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Conserved domains on  [gi|422010823|ref|NP_001258701|]
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ski-like protein isoform c [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 54-153 3.70e-67

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


:

Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.13  E-value: 3.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  54 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 133
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 422010823 134 SCGLITLTDAQRLCNALLRP 153
Cdd:cd21084   81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 178-273 5.17e-58

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.


:

Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.96  E-value: 5.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   178 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 257
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 422010823   258 EKKLKIILEEMKEKFS 273
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 401-540 5.79e-09

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: 58.91  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 480
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   481 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 54-153 3.70e-67

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.13  E-value: 3.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  54 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 133
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 422010823 134 SCGLITLTDAQRLCNALLRP 153
Cdd:cd21084   81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 178-273 5.17e-58

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.


Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.96  E-value: 5.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   178 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 257
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 422010823   258 EKKLKIILEEMKEKFS 273
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 178-272 5.59e-56

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4


Pssm-ID: 462602  Cd Length: 94  Bit Score: 182.85  E-value: 5.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  178 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 257
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 422010823  258 EKKLKIILEEMKEKF 272
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 53-152 3.00e-48

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 162.45  E-value: 3.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   53 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 132
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 422010823  133 PSCGLITLTDAQRLCNALLR 152
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 401-540 5.79e-09

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: 58.91  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 480
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   481 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-540 2.92e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  401 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 472
Cdd:COG4913   595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823  473 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4913   671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 407-541 2.11e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.60  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 486
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422010823 487 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 541
Cdd:PRK00409 580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 389-537 1.09e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.57  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 389 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 466
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823 467 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 537
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 404-540 2.23e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  404 VRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDL----EKKLEQVMQQK 479
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823  480 CTcdSTLEKDREAEYAAQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 425-535 1.37e-04

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   425 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 504
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 422010823   505 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 535
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 54-153 3.70e-67

Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like protein, also known as SKIL, Ski-related oncogene (Sno), or Ski-related protein, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.13  E-value: 3.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  54 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 133
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 422010823 134 SCGLITLTDAQRLCNALLRP 153
Cdd:cd21084   81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 178-273 5.17e-58

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4.


Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.96  E-value: 5.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   178 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 257
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 422010823   258 EKKLKIILEEMKEKFS 273
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 178-272 5.59e-56

c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through interaction with Smad proteins. This domain binds to Smad4


Pssm-ID: 462602  Cd Length: 94  Bit Score: 182.85  E-value: 5.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  178 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 257
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 422010823  258 EKKLKIILEEMKEKF 272
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 61-151 2.68e-53

Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410782  Cd Length: 91  Bit Score: 175.45  E-value: 2.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  61 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 140
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                         90
                 ....*....|.
gi 422010823 141 TDAQRLCNALL 151
Cdd:cd21079   81 TDAERLCSALL 91
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 54-151 7.94e-49

Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410786  Cd Length: 102  Bit Score: 164.09  E-value: 7.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  54 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 133
Cdd:cd21083    3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                         90
                 ....*....|....*...
gi 422010823 134 SCGLITLTDAQRLCNALL 151
Cdd:cd21083   83 SCGLITKTDAERLCNALL 100
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 53-152 3.00e-48

SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. All members of this family contain a conserved CLPQ motif. The c-ski proto-oncogene has been shown to influence proliferation, morphological transformation and myogenic differentiation. Sno, a Ski proto-oncogene homolog, is expressed in two isoforms and plays a role in the response to proliferation stimuli. Dachshund also contains this domain. It is involved in various aspects of development.


Pssm-ID: 460558  Cd Length: 100  Bit Score: 162.45  E-value: 3.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   53 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 132
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 422010823  133 PSCGLITLTDAQRLCNALLR 152
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 61-148 6.23e-34

Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. Members of this family include the Ski protein, Ski-like protein (Sno), and Dachshund proteins. Ski may play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. It functions as a repressor of transforming growth factor-beta (TGF-beta) signaling. Ski-like protein, also known as SKIL or Sno, is the ski proto-oncogene homolog. It may have regulatory roles in cell division or differentiation in response to extracellular signals. Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development.


Pssm-ID: 410781  Cd Length: 88  Bit Score: 123.56  E-value: 6.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  61 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 140
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                 ....*...
gi 422010823 141 TDAQRLCN 148
Cdd:cd21074   81 SDAERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 61-151 3.87e-16

Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and similar proteins; Skor1, also known as functional Smad-suppressing element on chromosome 15 (Fussel-15), LBX1 corepressor 1, or ladybird homeobox corepressor 1, acts as a transcriptional corepressor of LBX1 and inhibits BMP signaling. Skor2, also known as functional Smad-suppressing element on chromosome 18 (Fussel-18), LBX1 corepressor 1-like protein, or ladybird homeobox corepressor 1-like protein, exhibits transcriptional repressor activity. It acts as a transforming growth factor-beta (TGF-beta) antagonist in the nervous system. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410783  Cd Length: 91  Bit Score: 73.63  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  61 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 140
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                         90
                 ....*....|.
gi 422010823 141 TDAQRLCNALL 151
Cdd:cd21080   81 REAERLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 401-540 5.79e-09

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: 58.91  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 480
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   481 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
401-540 2.92e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  401 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 472
Cdd:COG4913   595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823  473 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4913   671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
405-539 5.66e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmEEFYIEQRDLEK---KLEQVMQQKCT 481
Cdd:COG4717  106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAelaELQEELEELLE 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 482 CDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 539
Cdd:COG4717  185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
413-530 1.88e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  413 ILQRKQQLQmevEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEKDREA 492
Cdd:COG4913   670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 422010823  493 EYAAQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 530
Cdd:COG4913   743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 405-540 3.05e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKctcds 484
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----- 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 485 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 390-541 4.19e-07

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: 53.15  E-value: 4.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   390 DDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 469
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI------QELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823   470 KKLEqvmqqkctcdstlekdreaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE-------MMIKELKLQIG 541
Cdd:TIGR02169  868 EELE-------------------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLE 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 403-540 1.25e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   403 YVRQQEKLNSILQRKQQL--QMEVEMLSSSKAMKELTEEQQNLQKELESLQSE---HAQRMEEFYIEQRDLEKKLEQVMQ 477
Cdd:TIGR02168  251 AEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823   478 QKcTCDSTLEKDREAEYA---AQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR02168  331 KL-DELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
400-540 1.32e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  400 MRTYVRQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQ----RMEEFYIEQRDLEKKLEQV 475
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLE--AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER 357

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422010823  476 ------MQQKC-TCDSTLEKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4913   358 errrarLEALLaALGLPLPASAE-EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
407-547 1.38e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQS----EH--AQRMEEfyiEQRDLEKKLEQVMQQKc 480
Cdd:COG3206  239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpNHpdVIALRA---QIAALRAQLQQEAQRI- 314

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 422010823 481 tcDSTLEKD------REAEYAAQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQIGKSSKPS 547
Cdd:COG3206  315 --LASLEAElealqaREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
407-540 1.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 486
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEELEERLEELRELEEELEELEAEL----AEL 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 422010823 487 EKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 407-541 2.11e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.60  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 486
Cdd:PRK00409 515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422010823 487 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 541
Cdd:PRK00409 580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 403-528 2.38e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.77  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 403 YVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNL--QKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKc 480
Cdd:COG1579   47 LEAAKTELEDLEKEIKRLELEIE--EVEARIKKYEEQLGNVrnNKEYEALQKE----IESLKRRISDLEDEILELMERI- 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 422010823 481 tcdSTLEKDREAEyAAQLAELRQRLDHAEADRQELQDELRQEREARQK 528
Cdd:COG1579  120 ---EELEEELAEL-EAELAELEAELEEKKAELDEELAELEAELEELEA 163
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 424-530 2.84e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 424 VEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekdreAEYAAQLAELR 502
Cdd:COG3883  121 LSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLS 188

                         90       100
                 ....*....|....*....|....*...
gi 422010823 503 QRLDHAEADRQELQDELRQEREARQKLE 530
Cdd:COG3883  189 AEEAAAEAQLAELEAELAAAEAAAAAAA 216
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 405-540 3.91e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLssSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQVMQqkctcds 484
Cdd:COG1196  324 ELAELEEELEELEEELEELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAE----AEEELEELAEELLE------- 390

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 485 tlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG1196  391 --ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 405-545 4.81e-06

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: 48.99  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQR--------------DLEK 470
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVR 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 471 K---LEQVMQQKctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 545
Cdd:COG4942  137 RlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 76-148 5.18e-06

Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar proteins; SKIDA1 is also known as protein DLN-1. Its biological function remains unclear. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA.


Pssm-ID: 410785  Cd Length: 91  Bit Score: 45.03  E-value: 5.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823  76 VGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCN 148
Cdd:cd21082   16 INGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDVERLYS 88
mukB PRK04863
chromosome partition protein MukB;
363-547 6.83e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 6.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  363 SAVCSLVRGTSKRDSEDSSPLLVRDGEDDKgkiMEDVMRTYVRQQekLNSILQRKQQLQMEVEMLSS----SKAMKELTE 438
Cdd:PRK04863  480 QLVRKIAGEVSRSEAWDVARELLRRLREQR---HLAEQLQQLRMR--LSELEQRLRQQQRAERLLAEfckrLGKNLDDED 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  439 EQQNLQKELESLQSEHAQRMEEFyIEQR-DLEKKLEQVMQQKctcdSTLEKDREAEYAAQ--LAELRQRLDHAEADR--- 512
Cdd:PRK04863  555 ELEQLQEELEARLESLSESVSEA-RERRmALRQQLEQLQARI----QRLAARAPAWLAAQdaLARLREQSGEEFEDSqdv 629

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 422010823  513 ----QELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 547
Cdd:PRK04863  630 teymQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 431-540 8.60e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 431 KAMKELTEEQQNLQ----------KELESL--QSEHAQRmeefYIEQRDLEKKLEQVMQqkctcdstLEKDREAEyaAQL 498
Cdd:COG1196  176 EAERKLEATEENLErledilgeleRQLEPLerQAEKAER----YRELKEELKELEAELL--------LLKLRELE--AEL 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 422010823 499 AELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
401-537 9.17e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQvmqqkc 480
Cdd:COG4717  395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE----ELAELEAELEQ------ 464

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422010823 481 tcdstLEKDREaeyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 537
Cdd:COG4717  465 -----LEEDGE------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
389-537 9.58e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 9.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 389 EDDKGKIME-------DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEF 461
Cdd:PRK03918 447 EEHRKELLEeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 462 YieqRDLEKKLEQVMQQKctcdSTLEKD--REAEYAAQLAELRQRLDHAEADRQELQDELRQER-EARQKLEMMIKELK 537
Cdd:PRK03918 527 Y---EKLKEKLIKLKGEI----KSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 389-537 1.09e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.57  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 389 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 466
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823 467 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 537
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 398-530 1.21e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 48.41  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  398 DVMRTYVRQQEKLNSILQRKQQLQMEvemlssskamkeLTEEQQNL--QKELESLQSEHAQRMEEFYIEQRDLEKKLEQV 475
Cdd:COG3096   495 QTARELLRRYRSQQALAQRLQQLRAQ------------LAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422010823  476 MQQKCTCDSTLEKDREaeyaaQLAELRQRLDHAEADRQELQDELRQEREARQKLE 530
Cdd:COG3096   563 EAQLEELEEQAAEAVE-----QRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 424-535 1.23e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 424 VEMLSSSKAMKELTEEQQNLQKELESLQSE----HAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 499
Cdd:COG0542  404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEEIQ 474

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 422010823 500 ELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 535
Cdd:COG0542  475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 388-530 1.60e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.49  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 388 GEDDKGKIMED---VMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIE 464
Cdd:PRK09510  46 GGSVIDAVMVDpgaVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 465 QRDLEKKLEQVMQQKCTCDSTL----EKDREAEYAAQLAELRQRLDHAEADRQelqdelrQEREARQKLE 530
Cdd:PRK09510 126 QAALKQKQAEEAAAKAAAAAKAkaeaEAKRAAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
PRK11637 PRK11637
AmiB activator; Provisional
 407-549 1.64e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 47.38  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEvemlssskamKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEqvmqqkctcdSTL 486
Cdd:PRK11637 169 QETIAELKQTREELAAQ----------KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLE----------SSL 228

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 487 EKDReaeyaAQLAELRQ---RLDHAEAdRQELQDELRQEREAR--QKLEMMIKELKlQIGKSSKPSKD 549
Cdd:PRK11637 229 QKDQ-----QQLSELRAnesRLRDSIA-RAEREAKARAEREAReaARVRDKQKQAK-RKGSTYKPTES 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 397-540 1.81e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 397 EDVMRTYVRQQEKLnsilqRKQqlqmevemlsSSKAMK--ELTEEQQNLQKELESLQSEHAQRMEEFYIEQRD-LEKKLE 473
Cdd:COG1196  192 EDILGELERQLEPL-----ERQ----------AEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEeLEAELE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 474 QVMQQKCTCDSTLEKDR----------------EAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 537
Cdd:COG1196  257 ELEAELAELEAELEELRleleeleleleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336


                 ...
gi 422010823 538 LQI 540
Cdd:COG1196  337 EEL 339
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 404-540 2.23e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  404 VRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDL----EKKLEQVMQQK 479
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823  480 CTcdSTLEKDREAEYAAQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 389-540 2.47e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  389 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEV-EMLSSSKAMKELTEEQQNLQKE-LESLQSEHAQRMEEFYIEQR 466
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 422010823  467 DLEKKLEQVMQQKCTcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:pfam13868 177 EIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 407-536 2.83e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 46.75  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQL--QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEF------YI-------EQRDLEKK 471
Cdd:PRK04778 281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 472 LEQVMQQkctcdstLEKDREA---------EYAAQLAELRQRLDHAEADRQELQDELRQ----EREARQKLEMMIKEL 536
Cdd:PRK04778 357 LESLEKQ-------YDEITERiaeqeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKL 427
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 409-549 2.85e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  409 KLNSIL--QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmeefyieQRDLEKKLEQVMQQKCTCDSTL 486
Cdd:TIGR04523 311 ELKSELknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK-------QRELEEKQNEIEKLKKENQSYK 383

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823  487 EKDREAEyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD 549
Cdd:TIGR04523 384 QEIKNLE--SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 394-542 2.91e-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: 46.98  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   394 KIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 473
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE--LEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRD 353

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823   474 QVMqqkctcdstlekDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGK 542
Cdd:TIGR02169  354 KLT------------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 405-542 3.52e-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: 46.97  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   405 RQQEKLNSILQRKQQLQMEVEMLSSSK-----AMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQK 479
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELE-ELEAELEELESRLEELEEQLETL 384

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823   480 CTcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMmiKELKLQIGK 542
Cdd:TIGR02168  385 RS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEE 444
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 407-543 4.76e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  407 QEKLNSILQRKQQL--QMEVEMLS----------SSKAMKELTEEQQNLQKELESLQseHAQRMEEFYIE-QRDLEKKLE 473
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  474 QVMQQkctCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQELQDELR----QEREARQKLEMMIKEL---KLQIG 541
Cdd:pfam06160 340 ELEKR---YDEIVERLEEkevaySELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVE 416


                  ..
gi 422010823  542 KS 543
Cdd:pfam06160 417 KS 418
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 406-548 5.71e-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: 45.53  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 406 QQEKLNSILQRK--QQLQMEVEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQrmeefyiEQRDLEKKLEQVMQQKctc 482
Cdd:COG4942  118 RQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA-------ERAELEALLAELEEER--- 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 483 dstlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSK 548
Cdd:COG4942  188 ---------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 405-536 6.51e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRME-EFYIEQRDLEKKLEQVMQQKCTCD 483
Cdd:COG1196  666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEElEEEALEEQLEAEREELLEELLEEE 745

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 484 STLEKDREAEYA--AQLAELRQRLDHAEADRQEL-----------------QDELRQER----EARQKLEMMIKEL 536
Cdd:COG1196  746 ELLEEEALEELPepPDLEELERELERLEREIEALgpvnllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
407-545 6.56e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKctcdSTL 486
Cdd:COG4372   44 QEELEQLREELEQAREELE--QLEEELEQARSELEQLEEELEELNEQ----LQAAQAELAQAQEELESLQEEA----EEL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 487 EKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 545
Cdd:COG4372  114 QEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
407-540 7.04e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstl 486
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ------- 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 422010823 487 ekdreaeyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4372  101 ---------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
PRK12704 PRK12704
phosphodiesterase; Provisional
 407-540 7.20e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQrkqQLQMEVEMLSSsKAMKELTEEQQNLQKELESlqsEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 486
Cdd:PRK12704  37 EEEAKRILE---EAKKEAEAIKK-EALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKL----ELL 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 422010823 487 EKdREAEYAAQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELKLQI 540
Cdd:PRK12704 106 EK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEARHEA 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 394-542 8.07e-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: 45.83  E-value: 8.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   394 KIMEDVMRTYVRQQEKLNSILQRKQ----QLQMEVEMLSSSKAMkeltEEQQNLQKELESLQSEHaQRMEEfyiEQRDLE 469
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEELEedlhKLEEALNDLEARLSH----SRIPEIQAELSKLEEEV-SRIEA---RLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   470 KKLEQVMQQKCTCDSTLE---------KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQelqeqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898


                   ..
gi 422010823   541 GK 542
Cdd:TIGR02169  899 RE 900
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 406-531 8.38e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.33  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  406 QQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdST 485
Cdd:pfam15709 382 QQRRFEEIRLRKQRLEEERQ---------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER----AE 448

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 422010823  486 LEKDREAEYAAQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 531
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 390-542 8.45e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 8.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 390 DDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 469
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELE--ALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 470 K------------------KLEQVMQQKctcDSTLE--KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKL 529
Cdd:COG3883  104 YldvllgsesfsdfldrlsALSKIADAD---ADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180

                        170
                 ....*....|...
gi 422010823 530 EMMIKELKLQIGK 542
Cdd:COG3883  181 EALLAQLSAEEAA 193
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
439-536 9.47e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 439 EQQNLQKELESLQSEHAQRMEEfyIEQrdLEKKLEQVMQQKCTCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQ 513
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEE--IER--YEEQREQARETRDEADEVLEEHEErreelETLEAEIEDLRETIAETERERE 275

                         90       100
                 ....*....|....*....|...
gi 422010823 514 ELQDELRQEREARQKLEMMIKEL 536
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEERDDL 298
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 374-540 9.50e-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: 9.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   374 KRDSEDSSPLLVRDGEDDKGKI--MEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ 451
Cdd:TIGR02169  282 KDLGEEEQLRVKEKIGELEAEIasLERSIAEKERELEDAE-----ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   452 SEHAQRMEEFyieqRDLEKKLEQVmqqkctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEM 531
Cdd:TIGR02169  357 EEYAELKEEL----EDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ....*....
gi 422010823   532 MIKELKLQI 540
Cdd:TIGR02169  421 ELADLNAAI 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
408-537 1.27e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 408 EKLNSILQRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQ----------SEHAQRMEEFYIEQRDLEKKLEQV- 475
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEvKELEELKEEIEELEKELESLEgskrkleekiRELEERIEELKKEIEELEEKVKELk 286

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823 476 -MQQKCTCDSTLEKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 537
Cdd:PRK03918 287 eLKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 391-537 1.28e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 44.20  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  391 DKGKIMEDVMRTYVRQQEKL-NSILQRKQQLqmeVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 469
Cdd:pfam02841 169 RKGVKAEEVLQEFLQSKEAVeEAILQTDQAL---TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHV 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823  470 KKLEQVMqqkctcdstlekdrEAEYAAQLAELRQRLDHaeaDRQELQDELRQEREAR-QKLEMMIKELK 537
Cdd:pfam02841 246 KQLIEKM--------------EAEREQLLAEQERMLEH---KLQEQEELLKEGFKTEaESLQKEIQDLK 297
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 425-535 1.37e-04

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   425 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 504
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 422010823   505 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 535
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 397-530 1.61e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 397 EDVMRTYVRQQEKLNSILQ--RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ---SEHAQRMEEFYIEQRDLEKK 471
Cdd:COG1196  252 EAELEELEAELAELEAELEelRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEE 331

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823 472 LEQvmqqkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDEL----RQEREARQKLE 530
Cdd:COG1196  332 LEE------------LEEELEELEEELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELE 382
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 398-540 2.30e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.17  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  398 DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKA-----MKELtEEQQNLQKELES-LQ--SEHAQRMEEFYIEQrdle 469
Cdd:COG3096   272 DYMRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQ---- 346

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823  470 KKLEQvmqqkctcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG3096   347 EKIER-------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
414-537 2.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 414 LQRKQQLQMEVEMLSSSKAMKELTEEQQNLqkelesLQSEHAQRMEEFYI------EQRDLEKKLEQVMQQkctCDSTLE 487
Cdd:COG4717  346 IEELQELLREAEELEEELQLEELEQEIAAL------LAEAGVEDEEELRAaleqaeEYQELKEELEELEEQ---LEELLG 416

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 422010823 488 KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 537
Cdd:COG4717  417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 396-537 2.44e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  396 MEDVMRTYVRQQEKLNSILQ-----RKQQLQMEVEMLSSSKAMKEL----TEEQQNLQKELESLQSEHAQRMEEFYIEQR 466
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMeqirAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 422010823  467 DLEKKLEQVMQQkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA----RQKLEMMIKELK 537
Cdd:pfam17380 457 ERQQQVERLRQQ--------EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieeERKRKLLEKEME 523
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
443-542 2.59e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  443 LQKELESLQSEHAqrmeEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDRE----AEYAAQLAEL---RQRLDHAEADRQEL 515
Cdd:COG4913   615 LEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDeidvASAEREIAELeaeLERLDASSDDLAAL 690

                          90       100
                  ....*....|....*....|....*..
gi 422010823  516 QDELRQEREARQKLEMMIKELKLQIGK 542
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGR 717
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 426-532 2.67e-04

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 43.05  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  426 MLSSSKAMKELTEEqqnLQKELESLQSEHAQRMEEF--YIEQRDLEKKleQVM---QQKCTCDSTLEKDREAEYAAQLAe 500
Cdd:pfam12037  37 ELESSPHAKKALEL---MKKQEQTRQAELQAKIKEYeaAQEQLKIERQ--RVEyeeRRKTLQEETKQKQQRAQYQDELA- 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 422010823  501 lRQRL-DHAEADRQELQDELRQEREARQKLEMM 532
Cdd:pfam12037 111 -RKRYqDQLEAQRRRNEELLRKQEESVAKQEAM 142
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 425-535 3.08e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 41.75  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 425 EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDlEKKLEQVMQQKctcdstlekdREAEYAAQLAELRQR 504
Cdd:COG2825   37 ESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKL---QKE-AATLSEEERQK----------KERELQKKQQELQRK 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 422010823 505 ldhaeadRQELQDELRQER-EARQKLEMMIKE 535
Cdd:COG2825  103 -------QQEAQQDLQKRQqELLQPILEKIQK 127
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 404-525 3.18e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   404 VRQQEKLNSILQRKQQLQMEVEMLS---SSKAMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQkc 480
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLkklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA-- 479

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 422010823   481 tcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREA 525
Cdd:TIGR02168  480 -------------AERELAQLQARLDSLERLQENLEGFSEGVKAL 511
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 413-547 3.24e-04

Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 41.82  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  413 ILQRKQQLQMeveMLSSSKAMKELTEEQQnlQKELESLQSEHAQRMEEfyIEQRDLEKKleqVMQQKCTCDS---TLEKD 489
Cdd:pfam13870  15 LITLKHTLAK---IQEKLEQKEELGEGLT--MIDFLQLQIENQALNEK--IEERNKELK---RLKLKVTNTVhalTHLKE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823  490 REAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 547
Cdd:pfam13870  85 KLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGLLHVPA 142
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
405-541 4.58e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDS 484
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422010823 485 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIG 541
Cdd:COG4372  176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
401-535 4.71e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKE--------LTEEQQNLQKELESLQSEHAQRMEEF-----YIEQRD 467
Cdd:COG4717  350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleQAEEYQELKEELEELEEQLEELLGELeelleALDEEE 429

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 468 LEKKLEQVMQQKctcdSTLEKDREaEYAAQLAELRQRLDHAEADRqELQDELRQEREARQKLEMMIKE 535
Cdd:COG4717  430 LEEELEELEEEL----EELEEELE-ELREELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEE 491
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-537 4.92e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 389 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEhaqrmeefyIEqrDL 468
Cdd:COG2433  387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELEEKDER---------IE--RL 446

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 469 EKKLEQVMQQKctcDSTLEKDREAeyaaqlaelrQRLDhAEADRqeLQDELRQEREARQKLEMMIKELK 537
Cdd:COG2433  447 ERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEEERERIEELKRKLERLK 499
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 396-540 4.98e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 396 MEDVMRTYVRQQE---KLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKL 472
Cdd:COG1579    2 MPEDLRALLDLQEldsELDRLEHRLKELPAELA---------ELEDELAALEARLEAAKTEL----EDLEKEIKRLELEI 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 473 EQVMQQkctcdstLEKDREA--------EYAAQLAELrqrlDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG1579   69 EEVEAR-------IKKYEEQlgnvrnnkEYEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
370-530 5.00e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 370 RGTSKRDSEDSSPLLVR--DGEDDKGKIMEDVMRTYVRQQEKLNSIlqrkQQLQMEVEMLSSSKamKELTEEQQNLQKEL 447
Cdd:PRK02224 299 LAEAGLDDADAEAVEARreELEDRDEELRDRLEECRVAAQAHNEEA----ESLREDADDLEERA--EELREEAAELESEL 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 448 ESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELrqeREA 525
Cdd:PRK02224 373 EEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELREREAELEATLRTARERV---EEA 445


                 ....*
gi 422010823 526 RQKLE 530
Cdd:PRK02224 446 EALLE 450
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 390-540 5.62e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   390 DDKGKIMEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQK---ELESLQSEHAQRMEEFYIEQR 466
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSKlknKHEAMISDLEERLKKEEKGRQ 204

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 422010823   467 DLEKkleqvMQQKCTCDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:pfam01576  205 ELEK-----AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 389-537 5.66e-04

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 41.57  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  389 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKE--LTEEQQNLQKELES---LQSEHAQRMEEFYI 463
Cdd:pfam15665  24 EEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  464 E----QRDLEKKLEQVMQQKctcdSTLEKDRE-------AEYAAQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQ 527
Cdd:pfam15665 104 EveeaKRAFEEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRK 179

                         170
                  ....*....|
gi 422010823  528 KLEMMIKELK 537
Cdd:pfam15665 180 EVEDLRKEKK 189
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
407-545 5.88e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  407 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHA------QRMEEFYIEQRDLEKKLEQVMQQKc 480
Cdd:COG4913   637 EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELDELKGEI- 715

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823  481 tcdSTLEKDREaEYAAQLAELRQRLDHAEAD-----RQELQDELRQ------EREARQKLEMMIKELKLQIGKSSK 545
Cdd:COG4913   716 ---GRLEKELE-QAEEELDELQDRLEAAEDLarlelRALLEERFAAalgdavERELRENLEERIDALRARLNRAEE 787
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
408-542 6.49e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 6.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 408 EKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQV--MQQkcTCDST 485
Cdd:COG1340   57 EEAQELREKRDELNEKVKELKEER--DELNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIERLewRQQ--TEVLS 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422010823 486 LEKDRE-----AEYAAQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKELKLQIGK 542
Cdd:COG1340  132 PEEEKElvekiKELEKELEKAKKALEKNE-KLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 405-500 6.54e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 483
Cdd:COG3883  130 ADADLLEELKADKAELEAKKAELEAKLAeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209

                         90
                 ....*....|....*..
gi 422010823 484 STLEKDREAEYAAQLAE 500
Cdd:COG3883  210 AAAAAAAAAAAAAAAAA 226
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
405-521 6.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  405 RQQEKLNSILQRKQQLQMEVEML------SSSKAMKELTEEQQNLQKELESLQSEHAQRME-------EFYIEQRDLEKK 471
Cdd:COG4913   306 RLEAELERLEARLDALREELDELeaqirgNGGDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAAL 385

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 422010823  472 LEQVMQQKctcdsTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQ 521
Cdd:COG4913   386 RAEAAALL-----EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 407-545 6.86e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   407 QEKLNSILQRKQQLQMEVEMLSSskAMKELTEEQQNLQKELESLQSEHAQ---RMEEFYIEQRDLEKKLEQVMQQKctcd 483
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEEAANlreRLESLERRIAATERRLEDLEEQI---- 847

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 422010823   484 stlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 545
Cdd:TIGR02168  848 --------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 68-146 7.85e-04

Dachshund-homology domain found in the retinal determination protein Dachshund and similar proteins; Dachshund proteins act as transcription factors involved in the regulation of organogenesis. They may be a regulator of SIX1, SIX6 and probably SIX5. The Dachshund-homology domain (DHD), also known as the N-terminal Ski/Sno/Dac domain, adopts a mixed alpha/beta structure containing a helix-turn-helix motif, similar to features found in the forkhead/winged-helix family of DNA binding proteins. It contains a conserved CLPQ motif and can bind co-factors. Its structure suggests that it may also bind DNA. It has been postulated that Dachshund proteins may bind to chromatin DNA via their DHD domains.


Pssm-ID: 410784  Cd Length: 95  Bit Score: 38.88  E-value: 7.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  68 GESISCFQVGGEKRLCLPQVLNSVLREF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 145
Cdd:cd21081   10 GAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                 .
gi 422010823 146 L 146
Cdd:cd21081   90 L 90
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
401-525 8.27e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 41.98  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 401 RTYVRQQEKLNSILQRKQQLQMEVEMLSSskAMKELTE------EQQNLQKELESLQseHAQR--------MEEFYIEQR 466
Cdd:COG0497  165 RAWRALKKELEELRADEAERARELDLLRF--QLEELEAaalqpgEEEELEEERRRLS--NAEKlrealqeaLEALSGGEG 240

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 467 DLEKKLEQVMQQkctcdstLEkdREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA 525
Cdd:COG0497  241 GALDLLGQALRA-------LE--RLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
DUF4175 pfam13779
Domain of unknown function (DUF4175);
406-535 9.10e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.28  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  406 QQEklnsILQRKQQLQ--MEvemlsssKAMKELTEEQQNLQKELESLQSEHAQRMeefyiEQRDLEKKLEQvMQQKctcd 483
Cdd:pfam13779 508 DEE----IAKLMQELReaLD-------DYMQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRMLDR-IEEL---- 566

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 422010823  484 stLEKDREAEYAAQLAELRQRLDHAE-ADRQELQDELRQE-REARQKLEMMIKE 535
Cdd:pfam13779 567 --ARSGRRAEAQQMLSQLQQMLENLQaGQPQQQQQQGQSEmQQAMDELGDLLRE 618
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 423-542 1.09e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  423 EVEMLSSSKAMKELTE---EQQNLQKELESLQSEHAQrMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 499
Cdd:COG3096   487 EVERSQAWQTARELLRryrSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQRI---------GQQLDAAEELE 556

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 422010823  500 ELRQRLdhaEADRQELQDELRQEREARQKLEMMIKELKLQIGK 542
Cdd:COG3096   557 ELLAEL---EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
437-545 1.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 437 TEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTLEKDREaeyaaQLAELRQRLDHAEADRQELQ 516
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKE-----EIEELEKELESLEGSKRKLE 258

                         90       100
                 ....*....|....*....|....*....
gi 422010823 517 DELRQEREARQKLEMMIKELKLQIGKSSK 545
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKE 287
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
407-540 1.39e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 407 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFYIEQR--DLEKKLEQVMQQKctcdS 484
Cdd:COG3206  151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGlvDLSEEAKLLLQQL----S 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 485 TLEKDReAEYAAQLAELRQRLDHAEADRQ-------------ELQDELRQEREARQKLEMM----------IKELKLQI 540
Cdd:COG3206  223 ELESQL-AEARAELAEAEARLAALRAQLGsgpdalpellqspVIQQLRAQLAELEAELAELsarytpnhpdVIALRAQI 300
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
438-540 1.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 438 EEQQNLQKELESLQSEHAQRmEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKdreAEYAAQLAELRQRLDHAEADRQELQ- 516
Cdd:COG4717   71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEK---LEKLLQLLPLYQELEALEAELAELPe 146

                         90       100
                 ....*....|....*....|....*.
gi 422010823 517 --DELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4717  147 rlEELEERLEELRELEEELEELEAEL 172
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
416-536 1.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 416 RKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkcTCDSTLEKDRE--AE 493
Cdd:PRK02224 322 RDEELRDRLE--ECRVAAQAHNEEAESLREDADDLEER-AEELRE---EAAELESELE-------EAREAVEDRREeiEE 388

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 422010823 494 YAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 536
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 416-539 1.84e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  416 RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFyieqrdlEKKLEQVMQQKCTCDSTLEKDREAEYA 495
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELR----KQLENY-------EKDKQSLKNLKARLKVLEKELKDLKWE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 422010823  496 AQLaeLRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQ 539
Cdd:pfam13851 108 HEV--LEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQ 152
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 404-545 1.89e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823   404 VRQQEKLNSILQRKQQLQMEVEMlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKlEQVMQQKCTcd 483
Cdd:pfam15921  428 VQRLEALLKAMKSECQGQMERQM-AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTA-- 503

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823   484 STLEKDREAEYA-AQLAELRQRLDhaeADRQELQdELRQEREARQKLEMMIKELKLQIGKSSK 545
Cdd:pfam15921  504 SLQEKERAIEATnAEITKLRSRVD---LKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDK 562
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 407-459 1.98e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 422010823  407 QEKLNSILQRKQQLQMEVEMLSSSKAmkELTEEQQNLQKELESLQSEHAQRME 459
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENE--ELKEEANELEEENQQLKQERNQWQE 60
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 423-521 2.46e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 423 EVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkctcdstlekdrEAEyaAQLAELR 502
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELE-----------------ALQ--AEIDKLQ 71

                         90
                 ....*....|....*....
gi 422010823 503 QRLDHAEADRQELQDELRQ 521
Cdd:COG3883   72 AEIAEAEAEIEERREELGE 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
359-538 2.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 359 KKSESAVCSLVRGTSKRDSEDSSplLVRDGEDDKGKIME-----DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAM 433
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKElekrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 434 KELtEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTC-------DSTLEKDREAEYAAQLAELRQRLD 506
Cdd:PRK03918 391 KEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRKELLEEYTAELKRIEKELK 469

                        170       180       190
                 ....*....|....*....|....*....|..
gi 422010823 507 HAEADRQELQDELRQEREARQKLEMMIKELKL 538
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKEL 501
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 420-547 2.62e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.13  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  420 LQMEVEMLSSSKAMkeLTEEQQNLQKELESLQSEhAQRMEEFYieQRDLEKKLEQVMQQKCTCDSTLEKDREAEyaAQLA 499
Cdd:pfam09787  45 LTLELEELRQERDL--LREEIQKLRGQIQQLRTE-LQELEAQQ--QEEAESSREQLQELEEQLATERSARREAE--AELE 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 422010823  500 ELRQRLDHAEadrqelqDELRQEREARQ----KLEMMIKELKLQIGKSSKPS 547
Cdd:pfam09787 118 RLQEELRYLE-------EELRRSKATLQsrikDREAEIEKLRNQLTSKSQSS 162
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 389-515 2.73e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.12  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  389 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSK-AMKELTEEQQNLQKELESLQSEHA---QRMEEFYIE 464
Cdd:pfam13851  42 EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqSLKNLKARLKVLEKELKDLKWEHEvleQRFEKVERE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422010823  465 QRDLEKKLEQVM---QQKCTCDST-LEKdreaeyaaQLAELRQRLDHAEADRQEL 515
Cdd:pfam13851 122 RDELYDKFEAAIqdvQQKTGLKNLlLEK--------KLQALGETLEKKEAQLNEV 168
46 PHA02562
endonuclease subunit; Provisional
 405-540 2.78e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSILQRKQQlqMEVEMLSSSKAMK----ELTEEQQNLQKELESlQSEHAQRMEEFYIeqrDLEKKLEQ-----V 475
Cdd:PHA02562 206 EQRKKNGENIARKQN--KYDELVEEAKTIKaeieELTDELLNLVMDIED-PSAALNKLNTAAA---KIKSKIEQfqkviK 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 422010823 476 MQQK---C-TCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKlemmIKELKLQI 540
Cdd:PHA02562 280 MYEKggvCpTCTQQISEgpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK----LLELKNKI 346
valS PRK05729
valyl-tRNA synthetase; Reviewed
 436-506 3.12e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 40.47  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 436 LTEEQQNLQKELESLQSEhaqrmeefyIEQrdLEKKL----------EQVMQQkctcdstlEKDREAEYAAQLAELRQRL 505
Cdd:PRK05729 809 VEAELARLEKELAKLEKE---------IER--VEKKLsnegfvakapEEVVEK--------EREKLAEYEEKLAKLKERL 869


                 .
gi 422010823 506 D 506
Cdd:PRK05729 870 A 870
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
405-540 3.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSIL-QRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHaqrmeEFYIEQRDLEKKLEQVmqqkctc 482
Cdd:PRK03918 310 REIEKRLSRLeEEINGIEERIKELEEKEErLEELKKKLKELEKRLEELEERH-----ELYEEAKAKKEELERL------- 377

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 483 dstleKDREAEYaaQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:PRK03918 378 -----KKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
PRK09039 PRK09039
peptidoglycan -binding protein;
405-516 3.31e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSIL----QRKQQLQMEVEMLSSSKAMKELTEEQ-QNLQKELESLQSEHAQRM--------EEFYIEQR----- 466
Cdd:PRK09039  60 SQIAELADLLslerQGNQDLQDSVANLRASLSAAEAERSRlQALLAELAGAGAAAEGRAgelaqeldSEKQVSARalaqv 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 422010823 467 -DLEKKLEQVMQQKCTCDSTLE--KDREAEYAAQLAELRQRLDHAEADR-QELQ 516
Cdd:PRK09039 140 eLLNQQIAALRRQLAALEAALDasEKRDRESQAKIADLGRRLNVALAQRvQELN 193
PRK09039 PRK09039
peptidoglycan -binding protein;
436-541 3.55e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 436 LTEEQQNLQKELESLQSEHAQRMEEFYIEQR---DLEKKLEQVMQQKctcdSTLEKDReAEYAAQLAELRQRLDHAEADR 512
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAELADLLSLERQgnqDLQDSVANLRASL----SAAEAER-SRLQALLAELAGAGAAAEGRA 118

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 422010823 513 QELQDELRQER----EARQKLEMM---IKELKLQIG 541
Cdd:PRK09039 119 GELAQELDSEKqvsaRALAQVELLnqqIAALRRQLA 154
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
433-540 3.64e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  433 MKELTEEQQNLQKELEslQSEHAQRMEEFYieqRDLEKKLEQVMQQKcTCDSTLEKDREAEyaaQLAELRQRLDHAEADR 512
Cdd:COG4913   234 FDDLERAHEALEDARE--QIELLEPIRELA---ERYAAARERLAELE-YLRAALRLWFAQR---RLELLEAELEELRAEL 304

                          90       100
                  ....*....|....*....|....*...
gi 422010823  513 QELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQI 332
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 410-472 3.72e-03

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 37.60  E-value: 3.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823 410 LNSILQR-KQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQS--EHAQRMEEFYIEQRDLEKKL 472
Cdd:cd14798    5 VSFLLEKlGELLEQEADLLSGVK------EEIESLKDELESMQAflKDADAKQDEDEELKDWVKQV 64
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
406-537 3.78e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 406 QQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQ-------SEHAQRMEEFY---IEQRDLEKKLEQV 475
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELE--KKLDELEEELAELLKELEELGfesveelEERLKELEPFYneyLELKDAEKELERE 617

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 476 MQQKCTCDSTLEKDRE---------------------------------------AEYA---AQLAELRQRLDHAEADRQ 513
Cdd:PRK03918 618 EKELKKLEEELDKAFEelaetekrleelrkeleelekkyseeeyeelreeylelsRELAglrAELEELEKRREEIKKTLE 697

                        170       180
                 ....*....|....*....|....
gi 422010823 514 ELQDELRQEREARQKLEMMIKELK 537
Cdd:PRK03918 698 KLKEELEEREKAKKELEKLEKALE 721
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
435-542 4.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  435 ELTEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQVMQQKCtcdSTLEKDREAEYAAQLAELRQRLDHAEADRQE 514
Cdd:COG4913   245 EDAREQIELLEPIRELAERYAAARER-LAELEYLRAALRLWFAQRR---LELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 422010823  515 LQDELRQEREARQK--------LEMMIKELKLQIGK 542
Cdd:COG4913   321 LREELDELEAQIRGnggdrleqLEREIERLERELEE 356
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 464-542 4.32e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823 464 EQRDLEKKLEQVMQQKctcdSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGK 542
Cdd:COG0542  412 ELDELERRLEQLEIEK----EALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
400-539 4.76e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.65  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 400 MRTYVRQqeKLNSILQR----KQQLQMEV-EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyieqrDLEKKLEQ 474
Cdd:COG1842    6 LSDIIRA--NINALLDKaedpEKMLDQAIrDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-------KWEEKARL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 475 vmqqkctcdsTLEKDREA---EYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 539
Cdd:COG1842   77 ----------ALEKGREDlarEALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 407-473 5.11e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 36.10  E-value: 5.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 422010823 407 QEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 473
Cdd:COG3074   10 EAKVQQAVDTIELLQMEVEELKEKN--EELEQENEELQSENEELQSEN----EQLKTENAEWQERIR 70
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 397-539 5.18e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  397 EDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKElTEEQQNLQKEleslQSEHAQRMEEfyieqrdlEKKLEQvm 476
Cdd:pfam15709 318 EDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRRE-QEEQRRLQQE----QLERAEKMRE--------ELELEQ-- 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823  477 qQKCTCDSTLEKDReaeyaaqLAELRQRLDHAEAdRQELQDELRQEREARQKLEMMIKELKLQ 539
Cdd:pfam15709 383 -QRRFEEIRLRKQR-------LEEERQRQEEEER-KQRLQLQAAQERARQQQEEFRRKLQELQ 436
PTZ00121 PTZ00121
MAEBL; Provisional
 336-549 5.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  336 ASQSKEATKAETNSSISNNSTSRKKSESAVCSLVRGT-SKRDSEDSSPLLVRDGEDDKG---KIMEDVMRTY-------V 404
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYeeekkmkA 1609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  405 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDS 484
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 422010823  485 TLEK-DREAEYAAQLAELRQRldhaEADRQELQDELRQEREARQ-KLEMMIKELKLQIGKSSKPSKD 549
Cdd:PTZ00121 1690 AAEAlKKEAEEAKKAEELKKK----EAEEKKKAEELKKAEEENKiKAEEAKKEAEEDKKKAEEAKKD 1752
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 407-541 5.32e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.01  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  407 QEKLNSILQRKQQLQMEVEMLSS---SKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDLEKKLEQVmqqkctcd 483
Cdd:pfam01442   3 EDSLDELSTYAEELQEQLGPVAQelvDRLEKETEALRERLQKDLEEVRAKLEPYLEEL---QAKLGQNVEEL-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 422010823  484 stlekdrEAEYAAQLAELRQRLdhaEADRQELQDELRQE-REARQKLEMMIKELKLQIG 541
Cdd:pfam01442  72 -------RQRLEPYTEELRKRL---NADAEELQEKLAPYgEELRERLEQNVDALRARLA 120
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 406-540 5.58e-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: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  406 QQEKLNSILQRKQQlqmevEMLSSSKAMKELTEEQQNLQKELESLQSEHAQR-MEEFYIEQRDLEKKLEQVMQQKCTCDS 484
Cdd:TIGR04523 261 EQNKIKKQLSEKQK-----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQNNK 335

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823  485 TLEKDREaeyaaQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 540
Cdd:TIGR04523 336 IISQLNE-----QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 394-505 5.62e-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: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 394 KIMEDVMRTYVRQQEKLNSILQRKQQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKL 472
Cdd:COG4942  150 EQAEELRADLAELAALRAELEAERAELEaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                         90       100       110
                 ....*....|....*....|....*....|...
gi 422010823 473 EQVMQQkctcdstLEKDREAEYAAQLAELRQRL 505
Cdd:COG4942  230 ARLEAE-------AAAAAERTPAAGFAALKGKL 255
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
405-540 5.98e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 405 RQQEKLNSI---LQRKQ--QLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieqrdlEKKLEQVMQQK 479
Cdd:COG4372   77 QLEEELEELneqLQAAQaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 422010823 480 ctcdstlekdreaeyAAQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQI 540
Cdd:COG4372  149 ---------------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA 196
PTZ00121 PTZ00121
MAEBL; Provisional
 386-535 6.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  386 RDGEDDKGKIMEDVMRT-YVRQQEKLNSIlqRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESL--QSEHAQRMEEFY 462
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAeELKKAEEENKI--KAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELK 1708

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 422010823  463 IEQRDLEKKLEQVMQQKCTCDSTLEK-DREAEYAAQLAElRQRLDHAEADR--QELQDELRQEREARQKLEMMIKE 535
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAE-EAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 376-544 6.31e-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: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  376 DSEDSSPLLVRDGEDDKGKiMEDVMRTYVRQQEKLNSiLQRKQQLQmevemlssSKAMKELTEEQQNLQKELESLQSEHA 455
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENK-MKDLTFLLEESRDKANQ-LEEKTKLQ--------DENLKELIEKKDHLTKELEDIKMSLQ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  456 QRMEefyiEQRDLEKKLEqvMQQKCTCDSTLEKDreaeyaAQLAEL-RQRLDHA------EADRQELQDELRQEREARQK 528
Cdd:pfam05483 307 RSMS----TQKALEEDLQ--IATKTICQLTEEKE------AQMEELnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEK 374

                         170
                  ....*....|....*.
gi 422010823  529 LEMMIKELKLQIGKSS 544
Cdd:pfam05483 375 NEDQLKIITMELQKKS 390
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 425-542 6.64e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  425 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKdREAEYAAQLAELRQR 504
Cdd:pfam03938  13 ESPEGKAAQAQLEKKFKKRQAELEAKQKE--------------LQKLYEELQKDGALLEEEREE-KEQELQKKEQELQQL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 422010823  505 ldhaeadRQELQDELRQER-EARQKLEMMIKELKLQIGK 542
Cdd:pfam03938  78 -------QQKAQQELQKKQqELLQPIQDKINKAIKEVAK 109
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
406-530 8.47e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 8.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 406 QQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELE----SLQSEHAQRMEEFYIEQRDLEKKLEQvmqqkct 481
Cdd:COG3064   23 AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqraaELAAEAAKKLAEAEKAAAEAEKKAAA------- 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 422010823 482 cdstlEKDREAEYAAQLAELRQRLDHAEADRQElQDELRQEREARQKLE 530
Cdd:COG3064   96 -----EKAKAAKEAEAAAAAEKAAAAAEKEKAE-EAKRKAEEEAKRKAE 138
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 394-535 8.75e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 38.02  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823 394 KIMEDVMRTYVRQQEKLNSIL---QRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 469
Cdd:cd07671   22 KDVEELLKQRAQAEERYGKELvqiARKAGGQTEINTLKASfDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 422010823 470 KKLEQVMQQ---------KCTCDSTL---EKDREAEYAAQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKE 535
Cdd:cd07671  102 KKYEAVMERvqkskvslyKKTMESKKtyeQRCREADEAEQTFERSSSTGNPK-QSEKSQNKAKQCRDAATEAERVYKQ 178
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 405-539 8.88e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 38.48  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  405 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 483
Cdd:pfam15558  17 HKEEQRMRELQQQAALAWEELRRRDQKRqETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRW 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422010823  484 STLEKDREA------EYAAQLAELR-----QRLDHAEADRQELQDE---LRQEREARQKLEMMIKELKLQ 539
Cdd:pfam15558  97 REQAEDQENqrqeklERARQEAEQRkqcqeQRLKEKEEELQALREQnslQLQERLEEACHKRQLKEREEQ 166
 
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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