.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  32 FSELQQDNALSRADVMRAFQfQNQHIMMLSTQLKKAESDLRTEtgdvakgVEVLQTDNDVFRTDIVELKTDVAELKtdvA 111
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAE---E 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 112 ELKTDVAELKTDVAELKTDVAELKTDVAKLktdvDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELK 191
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEEL----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1719041701 192 KDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK 254
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
103-213 1.76e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 103 VAELKTDVAELKTDVAELKTDVAElkTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKT---- 178
Cdd:COG2433   382 LEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeerr 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1719041701 179 ------DVAILKTDVAELKKDVAELKTDVAELKTDVAELKT 213
Cdd:COG2433   460 eirkdrEISRLDREIERLERELEEERERIEELKRKLERLKE 500
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-263 1.84e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  96 IVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKtdvaKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAE 175
Cdd:PRK03918  195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 176 LKTDVAILKTDVAELK--KDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAEL 253
Cdd:PRK03918  271 LKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350

                         170
                  ....*....|
gi 1719041701 254 KTDVGNLKND 263
Cdd:PRK03918  351 EKRLEELEER 360
CCDC90-like pfam07798
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ...
 6-152 1.87e-05

Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.


Pssm-ID: 462268 [Multi-domain]  Cd Length: 175  Bit Score: 44.04  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   6 MNTHKAFKRLQRAGINDRQAEAMVAIFSELQQDNA-------LSRADVMRAFQFQNQHIMMLSTQLKKAE----SDLRTE 74
Cdd:pfam07798   1 FDTHAFVRQLEEAGFTEEQAEAIMKALRDLLNDSLenvskdlVTKEDLENETYLQKADLAELRSELQILEksefAALRSE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1719041701  75 TGDVAKGVEVLQTDndvFRTDIVELKTDVA-ELKTDVAELKTDVAELKTDVAELKTdvaELKTDVAKLKTDVDELKTDV 152
Cdd:pfam07798  81 NEKLRRELEKLKQR---LREEITKLKADVRlDLNLEKGRIREELKAQELKIQETNN---KIDTEIANLRTQIESVKWDV 153
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 106-260 2.28e-05

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 44.71  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 106 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAelkTDVAELKKDVAELKTDVAELKTdvaiLKT 185
Cdd:cd21116    82 ADNLIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLD---DDSRNLQTDATKAQAQVAVLNA----LKN 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1719041701 186 DVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVaelktDVAELKTDVAELKTDVAELKTDVAELKTDVGNL 260
Cdd:cd21116   155 QLNSLAEQIDAAIDALEKLSNDWQTLDSDIKELITDL-----EDAESSIDAAFLQADLKAAKADWNQLYEQAKSL 224
PTZ00121 PTZ00121
MAEBL; Provisional
 63-254 2.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   63 QLKKAESDLRTEtgDVAKGVEVLQTDNDVFRTDivELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTdvAKLK 142
Cdd:PTZ00121  1216 EARKAEDAKKAE--AVKKAEEAKKDAEEAKKAE--EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--AEEK 1289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  143 TDVDELKTdvAELKTDVAELKKDVAEL-KTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTD 221
Cdd:PTZ00121  1290 KKADEAKK--AEEKKKADEAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1719041701  222 VAELKTDVAELKTDVAELKtdvAELKTDVAELK 254
Cdd:PTZ00121  1368 AAEKKKEEAKKKADAAKKK---AEEKKKADEAK 1397
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 94-259 2.74e-05

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: 44.67  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELktdVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAE-LKTDVAEL-KKDVAELKT 171
Cdd:cd22656   110 EELEEAKKTIKAL---LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDlLTDEGGAIaRKEIKDLQK 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 172 DVAELKTDVAI-LKTDVAELKKDVAELKtdvAELKTDVAeLKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 250
Cdd:cd22656   187 ELEKLNEEYAAkLKAKIDELKALIADDE---AKLAAALR-LIADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDL 262


                  ....*....
gi 1719041701 251 AELKTDVGN 259
Cdd:cd22656   263 DSLKDLLED 271
46 PHA02562
endonuclease subunit; Provisional
 53-263 3.67e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.01  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  53 QNQHIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVA 132
Cdd:PHA02562  179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALN 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 133 ELKTDVAKLKTDVDELKTD-----------------------VAELKTDVAELKKDVAELKTDVAELK---TDVAILKTD 186
Cdd:PHA02562  259 KLNTAAAKIKSKIEQFQKVikmyekggvcptctqqisegpdrITKIKDKLKELQHSLEKLDTAIDELEeimDEFNEQSKK 338

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1719041701 187 VAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PHA02562  339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKDS 415
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 161-264 3.94e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 44.24  E-value: 3.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  161 ELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKtdvaELKTDVAELK-TDVAELKTDVAELKTDVAEL 239
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK----QLEDELEDCDpTELDRAKEKLKKLLQEIMIK 223

                           90       100
                   ....*....|....*....|....*
gi 1719041701  240 KTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:smart00787 224 VKKLEELEEELQELESKIEDLTNKK 248
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-256 4.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 111 AELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVA-- 188
Cdd:COG4717   319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyq 398

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 189 ELKKDVAELKTDVAELKTDVAEL--KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 256
Cdd:COG4717   399 ELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 95-264 5.02e-05

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: 43.90  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  95 DIVELKTDVAELKTDVAELKTDV-AELKTDVAELKTDVAELKTDVAK--LKTDVDELKTDVAELKTDVAELKKDVAELKT 171
Cdd:cd22656    70 SIVSLAGDIYNYAQNAGGTIDSYyAEILELIDDLADATDDEELEEAKktIKALLDDLLKEAKKYQDKAAKVVDKLTDFEN 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 172 DVAELKTDVAILKTDVAEL--KKDVAELKTDVAELKTDVAELKTDVA-ELKTDVAELKtdvAELKTDVAELKTDVAeLKT 248
Cdd:cd22656   150 QTEKDQTALETLEKALKDLltDEGGAIARKEIKDLQKELEKLNEEYAaKLKAKIDELK---ALIADDEAKLAAALR-LIA 225

                         170
                  ....*....|....*.
gi 1719041701 249 DVAELKTDVGNLKNDM 264
Cdd:cd22656   226 DLTAADTDLDNLLALI 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 94-263 5.13e-05

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: 44.63  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDV 173
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 174 AELKTDVAILKTDVAELKKDVA-----ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 248
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363

                         170
                  ....*....|....*
gi 1719041701 249 DVAELKTDVGNLKND 263
Cdd:TIGR04523 364 ELEEKQNEIEKLKKE 378
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-263 5.24e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 104 AELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAIL 183
Cdd:COG4717   298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 184 KTDV---------AELKKDVAELKTDVAELKTDVAELKTDVAEL--KTDVAELKTDVAELKTDVAELKTDVAELKTDVAE 252
Cdd:COG4717   378 EAGVedeeelraaLEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELREELAE 457

                         170
                  ....*....|.
gi 1719041701 253 LKTDVGNLKND 263
Cdd:COG4717   458 LEAELEQLEED 468
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 98-195 6.24e-05

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: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  98 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELK 177
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                          90
                  ....*....|....*...
gi 1719041701 178 TDVAILKTDVAELKKDVA 195
Cdd:COG4942   227 ALIARLEAEAAAAAERTP 244
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
90-264 7.00e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAEL 169
Cdd:COG1340    18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 KTDVAELKTDvailKTDVAELKKDVAEL----------KTDVAELKTDVAELKTDVAELKtDVAELKTDVAELKTDVAEL 239
Cdd:COG1340    98 RKELAELNKA----GGSIDKLRKEIERLewrqqtevlsPEEEKELVEKIKELEKELEKAK-KALEKNEKLKELRAELKEL 172

                         170       180
                  ....*....|....*....|....*
gi 1719041701 240 KTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:COG1340   173 RKEAEEIHKKIKELAEEAQELHEEM 197
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
105-257 8.12e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 105 ELKTDVAELKTDVAELKTDVAELKTDVAELKtdvaKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILK 184
Cdd:PRK03918  197 EKEKELEEVLREINEISSELPELREELEKLE----KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 185 TDVAELKKDVAELK----------------TDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 248
Cdd:PRK03918  273 KEIEELEEKVKELKelkekaeeyiklsefyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352


                  ....*....
gi 1719041701 249 DVAELKTDV 257
Cdd:PRK03918  353 RLEELEERH 361
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
78-257 8.26e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  78 VAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKT 157
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 158 DVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTdvAELKTDVA 237
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALD 186

                         170       180
                  ....*....|....*....|
gi 1719041701 238 ELKTDVAELKTDVAELKTDV 257
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAE 206
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 17-284 1.50e-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: 43.18  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   17 RAGINDRQAEA--MVAIFSELQQDNALSRADVMRAFQFQNQ---HIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNdv 91
Cdd:pfam15921  418 RRELDDRNMEVqrLEALLKAMKSECQGQMERQMAAIQGKNEsleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE-- 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   92 fRTdIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLK---TDVDELKTDVAELKTDVAELKKDVAE 168
Cdd:pfam15921  496 -RT-VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIEN 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  169 LKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELK-------TDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 241
Cdd:pfam15921  574 MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1719041701  242 DVAELKTDVAELKTDVGNLKNDMCWVKRLM------MVMTTTLLMATMK 284
Cdd:pfam15921  654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnkseeMETTTNKLKMQLK 702
PTZ00121 PTZ00121
MAEBL; Provisional
 100-263 1.52e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  100 KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDvAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTD 179
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  180 VAILKTDVAELKKDVAELKTDVAELKTDvAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGN 259
Cdd:PTZ00121  1670 AEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                   ....
gi 1719041701  260 LKND 263
Cdd:PTZ00121  1749 AKKD 1752
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 82-188 1.63e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.41  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  82 VEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDEL-KTDVAELKTDVA 160
Cdd:TIGR04320 249 IPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALA 328

                          90       100
                  ....*....|....*....|....*...
gi 1719041701 161 ELKKDVAELKTDVAELKTDVAILKTDVA 188
Cdd:TIGR04320 329 NAEARLAKAKEALANLNADLAKKQAALD 356
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
158-255 1.67e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 158 DVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTdvaELKTDVAELKtDVAELKTDVAELKTDVA 237
Cdd:COG2433   407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARS---EERREIRKDR-EISRLDREIERLERELE 482

                          90
                  ....*....|....*...
gi 1719041701 238 ELKTDVAELKTDVAELKT 255
Cdd:COG2433   483 EERERIEELKRKLERLKE 500
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
95-255 1.79e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  95 DIVELKTDVAELKTDVAELKTDVAELKTDVaELKTDVAELKTDVAKLKT-----DVDELKTDVAELKTDVAELKKDVAEL 169
Cdd:PRK03918  332 ELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKI 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 170 KTDVAELKTDVAILKTDVAELKKdvAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 249
Cdd:PRK03918  411 TARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488


                  ....*.
gi 1719041701 250 VAELKT 255
Cdd:PRK03918  489 LKKESE 494
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 101-185 1.80e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  101 TDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELK----KDVAELKTDVA-- 174
Cdd:smart00787 204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKll 283

                           90
                   ....*....|.
gi 1719041701  175 ELKTDVAILKT 185
Cdd:smart00787 284 QSLTGWKITKL 294
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 89-255 1.85e-04

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 42.37  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  89 NDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELkTDVAELKTDVAKLKTDVDELKTDVAELKTDVAE-LKKDVA 167
Cdd:pfam04108 118 RDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESL-SSPSESISLIPTLLKELESLEEEMASLLESLTNhYDQCVT 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 168 ELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT---DVAELKTDVAELKTDVA 244
Cdd:pfam04108 197 AVKLTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSalqLIAEIQSRLPEYLAALK 276

                         170
                  ....*....|.
gi 1719041701 245 ELKTDVAELKT 255
Cdd:pfam04108 277 EFEERWEEEKE 287
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 62-255 2.23e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   62 TQLKKAESDLRT---ETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAE----LKTDVAELKTdVAEL 134
Cdd:TIGR00606  709 DKLKSTESELKKkekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetlLGTIMPEEES-AKVC 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  135 KTDVA---KLKTDVDELKTDVAEL--KTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVA 209
Cdd:TIGR00606  788 LTDVTimeRFQMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN 867

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1719041701  210 ELKTDVAELKTDVA---ELKTDVAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:TIGR00606  868 ELKSEKLQIGTNLQrrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
ClyA_NheA-like cd22654
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ...
 33-227 2.25e-04

Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.


Pssm-ID: 439152 [Multi-domain]  Cd Length: 333  Bit Score: 42.25  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  33 SELQQDNALSRADVMRAFQF---QNQHIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKT- 108
Cdd:cd22654   125 TLLDADSKNFSTDAKKAIDSlsgSNGEIAQLRTQIKTINDEIQEELTKILNRPIEVGDGSINIGKQVFTITITTATTKTv 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 109 DVAELKTDVAELKtdvAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAEL---KKDVAELKTDVAELKTDVAILKT 185
Cdd:cd22654   205 DVTSIGGLINGIG---NASDDEVKEAANKIQQKQKELVDLIKKLSDAEIQATQLtlvEDQVNGFTELIKRQIATLENLVE 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1719041701 186 DVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT 227
Cdd:cd22654   282 DWEMLNQNMNQLQTNVNSGKIDSKLLQKQLKQIKKISDELNK 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
59-262 2.28e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  59 MLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 138
Cdd:COG4372    24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 139 AKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTdvAEL 218
Cdd:COG4372   104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEA 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1719041701 219 KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKN 262
Cdd:COG4372   182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 88-263 2.48e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  88 DNDVFRtdIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAE----LKTDVAELK 163
Cdd:PRK04778   94 LNDKFR--FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLAnrfsFGPALDELE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 164 KDVAELKTDVAELKTDVAilKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDV----AELKTDVAELKTD---- 235
Cdd:PRK04778  172 KQLENLEEEFSQFVELTE--SGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELpdqlQELKAGYRELVEEgyhl 249

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1719041701 236 --------VAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PRK04778  250 dhldiekeIQDLKEQIDENLALLEELDLDEAEEKNE 285
PTZ00121 PTZ00121
MAEBL; Provisional
 61-256 2.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   61 STQLKKAESDLRTETGDVAKGV---EVLQTDNDVFRTDIV----ELKTDVAELKTdVAELKTDVAELKTDVAELKTDVAE 133
Cdd:PTZ00121  1190 AEELRKAEDARKAEAARKAEEErkaEEARKAEDAKKAEAVkkaeEAKKDAEEAKK-AEEERNNEEIRKFEEARMAHFARR 1268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  134 LKTDVAKLKTDVDELKTdvAELKTDVAELKKDVAELKTDVAELKTDVAiLKTDVAELKKDVAELKTDVAELKTDVAELKT 213
Cdd:PTZ00121  1269 QAAIKAEEARKADELKK--AEEKKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1719041701  214 DVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 256
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-252 4.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  98 ELKTDVAELKTDVAELK-TDVAELKTDVAEL-------------KTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELK 163
Cdd:PRK03918  567 ELEEELAELLKELEELGfESVEELEERLKELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 164 KDVAELKTDVAElkTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT------DVA 237
Cdd:PRK03918  647 KELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaleRVE 724

                         170
                  ....*....|....*
gi 1719041701 238 ELKTDVAELKTDVAE 252
Cdd:PRK03918  725 ELREKVKKYKALLKE 739
PLN02939 PLN02939
transferase, transferring glycosyl groups
 54-263 4.09e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.81  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  54 NQHIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELK-TD--VAELKTDVAELKTD 130
Cdd:PLN02939  193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAeTEerVFKLEKERSLLDAS 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 131 VAELKTDVAKLKTDVDELKTdvaeLKTDVAELKKDVAELKTDVAELKTDVAILKTDV-AELKKDVAELKTDVAElkTDVA 209
Cdd:PLN02939  273 LRELESKFIVAQEDVSKLSP----LQYDCWWEKVENLQDLLDRATNQVEKAALVLDQnQDLRDKVDKLEASLKE--ANVS 346

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1719041701 210 ELKTDVAELKTDvaELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKND 263
Cdd:PLN02939  347 KFSSYKVELLQQ--KLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
140-248 4.16e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.58  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 140 KLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTD-VAILKTDVAELKKDVAELKtdvAELKTDVAELKTDVAEL 218
Cdd:COG1842    34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKaRLALEKGREDLAREALERK---AELEAQAEALEAQLAQL 110

                          90       100       110
                  ....*....|....*....|....*....|
gi 1719041701 219 KTDVAELKTDVAELKTDVAELKTDVAELKT 248
Cdd:COG1842   111 EEQVEKLKEALRQLESKLEELKAKKDTLKA 140
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 90-229 5.90e-04

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.82  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAEL---------KTDVAKLKTDVDELKTDVA-ELKTDV 159
Cdd:cd22656   124 DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKELEKLNEEYAaKLKAKI 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1719041701 160 AELKKDVAELKTDVAELK---TDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 229
Cdd:cd22656   204 DELKALIADDEAKLAAALrliADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKI 276
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
126-245 6.12e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 126 ELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAE-LKTDVAELKTDVAILKtdvAELKKDVAELKTDVAEL 204
Cdd:COG1842    34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERK---AELEAQAEALEAQLAQL 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1719041701 205 KTDVAELKTDVAELKTDVAELKTDVAELKT--DVAELKTDVAE 245
Cdd:COG1842   111 EEQVEKLKEALRQLESKLEELKAKKDTLKAraKAAKAQEKVNE 153
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 84-264 6.15e-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: 41.21  E-value: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   84 VLQTD-------NDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDEL-------- 148
Cdd:TIGR02169  139 VLQGDvtdfismSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqallk 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  149 ---KTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTD-VAELKTDVAE 224
Cdd:TIGR02169  219 ekrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGE 298

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1719041701  225 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
95-196 7.16e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  95 DIVELKTDVAELKTDVAELKTDVAELKTDVAELKT-----------DVA-ELKTDVAKLKTDVDELKTDVAELKTDVAEL 162
Cdd:COG1842    38 DLVEARQALAQVIANQKRLERQLEELEAEAEKWEEkarlalekgreDLArEALERKAELEAQAEALEAQLAQLEEQVEKL 117

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1719041701 163 KKDVAELKTDVAELKTDVAILKT--DVAELKKDVAE 196
Cdd:COG1842   118 KEALRQLESKLEELKAKKDTLKAraKAAKAQEKVNE 153
ClyA_NheA-like cd22654
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ...
 60-248 7.99e-04

Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.


Pssm-ID: 439152 [Multi-domain]  Cd Length: 333  Bit Score: 40.33  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKT-DVAELKTDV 138
Cdd:cd22654   134 FSTDAKKAIDSLSGSNGEIAQLRTQIKTINDEIQEELTKILNRPIEVGDGSINIGKQVFTITITTATTKTvDVTSIGGLI 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 139 AKLK----TDVDELKTDVAELKTDVAELKKDVAELKTDVAELktdvAILKTDVAELKKDVAELKTDVAELKTDVAELKTD 214
Cdd:cd22654   214 NGIGnasdDEVKEAANKIQQKQKELVDLIKKLSDAEIQATQL----TLVEDQVNGFTELIKRQIATLENLVEDWEMLNQN 289

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1719041701 215 VAELKTDVAELKTDVAELKTDVAELKTDVAELKT 248
Cdd:cd22654   290 MNQLQTNVNSGKIDSKLLQKQLKQIKKISDELNK 323
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 119-192 8.67e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.10  E-value: 8.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1719041701 119 ELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKK 192
Cdd:COG4026   132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK 205
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 42-211 9.47e-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: 40.82  E-value: 9.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   42 SRADVMRAFQFQNQHIMMLSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELK 121
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  122 TdvaELKTDVAELKTDVAKLKTDVDELKTDVAE---LKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELK 198
Cdd:TIGR02169  441 E---EKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517

                          170
                   ....*....|...
gi 1719041701  199 TDVAELKTDVAEL 211
Cdd:TIGR02169  518 ASIQGVHGTVAQL 530
PRK09039 PRK09039
peptidoglycan -binding protein;
98-197 1.05e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  98 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELK 177
Cdd:PRK09039   57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136

                          90       100
                  ....*....|....*....|
gi 1719041701 178 TDVAILKTDVAELKKDVAEL 197
Cdd:PRK09039  137 AQVELLNQQIAALRRQLAAL 156
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
124-264 1.06e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 124 VAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAE 203
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1719041701 204 LKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 177-262 1.12e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 40.10  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 177 KTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAEL-KTDVAELKT 255
Cdd:TIGR04320 246 KTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQA 325


                  ....*..
gi 1719041701 256 DVGNLKN 262
Cdd:TIGR04320 326 ALANAEA 332
PTZ00121 PTZ00121
MAEBL; Provisional
 104-263 1.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  104 AELKTDVAELKTDVAELKTdVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKdvAELKTDVAELKTDVAIL 183
Cdd:PTZ00121  1226 AEAVKKAEEAKKDAEEAKK-AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEEKK 1302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  184 KTDvaELKKDVAEL-KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKN 262
Cdd:PTZ00121  1303 KAD--EAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380


                   .
gi 1719041701  263 D 263
Cdd:PTZ00121  1381 D 1381
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 94-263 1.21e-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: 40.39  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDV 173
Cdd:TIGR04523  68 EKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 174 AELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKT---DVAELKTDVAELKTDV 250
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiqKNKSLESQISELKKQN 227

                         170
                  ....*....|...
gi 1719041701 251 AELKTDVGNLKND 263
Cdd:TIGR04523 228 NQLKDNIEKKQQE 240
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 117-196 1.37e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 117 VAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAE 196
Cdd:COG3883   135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
115-239 1.51e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 115 TDVAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDV 194
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1719041701 195 AELKTDVAELKTDVAELKTDVAELKTDvaelKTDVAELKTDVAEL 239
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKA----GGSIDKLRKEIERL 121
ClyA_MakA-like cd22655
Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; ...
 90-195 1.74e-03

Vibrio cholerae cytotoxin MakA (motility associated killing factor A), and similar proteins; This model includes Vibrio cholerae motility associated killing factor A (MakA) cytotoxin, a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). The MakA protein is encoded by the mak operon. Transport of the MakA protein from the bacteria is shown to occur by flagellum-dependent secretion, highlighting a non-conventional and direct role of flagella in pathogenesis of V. cholerae; a conserved N-terminal FTPP motif is essential for MakA secretion via the flagellum channel in a proton motive force-dependent manner. Structure of MakA shows an elongated, almost entirely alpha-helical protein, with the head domain consisting of two helices and three beta-strands that together with the short beta-strand of the tail domain forms a four-stranded sheet. MakA has been demonstrated to cause toxicity in both Caenorhabditis elegans and zebrafish.


Pssm-ID: 439153 [Multi-domain]  Cd Length: 342  Bit Score: 39.19  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  90 DVFRTDIVELKTDVAELKTD--VAELKTDVAELKTDVAELKTDVAELKtdvAKLKTDVDELKTDVAELKTDVAELKKDVA 167
Cdd:cd22655    74 SAATSQILNIFKALPTAPDDaqVEQIIALLQALQKPVQEIISNIAAYQ---GKLKAWGDKMQAAHDNLTTGAAQIQAAET 150

                          90       100
                  ....*....|....*....|....*...
gi 1719041701 168 ELKTDVAELKTDVAILKTDVAELKKDVA 195
Cdd:cd22655   151 DLQADIDKINNAIANLNAEIAKDNKAIA 178
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
69-252 1.84e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  69 SDLRTETGDVAKGVEVLqtdndvfrTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDEL 148
Cdd:PRK02224  485 EDLEEEVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 149 KTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKtDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTD 228
Cdd:PRK02224  557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635

                         170       180
                  ....*....|....*....|....
gi 1719041701 229 VAELKTDVAELKTDVAELKTDVAE 252
Cdd:PRK02224  636 KRELEAEFDEARIEEAREDKERAE 659
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-211 2.04e-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: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   93 RTDIVELKTDVAELKTDVAELKTDVAELK----TDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAE 168
Cdd:COG4913    344 EREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1719041701  169 LKTDVAELKTDVAILKTDVAELKKDVAE-LKTDVAELKTdVAEL 211
Cdd:COG4913    424 LEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPF-VGEL 466
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
143-255 2.15e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 143 TDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDV 222
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1719041701 223 AELKTDVAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSIDK 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
60-171 2.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  60 LSTQLKKAESDLRTETGDVAKGVEVLQTDndvfrtdivELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDva 139
Cdd:COG4717   400 LKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELREELAELEAELEQLEED-- 468

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1719041701 140 klkTDVDELKTDVAELKTDVAELKKDVAELKT 171
Cdd:COG4717   469 ---GELAELLQELEELKAELRELAEEWAALKL 497
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 94-196 2.62e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  94 TDIVELKTDVAELKTDVAELKTD--------VAELKTDVAELKTDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKD 165
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEqdeasferLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1719041701 166 VAELKTDVAELKTDVAILKTDVAElkKDVAE 196
Cdd:COG0542   491 EKELAELEEELAELAPLLREEVTE--EDIAE 519
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
150-261 2.74e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 150 TDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDV 229
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1719041701 230 AELKTDVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSID 112
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
 87-234 2.78e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 38.82  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  87 TDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDV-AELKTDVAKLKTDVDE--LKTDVAELKTDVAELK 163
Cdd:NF033928  116 PLSSDDKEIVKELKEILEDLKNDIKDYQQKADDVKKELDDFENDLrEELLPQLKLKKKLYDDnlGSDSIEELREKIDQLE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 164 KDVAELKTDVAELKTDV---------------AILKTDVAELKKDVAELKtdvAELKTDVAELKTDVAeLKTDVAELKTD 228
Cdd:NF033928  196 KEIEQLNKEYDDYVKLSftglaggpiglaitgGIFGSKAEKIRKEKNALI---QEIDELQEQLKKKNA-LLGSLERLQTS 271


                  ....*.
gi 1719041701 229 VAELKT 234
Cdd:NF033928  272 LDDILT 277
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 139-258 2.97e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 139 AKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAilktdvAELKKDVAELKTDVAELKTDVAELKTDVAEL 218
Cdd:COG0542   400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERL------AELRDELAELEEELEALKARWEAEKELIEEI 473

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1719041701 219 KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVG 258
Cdd:COG0542   474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 111-231 3.13e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 111 AELKTDVAELKTDVAELKTDVAELKTDVAKLKTDVDEL-KTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAE 189
Cdd:COG0542   400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1719041701 190 LKKDVAELKTDVAELKTDVAELKTDVAELKTDVAElkTDVAE 231
Cdd:COG0542   480 LEQRYGKIPELEKELAELEEELAELAPLLREEVTE--EDIAE 519
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 154-226 3.48e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.17  E-value: 3.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1719041701 154 ELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELK 226
Cdd:COG4026   132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL 204
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
161-261 4.15e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 37.50  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 161 ELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDvAEL-----KTDVA-ELKTDVAELKTDVAELKTDVAELKT 234
Cdd:COG1842    34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEK-ARLalekgREDLArEALERKAELEAQAEALEAQLAQLEE 112

                          90       100
                  ....*....|....*....|....*..
gi 1719041701 235 DVAELKTDVAELKTDVAELKTDVGNLK 261
Cdd:COG1842   113 QVEKLKEALRQLESKLEELKAKKDTLK 139
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 144-264 4.16e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.34  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 144 DVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVA 223
Cdd:pfam07888  60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1719041701 224 ELKTDVAELKTDVAELKTDVAELKTDVAELKTDVGNLKNDM 264
Cdd:pfam07888 140 TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-254 4.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 132 AELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKtdvaELKTDVAEL 211
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEEL 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1719041701 212 KTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK 254
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
129-253 5.93e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.58  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701 129 TDVAELKTDVAKLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDV 208
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1719041701 209 AELKTDVAELKTDVAELKTDVAELKTDvaelKTDVAELKTDVAEL 253
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKA----GGSIDKLRKEIERL 121
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 161-233 6.89e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 37.40  E-value: 6.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1719041701 161 ELKKDVAELKTDVAELKTDVAILKTDVAELKKDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK 233
Cdd:COG4026   132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL 204
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 82-161 7.03e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  82 VEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKtdvAELKTDVAKLKTDVDELKTDVAELKTDVAE 161
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPP 174
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 62-149 7.52e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.30  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   62 TQLKKAESDLR----TETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELK-- 135
Cdd:smart00787 189 RQLKQLEDELEdcdpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRgf 268

                           90
                   ....*....|....*.
gi 1719041701  136 --TDVAKLKTDVDELK 149
Cdd:smart00787 269 tfKEIEKLKEQLKLLQ 284
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 60-255 8.34e-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: 37.90  E-value: 8.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701   60 LSTQLKKAESDLRTETGDVAKGVEVLQTDNDVFRTDIVELKTDVAELKTDVAELKTDVAELKTDVAELKTDVAELKTdva 139
Cdd:pfam12128  214 PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQ--- 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  140 KLKTDVDELKTDVAELKTDVAELKKDVAELKTDVAELKTDV-AILKTDVAELKKDVAELKTDVAELKTDVAELKT----- 213
Cdd:pfam12128  291 LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKAltgkh 370

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1719041701  214 -DVAElKTDVAELKTDvAELKTDVAELKTDVAELKTDVAELKT 255
Cdd:pfam12128  371 qDVTA-KYNRRRSKIK-EQNNRDIAGIKDKLAKIREARDRQLA 411
ClyA_XaxA-like cd22657
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ...
 41-172 9.50e-03

Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and similar proteins; This model includes Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, both parts of two-component alpha-helical pore-forming toxins (alpha-PFTs). The xaxAB genes encoding the XaxAB toxin have also been also identified in various plant and human pathogens. XaxAB triggers necrosis and apoptosis in both insect hemocytes and mammalian cells. Structure studies show that component A binds to component B's back, forming a subunit; twelve to fifteen of these subunits then conjoin as the pore-forming toxin. Component A stabilizes each subunit on the membrane and activates component B, which then punctures the membrane by swinging out its lower end. Similarly, Yersinia enterocolitica YaxA, encoded by the yaxAB gene, forms a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Although both subunits bear membrane-active moieties, only YaxA is capable of binding to membranes by itself and YaxB is subsequently recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices; pore formation then progresses by further oligomerization of YaxA-YaxB dimers. YaxAB has been found to be strongly upregulated by the Yersinia master regulator RovA, a transcriptional activator of Yersinia outer membrane protein invasion which is involved in bacterial attachment and invasion across the intestinal epithelium.


Pssm-ID: 439155 [Multi-domain]  Cd Length: 306  Bit Score: 37.18  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1719041701  41 LSRADVMRAFQFQNQH----------IMMLSTQLKKAESDLRTETGDVakgVEVlqtdndvfrtdIVELKTDVAELKTDV 110
Cdd:cd22657    39 LEPADFLELFQNIRNHarswspleddIKQVGSDLKLFAGSIISTGEQI---IEI-----------ISDLGEYLEDIKEDI 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1719041701 111 AELKTDVAELKTDVAELKTDVAELKTDVAKLKT---DVDELKTDVAELKTDVAELKKDVAELKTD 172
Cdd:cd22657   105 KEYSKSTEEVKARLDDFRDELREELIPEVKLKLkliDRNDLDEEIEELNEEIDELDEEIDELNKE 169
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH