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Conserved domains on  [gi|146134435|ref|NP_080839|]
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endosome-associated-trafficking regulator 1 isoform 1 [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 ...
 251-373 1.52e-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: 47.36  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435   251 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 146134435   328 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
ClyA-like super family cl45899
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 337-431 3.97e-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: 42.19  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 337 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 415
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 146134435 416 ILKSIDRISEVKDEVD 431
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 ...
 251-373 1.52e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435   251 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 146134435   328 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 293-420 3.20e-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: 45.91  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 293 QTEMVRTLERKLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRS 369
Cdd:COG4942   18 QADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 146134435 370 gqgaslSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLV--AEILKSI 420
Cdd:COG4942   98 ------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
ClyA_XaxA-like cd22657
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ...
 337-431 3.97e-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: 42.19  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 337 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 415
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 146134435 416 ILKSIDRISEVKDEVD 431
Cdd:cd22657  265 IDASAEELDKIDDALS 280
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 259-429 1.83e-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: 40.58  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  259 DRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQT------EMVRTLERklEAKMIKEES-----DFHDLESVVQQVE- 326
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQ--EVARYKEESgkaqaEVERLLGILREVEn 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  327 ---------QNLELMTKRAVKAEN-HVLKLK---QEINLLQAQL--SNLRRENEALRSGQG-------ASLSVVKQNTDV 384
Cdd:pfam10174 594 ekndkdkkiAELESLTLRQMKEQNkKVANIKhgqQEMKKKGAQLleEARRREDNLADNSQQlqleelmGALEKTRQELDA 673

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 146134435  385 ALQNLHLVMNSAHASIKQLVsgadtlNLVAEILKSIDRISEVKDE 429
Cdd:pfam10174 674 TKARLSSTQQSLAEKDGHLT------NLRAERRKQLEEILEMKQE 712
PRK12704 PRK12704
phosphodiesterase; Provisional
 266-371 9.48e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 266 QISYEALKDENSKLRRKLNEVQsfsetqtEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLK 345
Cdd:PRK12704  42 RILEEAKKEAEAIKKEALLEAK-------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114

                         90       100
                 ....*....|....*....|....*.
gi 146134435 346 LKQEINLLQAQLSNLRRENEALRSGQ 371
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQ 140
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-373 1.52e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435   251 AAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLE---AKMIKEESDFHDLESVVQQVEQ 327
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrERLANLERQLEELEAQLEELES 330

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 146134435   328 NLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQGA 373
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 293-420 3.20e-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: 45.91  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 293 QTEMVRTLERKLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRS 369
Cdd:COG4942   18 QADAAAEAEAELEQlqQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 146134435 370 gqgaslSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTLNLV--AEILKSI 420
Cdd:COG4942   98 ------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYL 144
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 270-384 6.47e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435   270 EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKL---EAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKL 346
Cdd:TIGR02169  395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 146134435   347 KQEINLLQAQLSNLRRENEALRSGQGASLSVVKQNTDV 384
Cdd:TIGR02169  475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
256-432 9.83e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 256 SLGDRHLRTLQISYEALKDENSKLRRKLNEvqsfseTQTEMvrtleRKLEAKMIKEESDFHDLESVVQQVEQNLELMTKR 335
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQ------AREEL-----EQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 336 AVKAENHVLKLKQEINLLQAQLSNLRRENEALRS------GQGASLSVVKQNTDVALQNLHLVMNSAHASIKQL------ 403
Cdd:COG4372   96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkqleAQIAELQSEIAEREEELKELEEQLESLQEELAALeqelqa 175

                        170       180
                 ....*....|....*....|....*....
gi 146134435 404 VSGADTLNLVAEILKSIDRISEVKDEVDS 432
Cdd:COG4372  176 LSEAEAEQALDELLKEANRNAEKEEELAE 204
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 259-363 1.67e-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: 40.99  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 259 DRHLRTLQISYEALKDENSKLRRKLN----EVQSFSETQTEMVRTLerkleaKMIKEESdfhdlESVVQQVEQNLELMTK 334
Cdd:COG3599   26 DEFLDEVAEDYERLIRENKELKEKLEeleeELEEYRELEETLQKTL------VVAQETA-----EEVKENAEKEAELIIK 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 146134435 335 RA-VKAENHVLKLKQEINLLQAQLSNLRRE 363
Cdd:COG3599   95 EAeLEAEKIIEEAQEKARKIVREIEELKRQ 124
ClyA_XaxA-like cd22657
Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA) and Yersinia enterocolitica YaxA, and ...
 337-431 3.97e-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: 42.19  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 337 VKAENhVLKLKQEINLLQAQLSNLRRENEALRsgqgASLSVVKQNtdvaLQNLHLVMNSAHASIKQLVsgaDTLNLV-AE 415
Cdd:cd22657  197 VKAEK-IRKERNELIAEREELIQKLKSKNRLL----GSLERLETD----LQDLDIRMIDAEVATKNLE---TVWNTIlTY 264

                         90
                 ....*....|....*.
gi 146134435 416 ILKSIDRISEVKDEVD 431
Cdd:cd22657  265 IDASAEELDKIDDALS 280
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 272-432 5.92e-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: 42.31  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  272 LKDENSKLRRKLNEVQSFSETQTEMVRTLER-------KLEA--KMIKE-ESDFHDLESVVQQVEQNLELMTKRAVKAEN 341
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqNLEQkqKELKSkEKELKKLNEEKKELEEKVKDLTKKISSLKE 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  342 HVLKLKQEINLLQAQLSNLRRENEALRSG-QGASLSVVKQNTDVALQNLHLVMNSAHASIKQLVSGADTL-----NLVAE 415
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKDDFElKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKekekkDLIKE 604

                         170
                  ....*....|....*..
gi 146134435  416 ILKSIDRISEVKDEVDS 432
Cdd:TIGR04523 605 IEEKEKKISSLEKELEK 621
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
259-365 7.85e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 259 DRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVK 338
Cdd:COG4717  138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                         90       100
                 ....*....|....*....|....*..
gi 146134435 339 AENHVLKLKQEINLLQAQLSNLRRENE 365
Cdd:COG4717  218 AQEELEELEEELEQLENELEAAALEER 244
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 259-429 1.83e-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: 40.58  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  259 DRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQT------EMVRTLERklEAKMIKEES-----DFHDLESVVQQVE- 326
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQ--EVARYKEESgkaqaEVERLLGILREVEn 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  327 ---------QNLELMTKRAVKAEN-HVLKLK---QEINLLQAQL--SNLRRENEALRSGQG-------ASLSVVKQNTDV 384
Cdd:pfam10174 594 ekndkdkkiAELESLTLRQMKEQNkKVANIKhgqQEMKKKGAQLleEARRREDNLADNSQQlqleelmGALEKTRQELDA 673

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 146134435  385 ALQNLHLVMNSAHASIKQLVsgadtlNLVAEILKSIDRISEVKDE 429
Cdd:pfam10174 674 TKARLSSTQQSLAEKDGHLT------NLRAERRKQLEEILEMKQE 712
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 279-367 1.97e-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: 37.93  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  279 LRRKLNEVQsfseTQTEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQEINLLQAQLS 358
Cdd:pfam13863  15 LDAKREEIE----RLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90


                  ....*....
gi 146134435  359 NLRRENEAL 367
Cdd:pfam13863  91 ELKSEISKL 99
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 271-430 3.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 271 ALKDENSKLRRKLNEVQsfsetqtEMVRTLERKLEAKMIKEESdfhdLESVVQQVEQNLELMTKRAVKAENHVLKLKQEI 350
Cdd:COG4942   17 AQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 351 NLLQAQLSNLRRENEAL------------RSGQGASLSVVKQNTDVA-----LQNLHLVMNSAHASIKQLVSGADTLN-L 412
Cdd:COG4942   86 AELEKEIAELRAELEAQkeelaellralyRLGRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAaL 165

                        170
                 ....*....|....*...
gi 146134435 413 VAEILKSIDRISEVKDEV 430
Cdd:COG4942  166 RAELEAERAELEALLAEL 183
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 272-368 3.97e-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: 39.62  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  272 LKDENSKLRRKLNEVQSFSETQ-------TEMVRTLERKLEA-KMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHV 343
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNnkkikelEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKII 337

                          90       100
                  ....*....|....*....|....*
gi 146134435  344 LKLKQEINLLQAQLSNLRRENEALR 368
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQ 362
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 260-374 4.00e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 260 RHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESdfhdLESVVQQVEQNLELMTKRAVKA 339
Cdd:COG4942  136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA----LEALKAERQKLLARLEKELAEL 211

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 146134435 340 ENHVLKLKQEINLLQAQLSNLRRENEALRSGQGAS 374
Cdd:COG4942  212 AAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-360 4.69e-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: 39.27  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435   270 EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMikeeSDFHDLESVVQQVEQNLELMTKRAVKAENHVLKLKQE 349
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEEALALLRSELEELS----EELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937

                           90
                   ....*....|.
gi 146134435   350 INLLQAQLSNL 360
Cdd:TIGR02168  938 IDNLQERLSEE 948
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
248-371 5.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  248 ADFAAHEESLGDRHLRTLQISY---EALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAkmikEESDFHDLesvVQQ 324
Cdd:COG4913   316 ARLDALREELDELEAQIRGNGGdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPA----SAEEFAAL---RAE 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 146134435  325 VEQNLELMTKRAVKAENHVLKLKQEINLLQAQLSNLRRENEALRSGQ 371
Cdd:COG4913   389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 251-358 5.89e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 37.30  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435  251 AAHEESLGDRHLRT------LQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLeaKMIKEEsdFHDLESVVQQ 324
Cdd:pfam11559  51 LEFRESLNETIRTLeaeierLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKL--KNEKEE--LQRLKNALQQ 126

                          90       100       110
                  ....*....|....*....|....*....|....
gi 146134435  325 veqnlelmtkRAVKAENHVLKLKQEINLLQAQLS 358
Cdd:pfam11559 127 ----------IKTQFAHEVKKRDREIEKLKERLA 150
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-403 8.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 8.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 260 RHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEEsdfhdlesvVQQVEQNLELMTKRAVKA 339
Cdd:COG4717   81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE---------LEALEAELAELPERLEEL 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146134435 340 ENHVLKLKQ---EINLLQAQLSNLRRE-NEALRSGQGASLSVVKQNTDvALQNLHLVMNSAHASIKQL 403
Cdd:COG4717  152 EERLEELREleeELEELEAELAELQEElEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEA 218
PRK12704 PRK12704
phosphodiesterase; Provisional
 266-371 9.48e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146134435 266 QISYEALKDENSKLRRKLNEVQsfsetqtEMVRTLERKLEAKMIKEESDFHDLESVVQQVEQNLELMTKRAVKAENHVLK 345
Cdd:PRK12704  42 RILEEAKKEAEAIKKEALLEAK-------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114

                         90       100
                 ....*....|....*....|....*.
gi 146134435 346 LKQEINLLQAQLSNLRRENEALRSGQ 371
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQ 140
 
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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