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Conserved domains on  [gi|2168696491|ref|NP_001385487|]
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ski-like protein isoform a [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 ...
 134-233 2.45e-66

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: 212.90  E-value: 2.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696491 214 SCGLITLTDAQRLCNALLRP 233
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 ...
 258-353 3.66e-57

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: 188.35  E-value: 3.66e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696491  338 EKKLKIILEEMKEKFS 353
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 527-666 4.41e-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: 60.07  E-value: 4.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 606
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  607 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
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 ...
 134-233 2.45e-66

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: 212.90  E-value: 2.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696491 214 SCGLITLTDAQRLCNALLRP 233
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 ...
 258-353 3.66e-57

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: 188.35  E-value: 3.66e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696491  338 EKKLKIILEEMKEKFS 353
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 ...
 258-352 2.24e-55

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: 183.62  E-value: 2.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 2168696491 338 EKKLKIILEEMKEKF 352
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. ...
 133-232 1.45e-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: 165.14  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 133 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 2168696491 213 PSCGLITLTDAQRLCNALLR 232
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 527-666 4.41e-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: 60.07  E-value: 4.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 606
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  607 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
527-666 2.31e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  527 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 598
Cdd:COG4913    595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491  599 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4913    671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 515-666 1.93e-06

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: 50.30  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEV-EMLSSSKAMKELTEEQQNLQKE-LESLQSEHAQRMEEFYIEQR 592
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 593 DLEKKLEQVMQQKCTcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:pfam13868 177 EIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 533-667 2.52e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.98  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 612
Cdd:PRK00409  515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696491 613 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 667
Cdd:PRK00409  580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 515-663 4.12e-06

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: 49.11  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 592
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491 593 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 663
Cdd:cd16269   234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 551-661 6.59e-05

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: 43.34  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  551 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 630
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168696491  631 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 661
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 ...
 134-233 2.45e-66

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: 212.90  E-value: 2.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696491 214 SCGLITLTDAQRLCNALLRP 233
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 ...
 258-353 3.66e-57

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: 188.35  E-value: 3.66e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696491  338 EKKLKIILEEMKEKFS 353
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 ...
 258-352 2.24e-55

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: 183.62  E-value: 2.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 2168696491 338 EKKLKIILEEMKEKF 352
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 141-231 2.88e-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: 177.76  E-value: 2.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21079     1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                          90
                  ....*....|.
gi 2168696491 221 TDAQRLCNALL 231
Cdd:cd21079    81 TDAERLCSALL 91
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 134-231 1.06e-48

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: 166.01  E-value: 1.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21083     3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                          90
                  ....*....|....*...
gi 2168696491 214 SCGLITLTDAQRLCNALL 231
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. ...
 133-232 1.45e-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: 165.14  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 133 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 2168696491 213 PSCGLITLTDAQRLCNALLR 232
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 141-228 2.91e-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: 125.48  E-value: 2.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21074     1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                  ....*...
gi 2168696491 221 TDAQRLCN 228
Cdd:cd21074    81 SDAERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 141-231 2.44e-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: 74.40  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21080     1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                          90
                  ....*....|.
gi 2168696491 221 TDAQRLCNALL 231
Cdd:cd21080    81 REAERLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 527-666 4.41e-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: 60.07  E-value: 4.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 606
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  607 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
527-666 2.31e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  527 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 598
Cdd:COG4913    595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491  599 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4913    671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
531-665 2.92e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmEEFYIEQRDLEK---KLEQVMQQKCT 607
Cdd:COG4717   106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAelaELQEELEELLE 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 608 CDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 665
Cdd:COG4717   185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 456-667 1.08e-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: 55.46  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  456 EEQEKMDLKTSRELYSCLDSSISNNSTSRKKSESAVCSLVRGTSKRDSEDSSP--LLVRDGEDDKGKIMEDVMRTYVRQQ 533
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRIE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  534 EKLNSILQRKQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEqvmqqkctcdstle 613
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEI------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-------------- 871

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491  614 kdreaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE-------MMIKELKLQIG 667
Cdd:TIGR02169  872 -----ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLE 927
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
539-656 1.69e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  539 ILQRKQQLQmevEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEKDREA 618
Cdd:COG4913    670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2168696491  619 EYAAQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 656
Cdd:COG4913    743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 531-666 2.06e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKctcds 610
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----- 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491 611 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 529-654 7.33e-07

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: 50.69  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 529 YVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNL--QKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKc 606
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIE--EVEARIKKYEEQLGNVrnNKEYEALQKE----IESLKRRISDLEDEILELMERI- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2168696491 607 tcdSTLEKDREAEyAAQLAELRQRLDHAEADRQELQDELRQEREARQK 654
Cdd:COG1579   120 ---EELEEELAEL-EAELAELEAELEEKKAELDEELAELEAELEELEA 163
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
533-666 8.75e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 612
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEELEERLEELRELEEELEELEAEL----AEL 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 613 EKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4717   176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 529-666 9.95e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 9.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  529 YVRQQEKLNSILQRKQQL--QMEVEMLSSSKAMKELTEEQQNLQKELESLQSE---HAQRMEEFYIEQRDLEKKLEQVMQ 603
Cdd:TIGR02168  251 AEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491  604 QKcTCDSTLEKDREAEYA---AQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:TIGR02168  331 KL-DELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
526-666 1.06e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  526 MRTYVRQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQ----RMEEFYIEQRDLEKKLEQV 601
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLE--AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER 357

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696491  602 ------MQQKC-TCDSTLEKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4913    358 errrarLEALLaALGLPLPASAE-EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
533-673 1.87e-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: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQS----EH--AQRMEEfyiEQRDLEKKLEQVMQQKc 606
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpNHpdVIALRA---QIAALRAQLQQEAQRI- 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168696491 607 tcDSTLEKD------REAEYAAQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQIGKSSKPS 673
Cdd:COG3206   315 --LASLEAElealqaREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 515-666 1.93e-06

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: 50.30  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEV-EMLSSSKAMKELTEEQQNLQKE-LESLQSEHAQRMEEFYIEQR 592
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 593 DLEKKLEQVMQQKCTcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:pfam13868 177 EIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 533-667 2.52e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.98  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 612
Cdd:PRK00409  515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696491 613 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 667
Cdd:PRK00409  580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 531-666 2.77e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLssSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQVMQqkctcds 610
Cdd:COG1196   324 ELAELEEELEELEEELEELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAE----AEEELEELAEELLE------- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491 611 tlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG1196   391 --ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 531-671 3.54e-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: 49.76  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQR--------------DLEK 596
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVR 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 597 K---LEQVMQQKctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 671
Cdd:COG4942   137 RlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 156-228 3.89e-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: 45.41  E-value: 3.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 156 VGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCN 228
Cdd:cd21082    16 INGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDVERLYS 88
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 515-663 4.12e-06

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: 49.11  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 592
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491 593 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 663
Cdd:cd16269   234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
527-663 4.36e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQvmqqkc 606
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE----ELAELEAELEQ------ 464

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696491 607 tcdstLEKDREaeyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 663
Cdd:COG4717   465 -----LEEDGE------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 557-666 5.34e-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: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 557 KAMKELTEEQQNLQ----------KELESL--QSEHAQRmeefYIEQRDLEKKLEQVMQqkctcdstLEKDREAEyaAQL 624
Cdd:COG1196   176 EAERKLEATEENLErledilgeleRQLEPLerQAEKAER----YRELKEELKELEAELL--------LLKLRELE--AEL 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2168696491 625 AELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
515-663 6.20e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIME-------DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEF 587
Cdd:PRK03918  447 EEHRKELLEeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 588 YieqRDLEKKLEQVMQQKctcdSTLEKD--REAEYAAQLAELRQRLDHAEADRQELQDELRQER-EARQKLEMMIKELK 663
Cdd:PRK03918  527 Y---EKLKEKLIKLKGEI----KSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 550-656 6.58e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 550 VEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekdreAEYAAQLAELR 628
Cdd:COG3883   121 LSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLS 188

                          90       100
                  ....*....|....*....|....*...
gi 2168696491 629 QRLDHAEADRQELQDELRQEREARQKLE 656
Cdd:COG3883   189 AEEAAAEAQLAELEAELAAAEAAAAAAA 216
mukB PRK04863
chromosome partition protein MukB;
489-673 7.23e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 7.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  489 SAVCSLVRGTSKRDSEDSSPLLVRDGEDDKgkiMEDVMRTYVRQQekLNSILQRKQQLQMEVEMLSS----SKAMKELTE 564
Cdd:PRK04863   480 QLVRKIAGEVSRSEAWDVARELLRRLREQR---HLAEQLQQLRMR--LSELEQRLRQQQRAERLLAEfckrLGKNLDDED 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  565 EQQNLQKELESLQSEHAQRMEEFyIEQR-DLEKKLEQVMQQKctcdSTLEKDREAEYAAQ--LAELRQRLDHAEADR--- 638
Cdd:PRK04863   555 ELEQLQEELEARLESLSESVSEA-RERRmALRQQLEQLQARI----QRLAARAPAWLAAQdaLARLREQSGEEFEDSqdv 629

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2168696491  639 ----QELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 673
Cdd:PRK04863   630 teymQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 523-666 1.13e-05

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: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 523 EDVMRTYVRQQEKLnsilqRKQqlqmevemlsSSKAMK--ELTEEQQNLQKELESLQSEHAQRMEEFYIEQRD-LEKKLE 599
Cdd:COG1196   192 EDILGELERQLEPL-----ERQ----------AEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEeLEAELE 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 600 QVMQQKCTCDSTLEKDR----------------EAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 663
Cdd:COG1196   257 ELEAELAELEAELEELRleleeleleleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336


                  ...
gi 2168696491 664 LQI 666
Cdd:COG1196   337 EEL 339
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 524-656 1.20e-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: 48.80  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  524 DVMRTYVRQQEKLNSILQRKQQLQMEvemlssskamkeLTEEQQNL--QKELESLQSEHAQRMEEFYIEQRDLEKKLEQV 601
Cdd:COG3096    495 QTARELLRRYRSQQALAQRLQQLRAQ------------LAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2168696491  602 MQQKCTCDSTLEKDREaeyaaQLAELRQRLDHAEADRQELQDELRQEREARQKLE 656
Cdd:COG3096    563 EAQLEELEEQAAEAVE-----QRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 550-661 1.29e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.54  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 550 VEMLSSSKAMKELTEEQQNLQKELESLQSE----HAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 625
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEEIQ 474

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2168696491 626 ELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 661
Cdd:COG0542   475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 514-656 1.38e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 514 GEDDKGKIMED---VMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIE 590
Cdd:PRK09510   46 GGSVIDAVMVDpgaVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 591 QRDLEKKLEQVMQQKCTCDSTL----EKDREAEYAAQLAELRQRLDHAEADRQelqdelrQEREARQKLE 656
Cdd:PRK09510  126 QAALKQKQAEEAAAKAAAAAKAkaeaEAKRAAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
PRK11637 PRK11637
AmiB activator; Provisional
 533-675 1.55e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 47.77  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEvemlssskamKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEqvmqqkctcdSTL 612
Cdd:PRK11637  169 QETIAELKQTREELAAQ----------KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLE----------SSL 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 613 EKDReaeyaAQLAELRQ---RLDHAEAdRQELQDELRQEREAR--QKLEMMIKELKlQIGKSSKPSKD 675
Cdd:PRK11637  229 QKDQ-----QQLSELRAnesRLRDSIA-RAEREAKARAEREAReaARVRDKQKQAK-RKGSTYKPTES 289
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 533-662 1.90e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.91  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQL--QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEF------YI-------EQRDLEKK 597
Cdd:PRK04778  281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 598 LEQVMQQkctcdstLEKDREA---------EYAAQLAELRQRLDHAEADRQELQDELRQ----EREARQKLEMMIKEL 662
Cdd:PRK04778  357 LESLEKQ-------YDEITERiaeqeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKL 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 520-662 2.37e-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: 47.76  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  520 KIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 599
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE--LEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRD 353

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491  600 QVMqqkctcdstlekDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREarqKLEMMIKEL 662
Cdd:TIGR02169  354 KLT------------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREI 401
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 530-666 2.59e-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: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 530 VRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDL----EKKLEQVMQQK 605
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491 606 CTcdSTLEKDREAEYAAQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
533-671 2.62e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKctcdSTL 612
Cdd:COG4372    44 QEELEQLREELEQAREELE--QLEEELEQARSELEQLEEELEELNEQ----LQAAQAELAQAQEELESLQEEA----EEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 613 EKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 671
Cdd:COG4372   114 QEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 531-668 2.86e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  531 RQQEKLNSILQRKQQLQMEVEMLSSSK-----AMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQK 605
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELE-ELEAELEELESRLEELEEQLETL 384

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491  606 CTcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMmiKELKLQIGK 668
Cdd:TIGR02168  385 RS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEE 444
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
533-666 3.03e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstl 612
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ------- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 613 ekdreaeyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4372   101 ---------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 533-669 3.08e-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: 47.16  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQL--QMEVEMLS----------SSKAMKELTEEQQNLQKELESLQseHAQRMEEFYIE-QRDLEKKLE 599
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 600 QVMQQkctCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQELQDELR----QEREARQKLEMMIKEL---KLQIG 667
Cdd:pfam06160 340 ELEKR---YDEIVERLEEkevaySELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVE 416


                  ..
gi 2168696491 668 KS 669
Cdd:pfam06160 417 KS 418
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 535-675 3.31e-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: 47.32  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 535 KLNSIL--QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmeefyieQRDLEKKLEQVMQQKCTCDSTL 612
Cdd:TIGR04523 311 ELKSELknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK-------QRELEEKQNEIEKLKKENQSYK 383

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 613 EKDREAEyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD 675
Cdd:TIGR04523 384 QEIKNLE--SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 531-662 4.25e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRME-EFYIEQRDLEKKLEQVMQQKCTCD 609
Cdd:COG1196   666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEElEEEALEEQLEAEREELLEELLEEE 745

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491 610 STLEKDREAEYA--AQLAELRQRLDHAEADRQEL-----------------QDELRQER----EARQKLEMMIKEL 662
Cdd:COG1196   746 ELLEEEALEELPepPDLEELERELERLEREIEALgpvnllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 520-674 4.43e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 520 KIMEDVMRTYVR--QQEKLNSILQRK--QQLQMEVEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQrmeefyiEQRDL 594
Cdd:COG4942   104 EELAELLRALYRlgRQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA-------ERAEL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 595 EKKLEQVMQQKctcdstlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSK 674
Cdd:COG4942   177 EALLAELEEER------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
PRK12704 PRK12704
phosphodiesterase; Provisional
 533-666 5.07e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQrkqQLQMEVEMLSSsKAMKELTEEQQNLQKELESlqsEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 612
Cdd:PRK12704   37 EEEAKRILE---EAKKEAEAIKK-EALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKL----ELL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696491 613 EKdREAEYAAQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELKLQI 666
Cdd:PRK12704  106 EK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEARHEA 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 520-668 6.15e-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: 46.60  E-value: 6.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  520 KIMEDVMRTYVRQQEKLNSILQRKQ----QLQMEVEMLSSSKAMkeltEEQQNLQKELESLQSEHaQRMEEfyiEQRDLE 595
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEELEedlhKLEEALNDLEARLSH----SRIPEIQAELSKLEEEV-SRIEA---RLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  596 KKLEQVMQQKCTCDSTLE---------KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQelqeqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898


                   ..
gi 2168696491  667 GK 668
Cdd:TIGR02169  899 RE 900
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 551-661 6.59e-05

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: 43.34  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  551 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 630
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168696491  631 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 661
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 500-666 7.94e-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: 46.21  E-value: 7.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  500 KRDSEDSSPLLVRDGEDDKGKI--MEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ 577
Cdd:TIGR02169  282 KDLGEEEQLRVKEKIGELEAEIasLERSIAEKERELEDAE-----ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  578 SEHAQRMEEFyieqRDLEKKLEQVmqqkctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEM 657
Cdd:TIGR02169  357 EEYAELKEEL----EDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ....*....
gi 2168696491  658 MIKELKLQI 666
Cdd:TIGR02169  421 ELADLNAAI 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
565-662 8.54e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 565 EQQNLQKELESLQSEHAQRMEEfyIEQrdLEKKLEQVMQQKCTCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQ 639
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEE--IER--YEEQREQARETRDEADEVLEEHEErreelETLEAEIEDLRETIAETERERE 275

                          90       100
                  ....*....|....*....|...
gi 2168696491 640 ELQDELRQEREARQKLEMMIKEL 662
Cdd:PRK02224  276 ELAEEVRDLRERLEELEEERDDL 298
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 517-663 8.87e-05

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: 44.97  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 517 DKGKIMEDVMRTYVRQQEKL-NSILQRKQQLqmeVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 595
Cdd:pfam02841 169 RKGVKAEEVLQEFLQSKEAVeEAILQTDQAL---TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHV 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 596 KKLEQVMqqkctcdstlekdrEAEYAAQLAELRQRLDHaeaDRQELQDELRQEREAR-QKLEMMIKELK 663
Cdd:pfam02841 246 KQLIEKM--------------EAEREQLLAEQERMLEH---KLQEQEELLKEGFKTEaESLQKEIQDLK 297
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 523-656 1.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 523 EDVMRTYVRQQEKLNSILQ--RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ---SEHAQRMEEFYIEQRDLEKK 597
Cdd:COG1196   252 EAELEELEAELAELEAELEelRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 598 LEQvmqqkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDEL----RQEREARQKLE 656
Cdd:COG1196   332 LEE------------LEEELEELEEELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELE 382
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
540-663 1.23e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 540 LQRKQQLQMEVEMLSSSKAMKELTEEQQNLqkelesLQSEHAQRMEEFYI------EQRDLEKKLEQVMQQkctCDSTLE 613
Cdd:COG4717   346 IEELQELLREAEELEEELQLEELEQEIAAL------LAEAGVEDEEELRAaleqaeEYQELKEELEELEEQ---LEELLG 416

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2168696491 614 KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 663
Cdd:COG4717   417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 532-657 1.26e-04

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: 44.94  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 532 QQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdST 611
Cdd:pfam15709 382 QQRRFEEIRLRKQRLEEERQ---------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER----AE 448

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696491 612 LEKDREAEYAAQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 657
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 551-661 1.28e-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: 42.90  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 551 EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDlEKKLEQVMQQKctcdstlekdREAEYAAQLAELRQR 630
Cdd:COG2825    37 ESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKL---QKE-AATLSEEERQK----------KERELQKKQQELQRK 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2168696491 631 ldhaeadRQELQDELRQER-EARQKLEMMIKE 661
Cdd:COG2825   103 -------QQEAQQDLQKRQqELLQPILEKIQK 127
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 522-666 1.39e-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: 43.76  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 522 MEDVMRTYVRQQE---KLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKL 598
Cdd:COG1579     2 MPEDLRALLDLQEldsELDRLEHRLKELPAELA---------ELEDELAALEARLEAAKTEL----EDLEKEIKRLELEI 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491 599 EQVMQQkctcdstLEKDREA--------EYAAQLAELrqrlDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG1579    69 EEVEAR-------IKKYEEQlgnvrnnkEYEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 539-673 1.41e-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: 42.98  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 539 ILQRKQQLQMeveMLSSSKAMKELTEeqqNLQK-ELESLQSEHAQRMEEfyIEQRDLEKKleqVMQQKCTCDS---TLEK 614
Cdd:pfam13870  15 LITLKHTLAK---IQEKLEQKEELGE---GLTMiDFLQLQIENQALNEK--IEERNKELK---RLKLKVTNTVhalTHLK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 615 DREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 673
Cdd:pfam13870  84 EKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGLLHVPA 142
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 552-658 1.77e-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: 43.82  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 552 MLSSSKAMKELTEEqqnLQKELESLQSEHAQRMEEF--YIEQRDLEKKleQVM---QQKCTCDSTLEKDREAEYAAQLAe 626
Cdd:pfam12037  37 ELESSPHAKKALEL---MKKQEQTRQAELQAKIKEYeaAQEQLKIERQ--RVEyeeRRKTLQEETKQKQQRAQYQDELA- 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2168696491 627 lRQRL-DHAEADRQELQDELRQEREARQKLEMM 658
Cdd:pfam12037 111 -RKRYqDQLEAQRRRNEELLRKQEESVAKQEAM 142
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 516-668 1.97e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 516 DDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 595
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELE--ALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 596 K------------------KLEQVMQQKctcDSTLE--KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKL 655
Cdd:COG3883   104 YldvllgsesfsdfldrlsALSKIADAD---ADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180

                         170
                  ....*....|...
gi 2168696491 656 EMMIKELKLQIGK 668
Cdd:COG3883   181 EALLAQLSAEEAA 193
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
527-661 1.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKE--------LTEEQQNLQKELESLQSEHAQRMEEF-----YIEQRD 593
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleQAEEYQELKEELEELEEQLEELLGELeelleALDEEE 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 594 LEKKLEQVMQQKctcdSTLEKDREaEYAAQLAELRQRLDHAEADRqELQDELRQEREARQKLEMMIKE 661
Cdd:COG4717   430 LEEELEELEEEL----EELEEELE-ELREELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEE 491
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 524-666 2.20e-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: 44.56  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  524 DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKA-----MKELtEEQQNLQKELES-LQ--SEHAQRMEEFYIEQrdle 595
Cdd:COG3096    272 DYMRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQ---- 346

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491  596 KKLEQvmqqkctcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG3096    347 EKIER-------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
569-668 2.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  569 LQKELESLQSEHAqrmeEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDRE----AEYAAQLAEL---RQRLDHAEADRQEL 641
Cdd:COG4913    615 LEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDeidvASAEREIAELeaeLERLDASSDDLAAL 690

                           90       100
                   ....*....|....*....|....*..
gi 2168696491  642 QDELRQEREARQKLEMMIKELKLQIGK 668
Cdd:COG4913    691 EEQLEELEAELEELEEELDELKGEIGR 717
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
531-667 2.54e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDS 610
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696491 611 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIG 667
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 522-663 2.61e-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: 44.34  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 522 MEDVMRTYVRQQEKLNSILQ-----RKQQLQMEVEMLSSSKAMKEL----TEEQQNLQKELESLQSEHAQRMEEFYIEQR 592
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMeqirAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168696491 593 DLEKKLEQVMQQkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA----RQKLEMMIKELK 663
Cdd:pfam17380 457 ERQQQVERLRQQ--------EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieeERKRKLLEKEME 523
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
534-668 2.77e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 534 EKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQV--MQQkcTCDST 611
Cdd:COG1340    57 EEAQELREKRDELNEKVKELKEER--DELNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIERLewRQQ--TEVLS 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696491 612 LEKDRE-----AEYAAQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKELKLQIGK 668
Cdd:COG1340   132 PEEEKElvekiKELEKELEKAKKALEKNE-KLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 530-651 2.83e-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: 44.28  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  530 VRQQEKLNSILQRKQQLQMEVEMLS---SSKAMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQkc 606
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLkklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA-- 479

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2168696491  607 tcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREA 651
Cdd:TIGR02168  480 -------------AERELAQLQARLDSLERLQENLEGFSEGVKAL 511
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 515-663 3.47e-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: 42.34  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKE--LTEEQQNLQKELES---LQSEHAQRMEEFYI 589
Cdd:pfam15665  24 EEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 590 E----QRDLEKKLEQVMQQKctcdSTLEKDRE-------AEYAAQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQ 653
Cdd:pfam15665 104 EveeaKRAFEEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRK 179

                         170
                  ....*....|
gi 2168696491 654 KLEMMIKELK 663
Cdd:pfam15665 180 EVEDLRKEKK 189
PTZ00121 PTZ00121
MAEBL; Provisional
 416-661 4.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  416 ASQSKEATKAETSKSTS--KQSEKPHESSQHQKTVSYPDVSL---EEQEKMDLKTSRELYSCLDSSISNNSTSRKKSESA 490
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  491 VCSLVRGTSKRDSEDSSPLLVRDGEDDKGKIMEdvmrtyVRQQEKLNSIlqRKQQLQMEVEmlSSSKAMKELTEEQQNLQ 570
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE------LKKAEEENKI--KAAEEAKKAE--EDKKKAEEAKKAEEDEK 1688

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  571 KELESL--QSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDSTLEK-DREAEYAAQLAElRQRLDHAEADR--QELQDEL 645
Cdd:PTZ00121  1689 KAAEALkkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAE-EAKKDEEEKKKiaHLKKEEE 1767

                          250
                   ....*....|....*.
gi 2168696491  646 RQEREARQKLEMMIKE 661
Cdd:PTZ00121  1768 KKAEEIRKEKEAVIEE 1783
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
496-656 4.44e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 496 RGTSKRDSEDSSPLLVR--DGEDDKGKIMEDVMRTYVRQQEKLNSIlqrkQQLQMEVEMLSSSKamKELTEEQQNLQKEL 573
Cdd:PRK02224  299 LAEAGLDDADAEAVEARreELEDRDEELRDRLEECRVAAQAHNEEA----ESLREDADDLEERA--EELREEAAELESEL 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 574 ESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELrqeREA 651
Cdd:PRK02224  373 EEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELREREAELEATLRTARERV---EEA 445


                  ....*
gi 2168696491 652 RQKLE 656
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 ...
 516-666 4.70e-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: 43.63  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  516 DDKGKIMEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQK---ELESLQSEHAQRMEEFYIEQR 592
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSKlknKHEAMISDLEERLKKEEKGRQ 204

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696491  593 DLEKkleqvMQQKCTCDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:pfam01576  205 ELEK-----AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
515-663 4.90e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEhaqrmeefyIEqrDL 594
Cdd:COG2433   387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELEEKDER---------IE--RL 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 595 EKKLEQVMQQKctcDSTLEKDREAeyaaqlaelrQRLDhAEADRqeLQDELRQEREARQKLEMMIKELK 663
Cdd:COG2433   447 ERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEEERERIEELKRKLERLK 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
523-671 4.96e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  523 EDVMRTYVRQQEKLNSIL----QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHA------QRMEEFYIEQR 592
Cdd:COG4913    623 EEELAEAEERLEALEAELdalqERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELE 702

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  593 DLEKKLEQVMQQKctcdSTLEKDREaEYAAQLAELRQRLDHAEAD-----RQELQDELRQ------EREARQKLEMMIKE 661
Cdd:COG4913    703 ELEEELDELKGEI----GRLEKELE-QAEEELDELQDRLEAAEDLarlelRALLEERFAAalgdavERELRENLEERIDA 777

                          170
                   ....*....|
gi 2168696491  662 LKLQIGKSSK 671
Cdd:COG4913    778 LRARLNRAEE 787
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 533-671 5.64e-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: 43.51  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  533 QEKLNSILQRKQQLQMEVEMLSSskAMKELTEEQQNLQKELESLQSEHAQ---RMEEFYIEQRDLEKKLEQVMQQKctcd 609
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEEAANlreRLESLERRIAATERRLEDLEEQI---- 847

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696491  610 stlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 671
Cdd:TIGR02168  848 --------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
531-647 5.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  531 RQQEKLNSILQRKQQLQMEVEML------SSSKAMKELTEEQQNLQKELESLQSEHAQRME-------EFYIEQRDLEKK 597
Cdd:COG4913    306 RLEAELERLEARLDALREELDELeaqirgNGGDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAAL 385

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2168696491  598 LEQVMQQKctcdsTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQ 647
Cdd:COG4913    386 RAEAAALL-----EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
564-666 7.59e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 564 EEQQNLQKELESLQSEHAQRmEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKdreAEYAAQLAELRQRLDHAEADRQELQ- 642
Cdd:COG4717    71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEK---LEKLLQLLPLYQELEALEAELAELPe 146

                          90       100
                  ....*....|....*....|....*.
gi 2168696491 643 --DELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4717   147 rlEELEERLEELRELEEELEELEAEL 172
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 148-226 7.68e-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: 39.27  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 148 GESISCFQVGGEKRLCLPQVLNSVLREF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 225
Cdd:cd21081    10 GAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                  .
gi 2168696491 226 L 226
Cdd:cd21081    90 L 90
DUF4175 pfam13779
Domain of unknown function (DUF4175);
532-661 7.85e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 42.67  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 532 QQEklnsILQRKQQLQ--MEvemlsssKAMKELTEEQQNLQKELESLQSEHAQRMeefyiEQRDLEKKLEQvMQQKctcd 609
Cdd:pfam13779 508 DEE----IAKLMQELReaLD-------DYMQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRMLDR-IEEL---- 566

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 610 stLEKDREAEYAAQLAELRQRLDHAE-ADRQELQDELRQE-REARQKLEMMIKE 661
Cdd:pfam13779 567 --ARSGRRAEAQQMLSQLQQMLENLQaGQPQQQQQQGQSEmQQAMDELGDLLRE 618
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
527-651 8.29e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 42.37  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 527 RTYVRQQEKLNSILQRKQQLQMEVEMLSSskAMKELTE------EQQNLQKELESLQseHAQR--------MEEFYIEQR 592
Cdd:COG0497   165 RAWRALKKELEELRADEAERARELDLLRF--QLEELEAaalqpgEEEELEEERRRLS--NAEKlrealqeaLEALSGGEG 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 593 DLEKKLEQVMQQkctcdstLEkdREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA 651
Cdd:COG0497   241 GALDLLGQALRA-------LE--RLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 542-665 9.56e-04

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: 41.05  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 542 RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFyieqrdlEKKLEQVMQQKCTCDSTLEKDREAEYA 621
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELR----KQLENY-------EKDKQSLKNLKARLKVLEKELKDLKWE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696491 622 AQLaeLRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQ 665
Cdd:pfam13851 108 HEV--LEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQ 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
563-671 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 563 TEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTLEKDREaeyaaQLAELRQRLDHAEADRQELQ 642
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKE-----EIEELEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|....*....
gi 2168696491 643 DELRQEREARQKLEMMIKELKLQIGKSSK 671
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEEKVKELKE 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
457-666 1.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 457 EQEKMDLKTSRELYSCLDSSISnnstSRKKSESAVCSLVRGTSKRDSEDSSPLlvRDGEDDKGKI--MEDVMRTYVRQQE 534
Cdd:PRK03918  227 EKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEERIEELKKEI--EELEEKVKELkeLKEKAEEYIKLSE 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 535 KLNSILQRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLqSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTLE 613
Cdd:PRK03918  301 FYEEYLDELREIEKRLSRLEEEiNGIEERIKELEEKEERLEEL-KKKLKELEKRLEELEERHELYEEAKAKK----EELE 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 614 KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:PRK03918  376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 549-668 1.12e-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: 42.25  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  549 EVEMLSSSKAMKELTE---EQQNLQKELESLQSEHAQrMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 625
Cdd:COG3096    487 EVERSQAWQTARELLRryrSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQRI---------GQQLDAAEELE 556

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2168696491  626 ELRQRLdhaEADRQELQDELRQEREARQKLEMMIKELKLQIGK 668
Cdd:COG3096    557 ELLAEL---EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 533-585 1.22e-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: 38.02  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSKAmkELTEEQQNLQKELESLQSEHAQRME 585
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENE--ELKEEANELEEENQQLKQERNQWQE 60
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 531-626 1.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 609
Cdd:COG3883   130 ADADLLEELKADKAELEAKKAELEAKLAeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209

                          90
                  ....*....|....*..
gi 2168696491 610 STLEKDREAEYAAQLAE 626
Cdd:COG3883   210 AAAAAAAAAAAAAAAAA 226
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
542-662 1.27e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 542 RKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkcTCDSTLEKDRE--AE 619
Cdd:PRK02224  322 RDEELRDRLE--ECRVAAQAHNEEAESLREDADDLEER-AEELRE---EAAELESELE-------EAREAVEDRREeiEE 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2168696491 620 YAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 662
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 515-641 1.49e-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: 40.27  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 515 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSK-AMKELTEEQQNLQKELESLQSEHA---QRMEEFYIE 590
Cdd:pfam13851  42 EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqSLKNLKARLKVLEKELKDLKWEHEvleQRFEKVERE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2168696491 591 QRDLEKKLEQVM---QQKCTCDST-LEKdreaeyaaQLAELRQRLDHAEADRQEL 641
Cdd:pfam13851 122 RDELYDKFEAAIqdvQQKTGLKNLlLEK--------KLQALGETLEKKEAQLNEV 168
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
533-666 1.82e-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: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFYIEQR--DLEKKLEQVMQQKctcdS 610
Cdd:COG3206   151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGlvDLSEEAKLLLQQL----S 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 611 TLEKDReAEYAAQLAELRQRLDHAEADRQ-------------ELQDELRQEREARQKLEMM----------IKELKLQI 666
Cdd:COG3206   223 ELESQL-AEARAELAEAEARLAALRAQLGsgpdalpellqspVIQQLRAQLAELEAELAELsarytpnhpdVIALRAQI 300
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
485-664 1.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 485 KKSESAVCSLVRGTSKRDSEDSSplLVRDGEDDKGKIME-----DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAM 559
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKElekrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 560 KELtEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTC-------DSTLEKDREAEYAAQLAELRQRLD 632
Cdd:PRK03918  391 KEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRKELLEEYTAELKRIEKELK 469

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2168696491 633 HAEADRQELQDELRQEREARQKLEMMIKELKL 664
Cdd:PRK03918  470 EIEEKERKLRKELRELEKVLKKESELIKLKEL 501
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
531-666 1.97e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSI---LQRKQ--QLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieqrdlEKKLEQVMQQK 605
Cdd:COG4372    77 QLEEELEELneqLQAAQaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 606 ctcdstlekdreaeyAAQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQI 666
Cdd:COG4372   149 ---------------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA 196
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
532-663 2.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 532 QQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQ-------SEHAQRMEEFY---IEQRDLEKKLEQV 601
Cdd:PRK03918  540 EIKSLKKELEKLEELKKKLAELE--KKLDELEEELAELLKELEELGfesveelEERLKELEPFYneyLELKDAEKELERE 617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 602 MQQKCTCDSTLEKDRE---------------------------------------AEYA---AQLAELRQRLDHAEADRQ 639
Cdd:PRK03918  618 EKELKKLEEELDKAFEelaetekrleelrkeleelekkyseeeyeelreeylelsRELAglrAELEELEKRREEIKKTLE 697

                         170       180
                  ....*....|....*....|....
gi 2168696491 640 ELQDELRQEREARQKLEMMIKELK 663
Cdd:PRK03918  698 KLKEELEEREKAKKELEKLEKALE 721
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
526-665 2.27e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 526 MRTYVRQqeKLNSILQR----KQQLQMEV-EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyieqrDLEKKLEQ 600
Cdd:COG1842     6 LSDIIRA--NINALLDKaedpEKMLDQAIrDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-------KWEEKARL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 601 vmqqkctcdsTLEKDREA---EYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 665
Cdd:COG1842    77 ----------ALEKGREDlarEALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
PTZ00121 PTZ00121
MAEBL; Provisional
 415-675 2.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  415 AASQSKEATKAETSKST--SKQSEKPHESSQHQKTvsypdvslEEQEKMD-LKTSRELYSCldSSISNNSTSRKKSESAV 491
Cdd:PTZ00121  1508 AKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKA--------EEKKKADeLKKAEELKKA--EEKKKAEEAKKAEEDKN 1577

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  492 CSLVRGTSKRDSEDSspllvRDGEDDKGKIMEDVMRTyvRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQK 571
Cdd:PTZ00121  1578 MALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  572 ELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDSTLEK-DREAEYAAQLAELRQRldhaEADRQELQDELRQERE 650
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKK----EAEEKKKAEELKKAEE 1726

                          250       260
                   ....*....|....*....|....*.
gi 2168696491  651 ARQ-KLEMMIKELKLQIGKSSKPSKD 675
Cdd:PTZ00121  1727 ENKiKAEEAKKEAEEDKKKAEEAKKD 1752
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 536-598 2.58e-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: 38.37  E-value: 2.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696491 536 LNSILQR-KQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQS--EHAQRMEEFYIEQRDLEKKL 598
Cdd:cd14798     5 VSFLLEKlGELLEQEADLLSGVK------EEIESLKDELESMQAflKDADAKQDEDEELKDWVKQV 64
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 551-668 2.63e-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: 38.71  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 551 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKdREAEYAAQLAELRQR 630
Cdd:pfam03938  13 ESPEGKAAQAQLEKKFKKRQAELEAKQKE--------------LQKLYEELQKDGALLEEEREE-KEQELQKKEQELQQL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2168696491 631 ldhaeadRQELQDELRQER-EARQKLEMMIKELKLQIGK 668
Cdd:pfam03938  78 -------QQKAQQELQKKQqELLQPIQDKINKAIKEVAK 109
46 PHA02562
endonuclease subunit; Provisional
 531-666 2.94e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQlqMEVEMLSSSKAMK----ELTEEQQNLQKELESlQSEHAQRMEEFYIeqrDLEKKLEQ-----V 601
Cdd:PHA02562  206 EQRKKNGENIARKQN--KYDELVEEAKTIKaeieELTDELLNLVMDIED-PSAALNKLNTAAA---KIKSKIEQfqkviK 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696491 602 MQQK---C-TCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKlemmIKELKLQI 666
Cdd:PHA02562  280 MYEKggvCpTCTQQISEgpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK----LLELKNKI 346
PRK09039 PRK09039
peptidoglycan -binding protein;
531-642 3.47e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSIL----QRKQQLQMEVEMLSSSKAMKELTEEQ-QNLQKELESLQSEHAQRM--------EEFYIEQR----- 592
Cdd:PRK09039   60 SQIAELADLLslerQGNQDLQDSVANLRASLSAAEAERSRlQALLAELAGAGAAAEGRAgelaqeldSEKQVSARalaqv 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696491 593 -DLEKKLEQVMQQKCTCDSTLE--KDREAEYAAQLAELRQRLDHAEADR-QELQ 642
Cdd:PRK09039  140 eLLNQQIAALRRQLAALEAALDasEKRDRESQAKIADLGRRLNVALAQRvQELN 193
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 533-599 3.53e-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: 36.87  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 599
Cdd:COG3074    10 EAKVQQAVDTIELLQMEVEELKEKN--EELEQENEELQSENEELQSEN----EQLKTENAEWQERIR 70
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 546-673 3.56e-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: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 546 LQMEVEMLSSSKAMkeLTEEQQNLQKELESLQSEhAQRMEEFYieQRDLEKKLEQVMQQKCTCDSTLEKDREAEyaAQLA 625
Cdd:pfam09787  45 LTLELEELRQERDL--LREEIQKLRGQIQQLRTE-LQELEAQQ--QEEAESSREQLQELEEQLATERSARREAE--AELE 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2168696491 626 ELRQRLDHAEadrqelqDELRQEREARQ----KLEMMIKELKLQIGKSSKPS 673
Cdd:pfam09787 118 RLQEELRYLE-------EELRRSKATLQsrikDREAEIEKLRNQLTSKSQSS 162
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 530-671 3.60e-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: 40.87  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  530 VRQQEKLNSILQRKQQLQMEVEMlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKlEQVMQQKCTcd 609
Cdd:pfam15921  428 VQRLEALLKAMKSECQGQMERQM-AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTA-- 503

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491  610 STLEKDREAEYA-AQLAELRQRLDhaeADRQELQdELRQEREARQKLEMMIKELKLQIGKSSK 671
Cdd:pfam15921  504 SLQEKERAIEATnAEITKLRSRVD---LKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDK 562
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
559-666 3.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  559 MKELTEEQQNLQKELEslQSEHAQRMEEFYieqRDLEKKLEQVMQQKcTCDSTLEKDREAEyaaQLAELRQRLDHAEADR 638
Cdd:COG4913    234 FDDLERAHEALEDARE--QIELLEPIRELA---ERYAAARERLAELE-YLRAALRLWFAQR---RLELLEAELEELRAEL 304

                           90       100
                   ....*....|....*....|....*...
gi 2168696491  639 QELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQI 332
PRK09039 PRK09039
peptidoglycan -binding protein;
562-667 3.69e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 562 LTEEQQNLQKELESLQSEHAQRMEEFYIEQR---DLEKKLEQVMQQKctcdSTLEKDReAEYAAQLAELRQRLDHAEADR 638
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADLLSLERQgnqDLQDSVANLRASL----SAAEAER-SRLQALLAELAGAGAAAEGRA 118

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2168696491 639 QELQDELRQER----EARQKLEMM---IKELKLQIG 667
Cdd:PRK09039  119 GELAQELDSEKqvsaRALAQVELLnqqIAALRRQLA 154
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
563-668 3.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  563 TEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQVMQQKCtcdSTLEKDREAEYAAQLAELRQRLDHAEADRQELQ 642
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARER-LAELEYLRAALRLWFAQRR---LELLEAELEELRAELARLEAELERLEARLDALR 322

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2168696491  643 DELRQEREARQK--------LEMMIKELKLQIGK 668
Cdd:COG4913    323 EELDELEAQIRGnggdrleqLEREIERLERELEE 356
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 531-665 3.90e-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: 40.02  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 609
Cdd:pfam15558  17 HKEEQRMRELQQQAALAWEELRRRDQKRqETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRW 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 610 STLEKDREA------EYAAQLAELR-----QRLDHAEADRQELQDE---LRQEREARQKLEMMIKELKLQ 665
Cdd:pfam15558  97 REQAEDQENqrqeklERARQEAEQRkqcqeQRLKEKEEELQALREQnslQLQERLEEACHKRQLKEREEQ 166
valS PRK05729
valyl-tRNA synthetase; Reviewed
 562-632 4.11e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 40.47  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 562 LTEEQQNLQKELESLQSEhaqrmeefyIEQrdLEKKL----------EQVMQQkctcdstlEKDREAEYAAQLAELRQRL 631
Cdd:PRK05729  809 VEAELARLEKELAKLEKE---------IER--VEKKLsnegfvakapEEVVEK--------EREKLAEYEEKLAKLKERL 869


                  .
gi 2168696491 632 D 632
Cdd:PRK05729  870 A 870
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 533-667 4.26e-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: 38.78  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 533 QEKLNSILQRKQQLQMEVEMLSS---SKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDLEKKLEQVmqqkctcd 609
Cdd:pfam01442   3 EDSLDELSTYAEELQEQLGPVAQelvDRLEKETEALRERLQKDLEEVRAKLEPYLEEL---QAKLGQNVEEL-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 610 stlekdrEAEYAAQLAELRQRLdhaEADRQELQDELRQE-REARQKLEMMIKELKLQIG 667
Cdd:pfam01442  72 -------RQRLEPYTEELRKRL---NADAEELQEKLAPYgEELRERLEQNVDALRARLA 120
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 531-660 4.51e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 531 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKLEQVMQQKCTCDS 610
Cdd:pfam05672  20 RRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEE--ERQRKAEEEAEEREQREQEEQE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2168696491 611 TLEKDRE-AEYAAQLAELRQRLdhaEADRQELQDElrQEREARQK-LEMMIK 660
Cdd:pfam05672  98 RLQKQKEeAEAKAREEAERQRQ---EREKIMQQEE--QERLERKKrIEEIMK 144
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 590-668 4.55e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 4.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 590 EQRDLEKKLEQVMQQKctcdSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGK 668
Cdd:COG0542   412 ELDELERRLEQLEIEK----EALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 541-666 5.07e-03

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: 39.52  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 541 QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYieQRDLEKKLEQVMQQKCTCDSTLEKDRE-AE 619
Cdd:pfam13868 216 ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--ERMLRKQAEDEEIEQEEAEKRRMKRLEhRR 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696491 620 YAAQLAELRQRLdhAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:pfam13868 294 ELEKQIEEREEQ--RAAEREEELEEGERLREEEAERRERIEEERQKK 338
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 520-631 5.13e-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: 39.75  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 520 KIMEDVMRTYVRQQEKLNSILQRKQQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKL 598
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2168696491 599 EQVMQQkctcdstLEKDREAEYAAQLAELRQRL 631
Cdd:COG4942   230 ARLEAE-------AAAAAERTPAAGFAALKGKL 255
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 549-647 5.19e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 549 EVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkctcdstlekdrEAEyaAQLAELR 628
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELE-----------------ALQ--AEIDKLQ 71

                          90
                  ....*....|....*....
gi 2168696491 629 QRLDHAEADRQELQDELRQ 647
Cdd:COG3883    72 AEIAEAEAEIEERREELGE 90
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
532-656 5.21e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 532 QQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELE----SLQSEHAQRMEEFYIEQRDLEKKLEQvmqqkct 607
Cdd:COG3064    23 AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqraaELAAEAAKKLAEAEKAAAEAEKKAAA------- 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2168696491 608 cdstlEKDREAEYAAQLAELRQRLDHAEADRQElQDELRQEREARQKLE 656
Cdd:COG3064    96 -----EKAKAAKEAEAAAAAEKAAAAAEKEKAE-EAKRKAEEEAKRKAE 138
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 532-666 6.38e-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: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 532 QQEKLNSILQRKQQlqmevEMLSSSKAMKELTEEQQNLQKELESLQSEHAQR-MEEFYIEQRDLEKKLEQVmqqkctcDS 610
Cdd:TIGR04523 261 EQNKIKKQLSEKQK-----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEI-------QN 328

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 611 TLEKDREA--EYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 666
Cdd:TIGR04523 329 QISQNNKIisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 502-670 6.56e-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: 39.70  E-value: 6.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 502 DSEDSSPLLVRDGEDDKGKiMEDVMRTYVRQQEKLNSiLQRKQQLQmevemlssSKAMKELTEEQQNLQKELESLQSEHA 581
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENK-MKDLTFLLEESRDKANQ-LEEKTKLQ--------DENLKELIEKKDHLTKELEDIKMSLQ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 582 QRMEefyiEQRDLEKKLEqvMQQKCTCDSTLEKDreaeyaAQLAEL-RQRLDHA------EADRQELQDELRQEREARQK 654
Cdd:pfam05483 307 RSMS----TQKALEEDLQ--IATKTICQLTEEKE------AQMEELnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEK 374

                         170
                  ....*....|....*.
gi 2168696491 655 LEMMIKELKLQIGKSS 670
Cdd:pfam05483 375 NEDQLKIITMELQKKS 390
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 520-661 6.76e-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: 38.79  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 520 KIMEDVMRTYVRQQEKLNSIL---QRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 595
Cdd:cd07671    22 KDVEELLKQRAQAEERYGKELvqiARKAGGQTEINTLKASfDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696491 596 KKLEQVMQQ---------KCTCDSTL---EKDREAEYAAQLAELRQRLDHaEADRQELQDELRQEREARQKLEMMIKE 661
Cdd:cd07671   102 KKYEAVMERvqkskvslyKKTMESKKtyeQRCREADEAEQTFERSSSTGN-PKQSEKSQNKAKQCRDAATEAERVYKQ 178
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
 565-645 7.21e-03

Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members also carry Kinesin-motor domains at their N-terminus, Kinesin, pfam00225.


Pssm-ID: 464291 [Multi-domain]  Cd Length: 107  Bit Score: 36.51  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 565 EQQNLQ--KELESLQSEHAQRMEEFYIEQRDLEKK---LEQVMQQkctcdstLEKDREaEYAAQLAELRQRLDHAEADRQ 639
Cdd:pfam14739   2 EEEKLQisKALVDLQIENNKLREQYEAEKFELKNKllnLENRVLE-------LELRLE-KAAEEIQDLRERLRELEDDRR 73


                  ....*.
gi 2168696491 640 ELQDEL 645
Cdd:pfam14739  74 ELAEEF 79
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 523-665 7.70e-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: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 523 EDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKElTEEQQNLQKEleslQSEHAQRMEEfyieqrdlEKKLEQvm 602
Cdd:pfam15709 318 EDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRRE-QEEQRRLQQE----QLERAEKMRE--------ELELEQ-- 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696491 603 qQKCTCDSTLEKDReaeyaaqLAELRQRLDHAEAdRQELQDELRQEREARQKLEMMIKELKLQ 665
Cdd:pfam15709 383 -QRRFEEIRLRKQR-------LEEERQRQEEEER-KQRLQLQAAQERARQQQEEFRRKLQELQ 436
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 565-668 7.76e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 36.78  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 565 EQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKleqvmqqkctcdstlekdrEAEYAAQLAELRQRLDHAEADRQELQDE 644
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKK-------------------EQELKEDLIKFDKFLKENDAKRRRALKK 67

                          90       100
                  ....*....|....*....|....
gi 2168696491 645 LRQEREARQKLEMMIKELKLQIGK 668
Cdd:pfam13863  68 AEEETKLKKEKEKEIKKLTAQIEE 91
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 519-649 9.05e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 37.63  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491 519 GKIMEDvmrtyvRQQEKLNSILQRKQQLQmevemlsssKAMKELTEEQQNL---QKELESLQSEHAQRMEEfyIEQrDLE 595
Cdd:PRK07352   45 GKILEE------RREAILQALKEAEERLR---------QAAQALAEAQQKLaqaQQEAERIRADAKARAEA--IRA-EIE 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696491 596 KKLEQVMQQkctCDSTLEKDREAEYAAQLAELRQR-----LDHAEADRQELQDELRQER 649
Cdd:PRK07352  107 KQAIEDMAR---LKQTAAADLSAEQERVIAQLRREaaelaIAKAESQLPGRLDEDAQQR 162
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 531-665 9.58e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.18  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696491  531 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKE-LTEEQQnlqKELESLQSEHAQRMEEFYIE-QRDLEKKLEQVMQQKCTC 608
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDiLQREQA---TIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITC 449

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696491  609 DSTLEKDREAEyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 665
Cdd:TIGR00618  450 TAQCEKLEKIH----LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
 
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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