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Conserved domains on  [gi|1333152024|ref|XP_023550800|]
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protein FLX-like 3 [Cucurbita pepo subsp. pepo]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-220 7.92e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   41 EELELQHREMQRIISDNRMVIDDntiLQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKSEV 120
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  121 LHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADmdgLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNL 200
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLERRIAATERRLEDLEEQIEELSEDI 854
                          170       180
                   ....*....|....*....|
gi 1333152024  201 VSMAREIEKLRAEKLNLERA 220
Cdd:TIGR02168  855 ESLAAEIEELEELIEELESE 874
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-220 7.92e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   41 EELELQHREMQRIISDNRMVIDDntiLQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKSEV 120
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  121 LHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADmdgLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNL 200
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLERRIAATERRLEDLEEQIEELSEDI 854
                          170       180
                   ....*....|....*....|
gi 1333152024  201 VSMAREIEKLRAEKLNLERA 220
Cdd:TIGR02168  855 ESLAAEIEELEELIEELESE 874
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
38-221 2.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  38 ALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIpkvlSEKEAQSRELLERGLKLEAELRASEPLK 117
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAEL 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 118 SEVLHLRGEI-QKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAM 196
Cdd:COG1196   361 AEAEEALLEAeAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180
                  ....*....|....*....|....*
gi 1333152024 197 EKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELL 465
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
97-221 3.07e-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: 41.54  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   97 RELLERGLKLEAElRASEPLKSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMR-ADMDGLLKELIEA 175
Cdd:smart00787 138 RMKLLEGLKEGLD-ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKL 216
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1333152024  176 RRAYEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
25-214 3.29e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.66  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  25 VERVPAPLPIHPAALEEELELQHREMQRIISDNRMVIDDNtILQRELSAAKE----EIHRLNQAIPKVLSEKEAQSRELL 100
Cdd:pfam07111 463 QESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAH-LIQQEVGRAREqgeaERQQLSEVAQQLEQELQRAQESLA 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 101 ERGLKLEAELRASEPLKSEVLHLRGEIQKLNNL-KQDLSAKVQSL-TKDVTRLQAENQQLNSMRADMDGLLKELIEARRA 178
Cdd:pfam07111 542 SVGQQLEVARQGQQESTEEAASLRQELTQQQEIyGQALQEKVAEVeTRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1333152024 179 YEYEKKSNEE-QNEQKQAMEKNLVSMAREIEKLRAEK 214
Cdd:pfam07111 622 ATQEKERNQElRRLQDEARKEEGQRLARRVQELERDK 658
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
50-168 2.53e-03

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: 38.16  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  50 MQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKvlsekeaQSRELLERglkLEAelrasepLKSEVL----HLRG 125
Cdd:cd21116    54 KPKLLSLPNDIIGYNNTFQSYYPDLIELADNLIKGDQG-------AKQQLLQG---LEA-------LQSQVTkkqtSVTS 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1333152024 126 EIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGL 168
Cdd:cd21116   117 FINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSL 159
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-221 3.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  41 EELELQHREMQRIISDNRMVIDDNTILQRELSAAKE---EIHRLNQAIPKVLSEKEAQSRELLERGLK----LEAELRAS 113
Cdd:PRK03918  518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKEL 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 114 EPLKSEVLHLRgeiqklnNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAY---EYEKKSNEEQN 190
Cdd:PRK03918  598 EPFYNEYLELK-------DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeEYEELREEYLE 670
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333152024 191 ---------EQKQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:PRK03918  671 lsrelaglrAELEELEKRREEIKKTLEKLKEELEEREKAK 710
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-220 7.92e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   41 EELELQHREMQRIISDNRMVIDDntiLQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKSEV 120
Cdd:TIGR02168  701 AELRKELEELEEELEQLRKELEE---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  121 LHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADmdgLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNL 200
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN---LRERLESLERRIAATERRLEDLEEQIEELSEDI 854
                          170       180
                   ....*....|....*....|
gi 1333152024  201 VSMAREIEKLRAEKLNLERA 220
Cdd:TIGR02168  855 ESLAAEIEELEELIEELESE 874
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
41-220 1.90e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   41 EELELQHREMQRIISDnrmviddntiLQRELSAAKEEIHRLNQAIpKVLSEKEAQSRELLERglkLEAELrasEPLKSEV 120
Cdd:TIGR02168  270 EELRLEVSELEEEIEE----------LQKELYALANEISRLEQQK-QILRERLANLERQLEE---LEAQL---EELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  121 LHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDgllKELIEARRAYEYEKKSNEEQNEQKQAMEKNL 200
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARL 409
                          170       180
                   ....*....|....*....|
gi 1333152024  201 VSMAREIEKLRAEKLNLERA 220
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKK 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
38-221 2.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  38 ALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIpkvlSEKEAQSRELLERGLKLEAELRASEPLK 117
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAEL 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 118 SEVLHLRGEI-QKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAM 196
Cdd:COG1196   361 AEAEEALLEAeAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180
                  ....*....|....*....|....*
gi 1333152024 197 EKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELL 465
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
67-221 2.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  67 LQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKSEVLHLRGEIQKLNNLKQDLSAKVQSLTK 146
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333152024 147 DVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
41-222 4.24e-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: 47.76  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   41 EELELQHREMQRIISDNRMVIDdntILQRELSAAKEEIHRLNqaipKVLSEKEAQSRELLERGLKLEAELRaseplKSEV 120
Cdd:TIGR02169  726 EQLEQEEEKLKERLEELEEDLS---SLEQEIENVKSELKELE----ARIEELEEDLHKLEEALNDLEARLS-----HSRI 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  121 LHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYE-------KKSNEEQNEQK 193
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlngkKEELEEELEEL 873
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1333152024  194 QA----MEKNLVSMAREIEKLRAEKLNLERARG 222
Cdd:TIGR02169  874 EAalrdLESRLGDLKKERDELEAQLRELERKIE 906
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
37-219 6.97e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 6.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   37 AALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPL 116
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  117 KSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRAD--MDGLLKELIEARRAYEYEKKSNEEQNEQKQ 194
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELE 457
                          170       180
                   ....*....|....*....|....*
gi 1333152024  195 AMEKNLVSMAREIEKLRAEKLNLER 219
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAER 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
65-218 9.55e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 9.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   65 TILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKSEVLHLRGEIQKLNNLKQDLSAKVQ-- 142
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQil 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  143 -----------------------SLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKN 199
Cdd:TIGR02168  308 rerlanlerqleeleaqleelesKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                          170
                   ....*....|....*....
gi 1333152024  200 LVSMAREIEKLRAEKLNLE 218
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLE 406
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
37-220 3.39e-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: 44.37  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  37 AALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIpkvlSEKEAQSRELLERGLKLEAELRASEPL 116
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL----AALEAELAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 117 KSEVLH--------------LRGE--------IQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIE 174
Cdd:COG4942   106 LAELLRalyrlgrqpplallLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1333152024 175 ARRAYEYEKKsneEQNEQKQAMEKNLVSMAREIEKLRAEKLNLERA 220
Cdd:COG4942   186 ERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEAL 228
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
40-225 4.33e-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: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  40 EEELELQHREMQRIISDNRMVIDDntiLQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEP---- 115
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLalll 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 116 ---------------------LKSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELie 174
Cdd:COG4942   127 spedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL-- 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333152024 175 arrayEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNLERARGLGA 225
Cdd:COG4942   205 -----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
37-195 6.61e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  37 AALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGL------------ 104
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGsvsyldvllgse 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 105 -------KLEAELRASEPLKSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARR 177
Cdd:COG3883   113 sfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
                         170
                  ....*....|....*...
gi 1333152024 178 AYEYEKKSNEEQNEQKQA 195
Cdd:COG3883   193 AAEAQLAELEAELAAAEA 210
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-221 1.61e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  37 AALEEELELQHREMQRIisdnrmvIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPL 116
Cdd:COG1196   263 AELEAELEELRLELEEL-------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 117 KSEVLHLRGEIQ----KLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQ 192
Cdd:COG1196   336 EEELEELEEELEeaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
                         170       180
                  ....*....|....*....|....*....
gi 1333152024 193 KQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEAL 444
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
97-221 3.07e-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: 41.54  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   97 RELLERGLKLEAElRASEPLKSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMR-ADMDGLLKELIEA 175
Cdd:smart00787 138 RMKLLEGLKEGLD-ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKL 216
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1333152024  176 RRAYEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
25-214 3.29e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 41.66  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  25 VERVPAPLPIHPAALEEELELQHREMQRIISDNRMVIDDNtILQRELSAAKE----EIHRLNQAIPKVLSEKEAQSRELL 100
Cdd:pfam07111 463 QESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAH-LIQQEVGRAREqgeaERQQLSEVAQQLEQELQRAQESLA 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 101 ERGLKLEAELRASEPLKSEVLHLRGEIQKLNNL-KQDLSAKVQSL-TKDVTRLQAENQQLNSMRADMDGLLKELIEARRA 178
Cdd:pfam07111 542 SVGQQLEVARQGQQESTEEAASLRQELTQQQEIyGQALQEKVAEVeTRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1333152024 179 YEYEKKSNEE-QNEQKQAMEKNLVSMAREIEKLRAEK 214
Cdd:pfam07111 622 ATQEKERNQElRRLQDEARKEEGQRLARRVQELERDK 658
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-222 4.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  37 AALEEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPL 116
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 117 KSEVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEAR-RAYEYEKKSNEEQNEQKQA 195
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeEEEEALEEAAEEEAELEEE 457
                         170       180
                  ....*....|....*....|....*..
gi 1333152024 196 MEKNLVSMAREIEKLRAEKLNLERARG 222
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLE 484
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
69-220 5.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  69 RELSAAKEEIHRLNQAIpKVLSEKEAQSRELLERGLKLEAELRAsepLKSEVLHLRGEIQKLNNLKQ---------DLSA 139
Cdd:COG4717    64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEE---LEAELEELREELEKLEKLLQllplyqeleALEA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 140 KVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRayeyekKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNLER 219
Cdd:COG4717   140 ELAELPERLEELEERLEELRELEEELEELEAELAELQE------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213

                  .
gi 1333152024 220 A 220
Cdd:COG4717   214 E 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
39-220 7.82e-04

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: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  39 LEEELELQHREMQRIISDNrmviddnTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRASEPLKS 118
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETI-------IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 119 EVLHLRGEIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELiearrayeYEKKSNEEQNEQKQAMEK 198
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL--------EDELNKDDFELKKENLEK 561
                         170       180
                  ....*....|....*....|..
gi 1333152024 199 NLVSMAREIEKLRAEKLNLERA 220
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKK 583
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
68-221 8.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 8.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  68 QRELSAAKEEIHRLNQaipkVLSEKEAQsRELLER---------GLKLEAELRASEPLKSEVLHLRGEIQKLNNLKQDLS 138
Cdd:COG1196   178 ERKLEATEENLERLED----ILGELERQ-LEPLERqaekaeryrELKEELKELEAELLLLKLRELEAELEELEAELEELE 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 139 AKVQSLTKDVTRLQAE-----------NQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNLVSMAREI 207
Cdd:COG1196   253 AELEELEAELAELEAEleelrleleelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                         170
                  ....*....|....
gi 1333152024 208 EKLRAEKLNLERAR 221
Cdd:COG1196   333 EELEEELEELEEEL 346
COG5022 COG5022
Myosin heavy chain [General function prediction only];
40-217 1.37e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.06  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   40 EEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLErglkLEAELRASEPLKSE 119
Cdd:COG5022    956 LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQ----LKELPVEVAELQSA 1031
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  120 VLHLRGEIQKLNNLKqDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEeqnEQKQAMEKN 199
Cdd:COG5022   1032 SKIISSESTELSILK-PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINV---KDLEVTNRN 1107
                          170
                   ....*....|....*...
gi 1333152024  200 LVSMAREIEKLRAEKLNL 217
Cdd:COG5022   1108 LVKPANVLQFIVAQMIKL 1125
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
40-212 1.80e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  40 EEELELQHREMQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKVLSEKEAQSRELLERGLKLEAELRAsepLKSE 119
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI---LENK 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 120 VLHLRGEIQKLNNLKQDLSAKVQSLTKDVTrlqAENQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKN 199
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGS---AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
                         170
                  ....*....|...
gi 1333152024 200 LVSmarEIEKLRA 212
Cdd:pfam05483 673 LLE---EVEKAKA 682
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
50-168 2.53e-03

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: 38.16  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  50 MQRIISDNRMVIDDNTILQRELSAAKEEIHRLNQAIPKvlsekeaQSRELLERglkLEAelrasepLKSEVL----HLRG 125
Cdd:cd21116    54 KPKLLSLPNDIIGYNNTFQSYYPDLIELADNLIKGDQG-------AKQQLLQG---LEA-------LQSQVTkkqtSVTS 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1333152024 126 EIQKLNNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGL 168
Cdd:cd21116   117 FINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSL 159
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-221 3.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  41 EELELQHREMQRIISDNRMVIDDNTILQRELSAAKE---EIHRLNQAIPKVLSEKEAQSRELLERGLK----LEAELRAS 113
Cdd:PRK03918  518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFEsveeLEERLKEL 597
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024 114 EPLKSEVLHLRgeiqklnNLKQDLSAKVQSLTKDVTRLQAENQQLNSMRADMDGLLKELIEARRAY---EYEKKSNEEQN 190
Cdd:PRK03918  598 EPFYNEYLELK-------DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeEYEELREEYLE 670
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333152024 191 ---------EQKQAMEKNLVSMAREIEKLRAEKLNLERAR 221
Cdd:PRK03918  671 lsrelaglrAELEELEKRREEIKKTLEKLKEELEEREKAK 710
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
67-213 4.47e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024   67 LQRELSAAKEEIHRLNQAIpkvlSEKEAQSRELLERGLKLEAELRAS-----EPLKSEVLHLRGEIQKLNNLKQDLSAKV 141
Cdd:COG4913    293 LEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEALL 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  142 QSLT-------KDVTRLQAE-NQQLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAE 213
Cdd:COG4913    369 AALGlplpasaEEFAALRAEaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
67-217 9.17e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.12  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333152024  67 LQRELSAAKEEIHRLNQAIpkvlSEKEAQSRELLERGLKLEAEL-RASEPLKSEVLHLRGEIQKLNNLKQDLSAKvqSLT 145
Cdd:COG3883    42 LQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIeERREELGERARALYRSGGSVSYLDVLLGSE--SFS 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333152024 146 KDVTRLQAenqqLNSMRADMDGLLKELIEARRAYEYEKKSNEEQNEQKQAMEKNLVSMAREIEKLRAEKLNL 217
Cdd:COG3883   116 DFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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