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Conserved domains on  [gi|568914155|ref|XP_006498325|]
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endosome-associated-trafficking regulator 1 isoform X2 [Mus musculus]

Protein Classification

ClyA-like and alpha/beta hydrolases superfamily-containing protein( domain architecture ID 1903979)

ClyA-like and alpha/beta hydrolases superfamily-containing protein

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 ...
 228-350 2.38e-05

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155   228 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 304
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568914155   305 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 350
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
ClyA-like super family cl45899
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 314-408 4.41e-04

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).


The actual alignment was detected with superfamily member cd22657:

Pssm-ID: 459244 [Multi-domain]  Cd Length: 306  Bit Score: 41.80  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 314 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 392
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 568914155 393 ILKSIDRISEVKDEVD 408
Cdd:cd22657  265 IDASAEELDKIDDALS 280
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 228-350 2.38e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155   228 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 304
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568914155   305 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 350
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 270-397 4.48e-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: 45.14  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 270 QTEMVRTLERKLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRS 346
Cdd:COG4942   18 QADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568914155 347 gqgaslSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLV--AEILKSI 397
Cdd:COG4942   98 ------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
ClyA_XaxA-like cd22657
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ...
 314-408 4.41e-04

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: 41.80  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 314 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 392
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 568914155 393 ILKSIDRISEVKDEVD 408
Cdd:cd22657  265 IDASAEELDKIDDALS 280
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 256-344 3.89e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  256 LRRKLNEVQsfseTQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLS 335
Cdd:pfam13863  15 LDAKREEIE----RLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90


                  ....*....
gi 568914155  336 NLRRENEAL 344
Cdd:pfam13863  91 ELKSEISKL 99
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 228-350 2.38e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155   228 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 304
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568914155   305 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 350
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 270-397 4.48e-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: 45.14  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 270 QTEMVRTLERKLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRS 346
Cdd:COG4942   18 QADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568914155 347 gqgaslSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLV--AEILKSI 397
Cdd:COG4942   98 ------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 247-361 9.99e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 9.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155   247 EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKL---EAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKL 323
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568914155   324 KQEINLLQAQLSNLRRENEALRSGQGASLSVVKQNTDV 361
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
ClyA_XaxA-like cd22657
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ...
 314-408 4.41e-04

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: 41.80  E-value: 4.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 314 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 392
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 568914155 393 ILKSIDRISEVKDEVD 408
Cdd:cd22657  265 IDASAEELDKIDDALS 280
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 236-340 4.51e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 39.84  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 236 DRHLRTLQISYEALKDENSKLRRKLN----EVQSFSETQTEMVRTLerkleaKMIKEESdfhdlESVVQQVEQNLELMTK 311
Cdd:COG3599   26 DEFLDEVAEDYERLIRENKELKEKLEeleeELEEYRELEETLQKTL------VVAQETA-----EEVKENAEKEAELIIK 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 568914155 312 RA-VKAENHVLKLKQEINLLQAQLSNLRRE 340
Cdd:COG3599   95 EAeLEAEKIIEEAQEKARKIVREIEELKRQ 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
233-345 4.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 233 SLGDRHLRTLQISYEALKDENSKLRRKLNEvqsfseTQTEMvrtleRKLEAKMIKEESDFHDLESVVQQVEQNLELMTKR 312
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-----EQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568914155 313 AVKAENHVLKLKQEINLLQAQLSNLRRENEALR 345
Cdd:COG4372   96 LAQAQEELESLQEEAEELQEELEELQKERQDLE 128
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
236-342 1.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 236 DRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVK 315
Cdd:COG4717  138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                         90       100
                 ....*....|....*....|....*..
gi 568914155 316 AENHVLKLKQEINLLQAQLSNLRRENE 342
Cdd:COG4717  218 AQEELEELEEELEQLENELEAAALEER 244
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 249-409 1.63e-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: 40.77  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  249 LKDENSKLRRKLNEVQSFSETQTEMVRTLER-------KLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAEN 318
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqNLEQkqKELKSkEKELKKLNEEKKELEEKVKDLTKKISSLKE 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  319 HVLKLKQEINLLQAQLSNLRRENEALRSG-QGASLSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTL-----NLVAE 392
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKekekkDLIKE 604

                         170
                  ....*....|....*..
gi 568914155  393 ILKSIDRISEVKDEVDS 409
Cdd:TIGR04523 605 IEEKEKKISSLEKELEK 621
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 256-344 3.89e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  256 LRRKLNEVQsfseTQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLS 335
Cdd:pfam13863  15 LDAKREEIE----RLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90


                  ....*....
gi 568914155  336 NLRRENEAL 344
Cdd:pfam13863  91 ELKSEISKL 99
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 237-351 4.60e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 237 RHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESdfhdLESVVQQVEQNLELMTKRAVKA 316
Cdd:COG4942  136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA----LEALKAERQKLLARLEKELAEL 211

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568914155 317 ENHVLKLKQEINLLQAQLSNLRRENEALRSGQGAS 351
Cdd:COG4942  212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 248-407 5.20e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 248 ALKDENSKLRRKLNEVQsfsetqtEMVRTLERKLEAKMIKEESdfhdLESVVQQVEQNLELMTKRAVKAENHVLKLKQEI 327
Cdd:COG4942   17 AQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155 328 NLLQAQLSNLRRENEAL------------RSGQGASLSVVKQNTDVA-----LQNLHLVMNSAHASIKQLVSGADTLN-L 389
Cdd:COG4942   86 AELEKEIAELRAELEAQkeelaellralyRLGRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAaL 165

                        170
                 ....*....|....*...
gi 568914155 390 VAEILKSIDRISEVKDEV 407
Cdd:COG4942  166 RAELEAERAELEALLAEL 183
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 236-406 6.39e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 38.65  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  236 DRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQT------EMVRTLERklEAKMIKEES-----DFHDLESVVQQVE- 303
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQ--EVARYKEESgkaqaEVERLLGILREVEn 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  304 ---------QNLELMTKRAVKAEN-HVLKLK---QEINLLQAQL--SNLRRENEALRSGQG-------ASLSVVKQNTDV 361
Cdd:pfam10174 594 ekndkdkkiAELESLTLRQMKEQNkKVANIKhgqQEMKKKGAQLleEARRREDNLADNSQQlqleelmGALEKTRQELDA 673

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568914155  362 ALQNLHLVMNSAHASIKQLVsgadtlNLVAEILKSIDRISEVKDE 406
Cdd:pfam10174 674 TKARLSSTQQSLAEKDGHLT------NLRAERRKQLEEILEMKQE 712
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 247-337 6.87e-03

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: 38.88  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155   247 EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMikeeSDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQE 326
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELS----EELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                           90
                   ....*....|.
gi 568914155   327 INLLQAQLSNL 337
Cdd:TIGR02168  938 IDNLQERLSEE 948
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 249-345 7.61e-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: 38.46  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  249 LKDENSKLRRKLNEVQSFSETQTEMVRTLERKL--------EAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHV 320
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlkseisDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKII 337

                          90       100
                  ....*....|....*....|....*
gi 568914155  321 LKLKQEINLLQAQLSNLRRENEALR 345
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQ 362
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
225-348 7.83e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914155  225 ADFAAHEESLGDRHLRTLQISY---EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAkmikEESDFHDLesvVQQ 301
Cdd:COG4913   316 ARLDALREELDELEAQIRGNGGdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPA----SAEEFAAL---RAE 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914155  302 VEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQ 348
Cdd:COG4913   389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
 
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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