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Conserved domains on  [gi|2168696487|ref|NP_001385489|]
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ski-like protein isoform b [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 6.52e-67

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


:

Pssm-ID: 410787  Cd Length: 100  Bit Score: 213.67  E-value: 6.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696487 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 1.54e-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: 1.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696487  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 ...
 481-620 3.80e-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: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 560
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  561 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
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 6.52e-67

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 213.67  E-value: 6.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696487 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 1.54e-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: 1.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696487  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 1.11e-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: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 2168696487 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 1.42e-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: 164.76  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 133 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 2168696487 213 PSCGLITLTDAQRLCNALLR 232
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 481-620 3.80e-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: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 560
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  561 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
481-620 2.57e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  481 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 552
Cdd:COG4913    595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487  553 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4913    671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 487-621 2.02e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.98  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 566
Cdd:PRK00409  515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696487 567 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 621
Cdd:PRK00409  580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 469-620 2.80e-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: 49.92  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEV-EMLSSSKAMKELTEEQQNLQKE-LESLQSEHAQRMEEFYIEQR 546
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 547 DLEKKLEQVMQQKCTcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:pfam13868 177 EIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 469-617 4.03e-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: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 546
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696487 547 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 617
Cdd:cd16269   234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 505-615 6.08e-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: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  505 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 584
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168696487  585 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 615
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 6.52e-67

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 213.67  E-value: 6.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 2168696487 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 1.54e-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: 1.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 2168696487  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 1.11e-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: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 2168696487 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 2.01e-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: 177.37  E-value: 2.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21079     1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                          90
                  ....*....|.
gi 2168696487 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 6.07e-49

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


Pssm-ID: 410786  Cd Length: 102  Bit Score: 166.01  E-value: 6.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 134 PSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21083     3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                          90
                  ....*....|....*...
gi 2168696487 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 1.42e-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: 164.76  E-value: 1.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 133 IPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 2168696487 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 2.86e-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: 125.10  E-value: 2.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21074     1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                  ....*...
gi 2168696487 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 2.52e-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: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 141 LTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21080     1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                          90
                  ....*....|.
gi 2168696487 221 TDAQRLCNALL 231
Cdd:cd21080    81 REAERLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 481-620 3.80e-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: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQsehaQRMEEFyieQRDLEKKLEQVMQQKC 560
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  561 tcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
481-620 2.57e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  481 RTYVRQQ--------EKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKL 552
Cdd:COG4913    595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487  553 EQVMQQKctcdSTLEKDreaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4913    671 AELEAEL----ERLDAS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
485-619 3.34e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmEEFYIEQRDLEK---KLEQVMQQKCT 561
Cdd:COG4717   106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAelaELQEELEELLE 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 562 CDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 619
Cdd:COG4717   185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
493-610 1.76e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  493 ILQRKQQLQmevEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEKDREA 572
Cdd:COG4913    670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2168696487  573 EYAAQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 610
Cdd:COG4913    743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 470-621 2.30e-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: 54.30  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  470 DDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 549
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI------QELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487  550 KKLEqvmqqkctcdstlekdreaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE-------MMIKELKLQIG 621
Cdd:TIGR02169  868 EELE-------------------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKLE 927
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 485-620 2.46e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKctcds 564
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----- 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 565 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 483-608 7.70e-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: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 483 YVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNL--QKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKc 560
Cdd:COG1579    47 LEAAKTELEDLEKEIKRLELEIE--EVEARIKKYEEQLGNVrnNKEYEALQKE----IESLKRRISDLEDEILELMERI- 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2168696487 561 tcdSTLEKDREAEyAAQLAELRQRLDHAEADRQELQDELRQEREARQK 608
Cdd:COG1579   120 ---EELEEELAEL-EAELAELEAELEEKKAELDEELAELEAELEELEA 163
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 483-620 8.45e-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: 8.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  483 YVRQQEKLNSILQRKQQL--QMEVEMLSSSKAMKELTEEQQNLQKELESLQSE---HAQRMEEFYIEQRDLEKKLEQVMQ 557
Cdd:TIGR02168  251 AEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487  558 QKcTCDSTLEKDREAEYA---AQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:TIGR02168  331 KL-DELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
487-620 1.04e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 566
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER-LEELEERLEELRELEEELEELEAEL----AEL 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 567 EKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4717   176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
480-620 1.21e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  480 MRTYVRQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQ----RMEEFYIEQRDLEKKLEQV 555
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLE--AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER 357

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696487  556 ------MQQKC-TCDSTLEKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4913    358 errrarLEALLaALGLPLPASAE-EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 487-621 2.02e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.98  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCtcdstl 566
Cdd:PRK00409  515 KEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAI------ 579

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696487 567 eKDREAEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLE-----MMIKELKLQIG 621
Cdd:PRK00409  580 -KEAKKEADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEkkkkkQKEKQEELKVG 640
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
487-627 2.04e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.79  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQS----EH--AQRMEEfyiEQRDLEKKLEQVMQQKc 560
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpNHpdVIALRA---QIAALRAQLQQEAQRI- 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168696487 561 tcDSTLEKD------REAEYAAQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQIGKSSKPS 627
Cdd:COG3206   315 --LASLEAElealqaREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 469-620 2.80e-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: 49.92  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEV-EMLSSSKAMKELTEEQQNLQKE-LESLQSEHAQRMEEFYIEQR 546
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 547 DLEKKLEQVMQQKCTcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:pfam13868 177 EIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 485-620 3.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLssSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQVMQqkctcds 564
Cdd:COG1196   324 ELAELEEELEELEEELEELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAE----AEEELEELAEELLE------- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 565 tlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG1196   391 --ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 156-228 3.68e-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: 3.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 156 VGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCN 228
Cdd:cd21082    16 INGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDVERLYS 88
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 485-625 3.93e-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: 49.38  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQR--------------DLEK 550
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVR 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 551 K---LEQVMQQKctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:COG4942   137 RlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
469-617 3.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIME-------DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEF 541
Cdd:PRK03918  447 EEHRKELLEeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 542 YieqRDLEKKLEQVMQQKctcdSTLEKD--REAEYAAQLAELRQRLDHAEADRQELQDELRQER-EARQKLEMMIKELK 617
Cdd:PRK03918  527 Y---EKLKEKLIKLKGEI----KSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 469-617 4.03e-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: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKL-NSILQRKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEfyiEQR 546
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696487 547 DLEKKLEQvmqqkctcdstLEKDREAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 617
Cdd:cd16269   234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 504-610 4.10e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 504 VEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekdreAEYAAQLAELR 582
Cdd:COG3883   121 LSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLS 188

                          90       100
                  ....*....|....*....|....*...
gi 2168696487 583 QRLDHAEADRQELQDELRQEREARQKLE 610
Cdd:COG3883   189 AEEAAAEAQLAELEAELAAAEAAAAAAA 216
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
481-617 5.03e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 5.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyiEQRDLEKKLEQvmqqkc 560
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE----ELAELEAELEQ------ 464

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487 561 tcdstLEKDREaeyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 617
Cdd:COG4717   465 -----LEEDGE------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 511-620 6.19e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 511 KAMKELTEEQQNLQ----------KELESL--QSEHAQRmeefYIEQRDLEKKLEQVMQqkctcdstLEKDREAEyaAQL 578
Cdd:COG1196   176 EAERKLEATEENLErledilgeleRQLEPLerQAEKAER----YRELKEELKELEAELL--------LLKLRELE--AEL 241

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2168696487 579 AELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
mukB PRK04863
chromosome partition protein MukB;
443-627 6.48e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 6.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  443 SAVCSLVRGTSKRDSEDSSPLLVRDGEDDKgkiMEDVMRTYVRQQekLNSILQRKQQLQMEVEMLSS----SKAMKELTE 518
Cdd:PRK04863   480 QLVRKIAGEVSRSEAWDVARELLRRLREQR---HLAEQLQQLRMR--LSELEQRLRQQQRAERLLAEfckrLGKNLDDED 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  519 EQQNLQKELESLQSEHAQRMEEFyIEQR-DLEKKLEQVMQQKctcdSTLEKDREAEYAAQ--LAELRQRLDHAEADR--- 592
Cdd:PRK04863   555 ELEQLQEELEARLESLSESVSEA-RERRmALRQQLEQLQARI----QRLAARAPAWLAAQdaLARLREQSGEEFEDSqdv 629

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2168696487  593 ----QELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 627
Cdd:PRK04863   630 teymQQLLERERELTVERDELAARKQALDEEIERLSQPG 668
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 489-629 1.06e-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: 48.48  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 489 KLNSIL--QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmeefyieQRDLEKKLEQVMQQKCTCDSTL 566
Cdd:TIGR04523 311 ELKSELknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK-------QRELEEKQNEIEKLKKENQSYK 383

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 567 EKDREAEyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD 629
Cdd:TIGR04523 384 QEIKNLE--SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 478-610 1.16e-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: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  478 DVMRTYVRQQEKLNSILQRKQQLQMEvemlssskamkeLTEEQQNL--QKELESLQSEHAQRMEEFYIEQRDLEKKLEQV 555
Cdd:COG3096    495 QTARELLRRYRSQQALAQRLQQLRAQ------------LAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2168696487  556 MQQKCTCDSTLEKDREaeyaaQLAELRQRLDHAEADRQELQDELRQEREARQKLE 610
Cdd:COG3096    563 EAQLEELEEQAAEAVE-----QRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 477-620 1.28e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 477 EDVMRTYVRQQEKLnsilqRKQqlqmevemlsSSKAMK--ELTEEQQNLQKELESLQSEHAQRMEEFYIEQRD-LEKKLE 553
Cdd:COG1196   192 EDILGELERQLEPL-----ERQ----------AEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEeLEAELE 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 554 QVMQQKCTCDSTLEKDR----------------EAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 617
Cdd:COG1196   257 ELEAELAELEAELEELRleleeleleleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336


                  ...
gi 2168696487 618 LQI 620
Cdd:COG1196   337 EEL 339
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 504-615 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 2168696487 504 VEMLSSSKAMKELTEEQQNLQKELESLQSE----HAQRMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 579
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEEIQ 474

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2168696487 580 ELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 615
Cdd:COG0542   475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
PRK11637 PRK11637
AmiB activator; Provisional
 487-629 1.30e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 48.15  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEvemlssskamKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEqvmqqkctcdSTL 566
Cdd:PRK11637  169 QETIAELKQTREELAAQ----------KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLE----------SSL 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 567 EKDReaeyaAQLAELRQ---RLDHAEAdRQELQDELRQEREAR--QKLEMMIKELKlQIGKSSKPSKD 629
Cdd:PRK11637  229 QKDQ-----QQLSELRAnesRLRDSIA-RAEREAKARAEREAReaARVRDKQKQAK-RKGSTYKPTES 289
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 468-610 1.37e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 468 GEDDKGKIMED---VMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIE 544
Cdd:PRK09510   46 GGSVIDAVMVDpgaVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 545 QRDLEKKLEQVMQQKCTCDSTL----EKDREAEYAAQLAELRQRLDHAEADRQelqdelrQEREARQKLE 610
Cdd:PRK09510  126 QAALKQKQAEEAAAKAAAAAKAkaeaEAKRAAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 487-616 1.47e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.91  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQL--QMEVEMlsssKAMKELTEEQQNLQKELESLQSEHAQRMEEF------YI-------EQRDLEKK 551
Cdd:PRK04778  281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 552 LEQVMQQkctcdstLEKDREA---------EYAAQLAELRQRLDHAEADRQELQDELRQ----EREARQKLEMMIKEL 616
Cdd:PRK04778  357 LESLEKQ-------YDEITERiaeqeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKL 427
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 484-620 1.57e-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: 48.20  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 484 VRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDL----EKKLEQVMQQK 559
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696487 560 CTcdSTLEKDREAEYAAQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 474-616 1.73e-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: 48.14  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  474 KIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 553
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE--LEDAEERLAKLEAEIDKLLAEI----EELEREIEEERKRRD 353

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487  554 QVMqqkctcdstlekDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREarqKLEMMIKEL 616
Cdd:TIGR02169  354 KLT------------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREI 401
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
487-625 1.75e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhaqrMEEFYIEQRDLEKKLEQVMQQKctcdSTL 566
Cdd:COG4372    44 QEELEQLREELEQAREELE--QLEEELEQARSELEQLEEELEELNEQ----LQAAQAELAQAQEELESLQEEA----EEL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 567 EKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:COG4372   114 QEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 487-623 1.96e-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: 47.54  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQL--QMEVEMLS----------SSKAMKELTEEQQNLQKELESLQseHAQRMEEFYIE-QRDLEKKLE 553
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 554 QVMQQkctCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQELQDELR----QEREARQKLEMMIKEL---KLQIG 621
Cdd:pfam06160 340 ELEKR---YDEIVERLEEkevaySELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVE 416


                  ..
gi 2168696487 622 KS 623
Cdd:pfam06160 417 KS 418
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
487-620 2.14e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdstl 566
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ------- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 567 ekdreaeyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4372   101 ---------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 485-622 2.51e-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: 47.74  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  485 RQQEKLNSILQRKQQLQMEVEMLSSSK-----AMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQK 559
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLdelaeELAELEEKLEELKEELESLEAELE-ELEAELEELESRLEELEEQLETL 384

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487  560 CTcDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMmiKELKLQIGK 622
Cdd:TIGR02168  385 RS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEE 444
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 474-622 4.63e-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: 4.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  474 KIMEDVMRTYVRQQEKLNSILQRKQ----QLQMEVEMLSSSKAMkeltEEQQNLQKELESLQSEHaQRMEEfyiEQRDLE 549
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEELEedlhKLEEALNDLEARLSH----SRIPEIQAELSKLEEEV-SRIEA---RLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  550 KKLEQVMQQKCTCDSTLE---------KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQelqeqridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898


                   ..
gi 2168696487  621 GK 622
Cdd:TIGR02169  899 RE 900
PRK12704 PRK12704
phosphodiesterase; Provisional
 487-620 4.80e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 4.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQrkqQLQMEVEMLSSsKAMKELTEEQQNLQKELESlqsEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTL 566
Cdd:PRK12704   37 EEEAKRILE---EAKKEAEAIKK-EALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKL----ELL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487 567 EKdREAEYAAQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELKLQI 620
Cdd:PRK12704  106 EK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEARHEA 171
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 485-616 4.86e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRME-EFYIEQRDLEKKLEQVMQQKCTCD 563
Cdd:COG1196   666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEElEEEALEEQLEAEREELLEELLEEE 745

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 564 STLEKDREAEYA--AQLAELRQRLDHAEADRQEL-----------------QDELRQER----EARQKLEMMIKEL 616
Cdd:COG1196   746 ELLEEEALEELPepPDLEELERELERLEREIEALgpvnllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 474-628 5.07e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 474 KIMEDVMRTYVR--QQEKLNSILQRK--QQLQMEVEMLSS-SKAMKELTEEQQNLQKELESLQSEHAQrmeefyiEQRDL 548
Cdd:COG4942   104 EELAELLRALYRlgRQPPLALLLSPEdfLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA-------ERAEL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 549 EKKLEQVMQQKctcdstlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSK 628
Cdd:COG4942   177 EALLAELEEER------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 454-620 5.77e-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: 5.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  454 KRDSEDSSPLLVRDGEDDKGKI--MEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ 531
Cdd:TIGR02169  282 KDLGEEEQLRVKEKIGELEAEIasLERSIAEKERELEDAE-----ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  532 SEHAQRMEEFyieqRDLEKKLEQVmqqkctcdstleKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEM 611
Cdd:TIGR02169  357 EEYAELKEEL----EDLRAELEEV------------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ....*....
gi 2168696487  612 MIKELKLQI 620
Cdd:TIGR02169  421 ELADLNAAI 429
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 505-615 6.08e-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: 6.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  505 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQr 584
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2168696487  585 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 615
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 486-611 6.09e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 486 QQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdST 565
Cdd:pfam15709 382 QQRRFEEIRLRKQRLEEERQ---------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER----AE 448

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696487 566 LEKDREAEYAAQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 611
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
488-617 6.26e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 488 EKLNSILQRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQ----------SEHAQRMEEFYIEQRDLEKKLEQV- 555
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEvKELEELKEEIEELEKELESLEgskrkleekiRELEERIEELKKEIEELEEKVKELk 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 556 -MQQKCTCDSTLEKDREaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 617
Cdd:PRK03918  287 eLKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 471-617 6.43e-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: 45.36  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 471 DKGKIMEDVMRTYVRQQEKL-NSILQRKQQLqmeVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 549
Cdd:pfam02841 169 RKGVKAEEVLQEFLQSKEAVeEAILQTDQAL---TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHV 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 550 KKLEQVMqqkctcdstlekdrEAEYAAQLAELRQRLDHaeaDRQELQDELRQEREAR-QKLEMMIKELK 617
Cdd:pfam02841 246 KQLIEKM--------------EAEREQLLAEQERMLEH---KLQEQEELLKEGFKTEaESLQKEIQDLK 297
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
519-616 7.30e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 519 EQQNLQKELESLQSEHAQRMEEfyIEQrdLEKKLEQVMQQKCTCDSTLEKDRE-----AEYAAQLAELRQRLDHAEADRQ 593
Cdd:PRK02224  200 EEKDLHERLNGLESELAELDEE--IER--YEEQREQARETRDEADEVLEEHEErreelETLEAEIEDLRETIAETERERE 275

                          90       100
                  ....*....|....*....|...
gi 2168696487 594 ELQDELRQEREARQKLEMMIKEL 616
Cdd:PRK02224  276 ELAEEVRDLRERLEELEEERDDL 298
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 493-627 9.89e-05

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: 43.36  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 493 ILQRKQQLQMeveMLSSSKAMKELTEeqqNLQK-ELESLQSEHAQRMEEfyIEQRDLEKKleqVMQQKCTCDS---TLEK 568
Cdd:pfam13870  15 LITLKHTLAK---IQEKLEQKEELGE---GLTMiDFLQLQIENQALNEK--IEERNKELK---RLKLKVTNTVhalTHLK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 569 DREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPS 627
Cdd:pfam13870  84 EKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQGGLLHVPA 142
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 470-622 1.15e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 470 DDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 549
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELE--ALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 550 K------------------KLEQVMQQKctcDSTLE--KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKL 609
Cdd:COG3883   104 YldvllgsesfsdfldrlsALSKIADAD---ADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180

                         170
                  ....*....|...
gi 2168696487 610 EMMIKELKLQIGK 622
Cdd:COG3883   181 EALLAQLSAEEAA 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 477-610 1.30e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 477 EDVMRTYVRQQEKLNSILQ--RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ---SEHAQRMEEFYIEQRDLEKK 551
Cdd:COG1196   252 EAELEELEAELAELEAELEelRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 552 LEQvmqqkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDEL----RQEREARQKLE 610
Cdd:COG1196   332 LEE------------LEEELEELEEELEEAEEELEEAEAELAEAEEALleaeAELAEAEEELE 382
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
494-617 1.38e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 494 LQRKQQLQMEVEMLSSSKAMKELTEEQQNLqkelesLQSEHAQRMEEFYI------EQRDLEKKLEQVMQQkctCDSTLE 567
Cdd:COG4717   346 IEELQELLREAEELEEELQLEELEQEIAAL------LAEAGVEDEEELRAaleqaeEYQELKEELEELEEQ---LEELLG 416

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2168696487 568 KDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 617
Cdd:COG4717   417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 505-615 1.41e-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: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 505 EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDlEKKLEQVMQQKctcdstlekdREAEYAAQLAELRQR 584
Cdd:COG2825    37 ESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKL---QKE-AATLSEEERQK----------KERELQKKQQELQRK 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2168696487 585 ldhaeadRQELQDELRQER-EARQKLEMMIKE 615
Cdd:COG2825   103 -------QQEAQQDLQKRQqELLQPILEKIQK 127
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 476-620 1.45e-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: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 476 MEDVMRTYVRQQE---KLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKL 552
Cdd:COG1579     2 MPEDLRALLDLQEldsELDRLEHRLKELPAELA---------ELEDELAALEARLEAAKTEL----EDLEKEIKRLELEI 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 553 EQVMQQkctcdstLEKDREA--------EYAAQLAELrqrlDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG1579    69 EEVEAR-------IKKYEEQlgnvrnnkEYEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 506-612 1.59e-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: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 506 MLSSSKAMKELTEEqqnLQKELESLQSEHAQRMEEF--YIEQRDLEKKleQVM---QQKCTCDSTLEKDREAEYAAQLAe 580
Cdd:pfam12037  37 ELESSPHAKKALEL---MKKQEQTRQAELQAKIKEYeaAQEQLKIERQ--RVEyeeRRKTLQEETKQKQQRAQYQDELA- 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2168696487 581 lRQRL-DHAEADRQELQDELRQEREARQKLEMM 612
Cdd:pfam12037 111 -RKRYqDQLEAQRRRNEELLRKQEESVAKQEAM 142
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 476-617 1.64e-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: 43.11  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 476 MEDVMRTYvrqQEKLNSILQRKQQLQMEVEMLSSSKAMKE--LTEEQQNLQKELES---LQSEHAQRMEEFYIE----QR 546
Cdd:pfam15665  34 TREKILQY---KSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSREveeaKR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 547 DLEKKLEQVMQQKctcdSTLEKDRE-------AEYAAQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQKLEMMIK 614
Cdd:pfam15665 111 AFEEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRKEVEDLRK 186


                  ...
gi 2168696487 615 ELK 617
Cdd:pfam15665 187 EKK 189
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 476-617 1.69e-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: 44.73  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 476 MEDVMRTYVRQQEKLNSILQ-----RKQQLQMEVEMLSSSKAMKEL----TEEQQNLQKELESLQSEHAQRMEEFYIEQR 546
Cdd:pfam17380 377 MRELERLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKVEMeqirAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168696487 547 DLEKKLEQVMQQkctcdstlEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA----RQKLEMMIKELK 617
Cdd:pfam17380 457 ERQQQVERLRQQ--------EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieeERKRKLLEKEME 523
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
488-622 1.73e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 488 EKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQV--MQQkcTCDST 565
Cdd:COG1340    57 EEAQELREKRDELNEKVKELKEER--DELNEKLNELREELDELRKELAELNKA-GGSIDKLRKEIERLewRQQ--TEVLS 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696487 566 LEKDRE-----AEYAAQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKELKLQIGK 622
Cdd:COG1340   132 PEEEKElvekiKELEKELEKAKKALEKNE-KLKELRAELKELRKEAEEIHKKIKELAEEAQE 192
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
485-621 1.91e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDS 564
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487 565 TLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIG 621
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 478-620 2.23e-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: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  478 DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKA-----MKELtEEQQNLQKELES-LQ--SEHAQRMEEFYIEQrdle 549
Cdd:COG3096    272 DYMRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQ---- 346

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696487  550 KKLEQvmqqkctcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG3096    347 EKIER-------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
523-622 2.36e-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: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  523 LQKELESLQSEHAqrmeEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDRE----AEYAAQLAEL---RQRLDHAEADRQEL 595
Cdd:COG4913    615 LEAELAELEEELA----EAEERLEALEAELDALQERREALQRLAEYSWDeidvASAEREIAELeaeLERLDASSDDLAAL 690

                           90       100
                   ....*....|....*....|....*..
gi 2168696487  596 QDELRQEREARQKLEMMIKELKLQIGK 622
Cdd:COG4913    691 EEQLEELEAELEELEEELDELKGEIGR 717
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
481-615 2.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKE--------LTEEQQNLQKELESLQSEHAQRMEEF-----YIEQRD 547
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraaleQAEEYQELKEELEELEEQLEELLGELeelleALDEEE 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 548 LEKKLEQVMQQKctcdSTLEKDREaEYAAQLAELRQRLDHAEADRqELQDELRQEREARQKLEMMIKE 615
Cdd:COG4717   430 LEEELEELEEEL----EELEEELE-ELREELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 484-605 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  484 VRQQEKLNSILQRKQQLQMEVEMLS---SSKAMKELTEEQQNLQKELESLQSEHAqRMEEFYIEQRDLEKKLEQVMQQkc 560
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLkklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA-- 479

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2168696487  561 tcdstlekdreaeYAAQLAELRQRLDHAEADRQELQDELRQEREA 605
Cdd:TIGR02168  480 -------------AERELAQLQARLDSLERLQENLEGFSEGVKAL 511
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 470-620 2.87e-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: 44.01  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  470 DDKGKIMEDVMRTYVRQQEKLNsilqrKQQLQMEVEMLSSSKAMKELTEEQQNLQK---ELESLQSEHAQRMEEFYIEQR 546
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSKlknKHEAMISDLEERLKKEEKGRQ 204

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168696487  547 DLEKkleqvMQQKCTCDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:pfam01576  205 ELEK-----AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
450-610 3.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 450 RGTSKRDSEDSSPLLVR--DGEDDKGKIMEDVMRTYVRQQEKLNSIlqrkQQLQMEVEMLSSSKamKELTEEQQNLQKEL 527
Cdd:PRK02224  299 LAEAGLDDADAEAVEARreELEDRDEELRDRLEECRVAAQAHNEEA----ESLREDADDLEERA--EELREEAAELESEL 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 528 ESLQSEHAQRMEEfyieQRDLEKKLEQVMQQKCTCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELrqeREA 605
Cdd:PRK02224  373 EEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELREREAELEATLRTARERV---EEA 445


                  ....*
gi 2168696487 606 RQKLE 610
Cdd:PRK02224  446 EALLE 450
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
469-617 4.50e-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: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEmlssskamkELTEEQQNLQKELESLQSEhaqrmeefyIEqrDL 548
Cdd:COG2433   387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELEEKDER---------IE--RL 446

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 549 EKKLEQVMQQKctcDSTLEKDREAeyaaqlaelrQRLDhAEADRqeLQDELRQEREARQKLEMMIKELK 617
Cdd:COG2433   447 ERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEEERERIEELKRKLERLK 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 487-625 5.00e-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: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  487 QEKLNSILQRKQQLQMEVEMLSSskAMKELTEEQQNLQKELESLQSEHAQ---RMEEFYIEQRDLEKKLEQVMQQKctcd 563
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEEAANlreRLESLERRIAATERRLEDLEEQI---- 847

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168696487  564 stlekdreAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:TIGR02168  848 --------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
487-625 5.54e-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: 5.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  487 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHA------QRMEEFYIEQRDLEKKLEQVMQQKc 560
Cdd:COG4913    637 EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELDELKGEI- 715

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487  561 tcdSTLEKDREaEYAAQLAELRQRLDHAEAD-----RQELQDELRQ------EREARQKLEMMIKELKLQIGKSSK 625
Cdd:COG4913    716 ---GRLEKELE-QAEEELDELQDRLEAAEDLarlelRALLEERFAAalgdavERELRENLEERIDALRARLNRAEE 787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
485-601 6.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  485 RQQEKLNSILQRKQQLQMEVEML------SSSKAMKELTEEQQNLQKELESLQSEHAQRME-------EFYIEQRDLEKK 551
Cdd:COG4913    306 RLEAELERLEARLDALREELDELeaqirgNGGDRLEQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAAL 385

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2168696487  552 LEQVMQQKctcdsTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQ 601
Cdd:COG4913    386 RAEAAALL-----EALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 148-226 7.12e-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: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 148 GESISCFQVGGEKRLCLPQVLNSVLREF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 225
Cdd:cd21081    10 GAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                  .
gi 2168696487 226 L 226
Cdd:cd21081    90 L 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
517-625 7.29e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 7.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 517 TEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKctcdSTLEKDREaeyaaQLAELRQRLDHAEADRQELQ 596
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKE-----EIEELEKELESLEGSKRKLE 258

                          90       100
                  ....*....|....*....|....*....
gi 2168696487 597 DELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELEEKVKELKE 287
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 496-619 7.44e-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: 7.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 496 RKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFyieqrdlEKKLEQVMQQKCTCDSTLEKDREAEYA 575
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELR----KQLENY-------EKDKQSLKNLKARLKVLEKELKDLKWE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696487 576 AQLaeLRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQ 619
Cdd:pfam13851 108 HEV--LEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQ 152
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 485-580 8.40e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 563
Cdd:COG3883   130 ADADLLEELKADKAELEAKKAELEAKLAeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209

                          90
                  ....*....|....*..
gi 2168696487 564 STLEKDREAEYAAQLAE 580
Cdd:COG3883   210 AAAAAAAAAAAAAAAAA 226
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
518-620 8.87e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 518 EEQQNLQKELESLQSEHAQRmEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKdreAEYAAQLAELRQRLDHAEADRQELQ- 596
Cdd:COG4717    71 KELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEK---LEKLLQLLPLYQELEALEAELAELPe 146

                          90       100
                  ....*....|....*....|....*.
gi 2168696487 597 --DELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4717   147 rlEELEERLEELRELEEELEELEAEL 172
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
481-605 9.05e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 42.37  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 481 RTYVRQQEKLNSILQRKQQLQMEVEMLSSskAMKELTE------EQQNLQKELESLQseHAQR--------MEEFYIEQR 546
Cdd:COG0497   165 RAWRALKKELEELRADEAERARELDLLRF--QLEELEAaalqpgEEEELEEERRRLS--NAEKlrealqeaLEALSGGEG 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 547 DLEKKLEQVMQQkctcdstLEkdREAEYAAQLAELRQRLDHAEADRQELQDELRQEREA 605
Cdd:COG0497   241 GALDLLGQALRA-------LE--RLAEYDPSLAELAERLESALIELEEAASELRRYLDS 290
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
496-616 9.99e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 496 RKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkcTCDSTLEKDRE--AE 573
Cdd:PRK02224  322 RDEELRDRLE--ECRVAAQAHNEEAESLREDADDLEER-AEELRE---EAAELESELE-------EAREAVEDRREeiEE 388

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2168696487 574 YAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 616
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 503-622 1.04e-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: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  503 EVEMLSSSKAMKELTE---EQQNLQKELESLQSEHAQrMEEFYIEQRDLEKKLEQVMQQKctcdstlekDREAEYAAQLA 579
Cdd:COG3096    487 EVERSQAWQTARELLRryrSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQRI---------GQQLDAAEELE 556

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2168696487  580 ELRQRLdhaEADRQELQDELRQEREARQKLEMMIKELKLQIGK 622
Cdd:COG3096    557 ELLAEL---EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 487-539 1.07e-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: 1.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSKAmkELTEEQQNLQKELESLQSEHAQRME 539
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENE--ELKEEANELEEENQQLKQERNQWQE 60
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 469-595 1.09e-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: 40.66  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 469 EDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSK-AMKELTEEQQNLQKELESLQSEHA---QRMEEFYIE 544
Cdd:pfam13851  42 EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKqSLKNLKARLKVLEKELKDLKWEHEvleQRFEKVERE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2168696487 545 QRDLEKKLEQVM---QQKCTCDST-LEKdreaeyaaQLAELRQRLDHAEADRQEL 595
Cdd:pfam13851 122 RDELYDKFEAAIqdvQQKTGLKNLlLEK--------KLQALGETLEKKEAQLNEV 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
439-618 1.29e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 439 KKSESAVCSLVRGTSKRDSEDSSplLVRDGEDDKGKIME-----DVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAM 513
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKElekrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 514 KELtEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTC-------DSTLEKDREAEYAAQLAELRQRLD 586
Cdd:PRK03918  391 KEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRKELLEEYTAELKRIEKELK 469

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2168696487 587 HAEADRQELQDELRQEREARQKLEMMIKELKL 618
Cdd:PRK03918  470 EIEEKERKLRKELRELEKVLKKESELIKLKEL 501
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
485-620 1.30e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSI---LQRKQ--QLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyieqrdlEKKLEQVMQQK 559
Cdd:COG4372    77 QLEEELEELneqLQAAQaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 560 ctcdstlekdreaeyAAQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQI 620
Cdd:COG4372   149 ---------------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNA 196
DUF4175 pfam13779
Domain of unknown function (DUF4175);
486-615 1.35e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.90  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 486 QQEklnsILQRKQQLQ--MEvemlsssKAMKELTEEQQNLQKELESLQSEHAQRMeefyiEQRDLEKKLEQvMQQKctcd 563
Cdd:pfam13779 508 DEE----IAKLMQELReaLD-------DYMQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRMLDR-IEEL---- 566

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 564 stLEKDREAEYAAQLAELRQRLDHAE-ADRQELQDELRQE-REARQKLEMMIKE 615
Cdd:pfam13779 567 --ARSGRRAEAQQMLSQLQQMLENLQaGQPQQQQQQGQSEmQQAMDELGDLLRE 618
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
485-620 1.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSIL-QRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHaqrmeEFYIEQRDLEKKLEQVmqqkctc 562
Cdd:PRK03918  310 REIEKRLSRLeEEINGIEERIKELEEKEErLEELKKKLKELEKRLEELEERH-----ELYEEAKAKKEELERL------- 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 563 dstleKDREAEYaaQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:PRK03918  378 -----KKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
486-617 1.48e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 486 QQEKLNSILQRKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQ-------SEHAQRMEEFY---IEQRDLEKKLEQV 555
Cdd:PRK03918  540 EIKSLKKELEKLEELKKKLAELE--KKLDELEEELAELLKELEELGfesveelEERLKELEPFYneyLELKDAEKELERE 617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 556 MQQKCTCDSTLEKDRE---------------------------------------AEYA---AQLAELRQRLDHAEADRQ 593
Cdd:PRK03918  618 EKELKKLEEELDKAFEelaetekrleelrkeleelekkyseeeyeelreeylelsRELAglrAELEELEKRREEIKKTLE 697

                         170       180
                  ....*....|....*....|....
gi 2168696487 594 ELQDELRQEREARQKLEMMIKELK 617
Cdd:PRK03918  698 KLKEELEEREKAKKELEKLEKALE 721
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 484-625 1.50e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  484 VRQQEKLNSILQRKQQLQMEVEMlSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKlEQVMQQKCTcd 563
Cdd:pfam15921  428 VQRLEALLKAMKSECQGQMERQM-AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTA-- 503

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487  564 STLEKDREAEYA-AQLAELRQRLDhaeADRQELQdELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:pfam15921  504 SLQEKERAIEATnAEITKLRSRVD---LKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDK 562
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 500-627 1.73e-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: 40.90  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 500 LQMEVEMLSSSKAMkeLTEEQQNLQKELESLQSEhAQRMEEFYieQRDLEKKLEQVMQQKCTCDSTLEKDREAEyaAQLA 579
Cdd:pfam09787  45 LTLELEELRQERDL--LREEIQKLRGQIQQLRTE-LQELEAQQ--QEEAESSREQLQELEEQLATERSARREAE--AELE 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2168696487 580 ELRQRLDHAEadrqelqDELRQEREARQ----KLEMMIKELKLQIGKSSKPS 627
Cdd:pfam09787 118 RLQEELRYLE-------EELRRSKATLQsrikDREAEIEKLRNQLTSKSQSS 162
46 PHA02562
endonuclease subunit; Provisional
 485-620 1.81e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQlqMEVEMLSSSKAMK----ELTEEQQNLQKELESlQSEHAQRMEEFYIeqrDLEKKLEQ-----V 555
Cdd:PHA02562  206 EQRKKNGENIARKQN--KYDELVEEAKTIKaeieELTDELLNLVMDIED-PSAALNKLNTAAA---KIKSKIEQfqkviK 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168696487 556 MQQK---C-TCDSTLEK--DREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKlemmIKELKLQI 620
Cdd:PHA02562  280 MYEKggvCpTCTQQISEgpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK----LLELKNKI 346
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 486-620 1.93e-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: 41.16  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 486 QQEKLNSILQRKQQlqmEVEmlSSSKAMKELTEEQQNLQKELESLQSEHAQR-MEEFYIEQRDLEKKLEQVmqqkctcDS 564
Cdd:TIGR04523 261 EQNKIKKQLSEKQK---ELE--QNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEI-------QN 328

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 565 TLEKDREA--EYAAQLAELRQRLDHAEADRQELQDELRQ--------EREARQKLEmMIKELKLQI 620
Cdd:TIGR04523 329 QISQNNKIisQLNEQISQLKKELTNSESENSEKQRELEEkqneieklKKENQSYKQ-EIKNLESQI 393
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
487-620 1.94e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQsehaQRMEEFYIEQR--DLEKKLEQVMQQKctcdS 564
Cdd:COG3206   151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGlvDLSEEAKLLLQQL----S 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 565 TLEKDReAEYAAQLAELRQRLDHAEADRQ-------------ELQDELRQEREARQKLEMM----------IKELKLQI 620
Cdd:COG3206   223 ELESQL-AEARAELAEAEARLAALRAQLGsgpdalpellqspVIQQLRAQLAELEAELAELsarytpnhpdVIALRAQI 300
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 456-624 1.99e-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: 41.25  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 456 DSEDSSPLLVRDGEDDKGKiMEDVMRTYVRQQEKLNSiLQRKQQLQmevemlssSKAMKELTEEQQNLQKELESLQSEHA 535
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENK-MKDLTFLLEESRDKANQ-LEEKTKLQ--------DENLKELIEKKDHLTKELEDIKMSLQ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 536 QRMEefyiEQRDLEKKLEqvMQQKCTCDSTLEKDreaeyaAQLAEL-RQRLDHA------EADRQELQDELRQEREARQK 608
Cdd:pfam05483 307 RSMS----TQKALEEDLQ--IATKTICQLTEEKE------AQMEELnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEK 374

                         170
                  ....*....|....*.
gi 2168696487 609 LEMMIKELKLQIGKSS 624
Cdd:pfam05483 375 NEDQLKIITMELQKKS 390
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 490-552 2.27e-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: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 490 LNSILQR-KQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQS--EHAQRMEEFYIEQRDLEKKL 552
Cdd:cd14798     5 VSFLLEKlGELLEQEADLLSGVK------EEIESLKDELESMQAflKDADAKQDEDEELKDWVKQV 64
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
480-619 2.39e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 480 MRTYVRQqeKLNSILQR----KQQLQMEV-EMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEefyieqrDLEKKLEQ 554
Cdd:COG1842     6 LSDIIRA--NINALLDKaedpEKMLDQAIrDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-------KWEEKARL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 555 vmqqkctcdsTLEKDREA---EYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 619
Cdd:COG1842    77 ----------ALEKGREDlarEALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK 134
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 505-622 2.50e-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: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 505 EMLSSSKAMKELTEEQQNLQKELESLQSEhaqrmeefyieqrdLEKKLEQVMQQKCTCDSTLEKdREAEYAAQLAELRQR 584
Cdd:pfam03938  13 ESPEGKAAQAQLEKKFKKRQAELEAKQKE--------------LQKLYEELQKDGALLEEEREE-KEQELQKKEQELQQL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2168696487 585 ldhaeadRQELQDELRQER-EARQKLEMMIKELKLQIGK 622
Cdd:pfam03938  78 -------QQKAQQELQKKQqELLQPIQDKINKAIKEVAK 109
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 487-553 2.56e-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: 37.26  E-value: 2.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQSEHaqrmEEFYIEQRDLEKKLE 553
Cdd:COG3074    10 EAKVQQAVDTIELLQMEVEELKEKN--EELEQENEELQSENEELQSEN----EQLKTENAEWQERIR 70
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 487-621 3.28e-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: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 487 QEKLNSILQRKQQLQMEVEMLSS---SKAMKELTEEQQNLQKELESLQSEHAQRMEEFyieQRDLEKKLEQVmqqkctcd 563
Cdd:pfam01442   3 EDSLDELSTYAEELQEQLGPVAQelvDRLEKETEALRERLQKDLEEVRAKLEPYLEEL---QAKLGQNVEEL-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 564 stlekdrEAEYAAQLAELRQRLdhaEADRQELQDELRQE-REARQKLEMMIKELKLQIG 621
Cdd:pfam01442  72 -------RQRLEPYTEELRKRL---NADAEELQEKLAPYgEELRERLEQNVDALRARLA 120
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 503-601 3.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 503 EVEMLSSSKAMKELTEEQQNLQKELESLQSEhAQRMEEfyiEQRDLEKKLEqvmqqkctcdstlekdrEAEyaAQLAELR 582
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELE-----------------ALQ--AEIDKLQ 71

                          90
                  ....*....|....*....
gi 2168696487 583 QRLDHAEADRQELQDELRQ 601
Cdd:COG3883    72 AEIAEAEAEIEERREELGE 90
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 485-619 3.47e-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: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCD 563
Cdd:pfam15558  17 HKEEQRMRELQQQAALAWEELRRRDQKRqETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRW 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 564 STLEKDREA------EYAAQLAELR-----QRLDHAEADRQELQDE---LRQEREARQKLEMMIKELKLQ 619
Cdd:pfam15558  97 REQAEDQENqrqeklERARQEAEQRkqcqeQRLKEKEEELQALREQnslQLQERLEEACHKRQLKEREEQ 166
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
513-620 3.62e-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: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  513 MKELTEEQQNLQKELEslQSEHAQRMEEFYieqRDLEKKLEQVMQQKcTCDSTLEKDREAEyaaQLAELRQRLDHAEADR 592
Cdd:COG4913    234 FDDLERAHEALEDARE--QIELLEPIRELA---ERYAAARERLAELE-YLRAALRLWFAQR---RLELLEAELEELRAEL 304

                           90       100
                   ....*....|....*....|....*...
gi 2168696487  593 QELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQI 332
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 477-619 3.63e-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: 40.32  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 477 EDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKElTEEQQNLQKEleslQSEHAQRMEEfyieqrdlEKKLEQvm 556
Cdd:pfam15709 318 EDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRRE-QEEQRRLQQE----QLERAEKMRE--------ELELEQ-- 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168696487 557 qQKCTCDSTLEKDReaeyaaqLAELRQRLDHAEAdRQELQDELRQEREARQKLEMMIKELKLQ 619
Cdd:pfam15709 383 -QRRFEEIRLRKQR-------LEEERQRQEEEER-KQRLQLQAAQERARQQQEEFRRKLQELQ 436
valS PRK05729
valyl-tRNA synthetase; Reviewed
 516-586 3.75e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 40.47  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 516 LTEEQQNLQKELESLQSEhaqrmeefyIEQrdLEKKL----------EQVMQQkctcdstlEKDREAEYAAQLAELRQRL 585
Cdd:PRK05729  809 VEAELARLEKELAKLEKE---------IER--VEKKLsnegfvakapEEVVEK--------EREKLAEYEEKLAKLKERL 869


                  .
gi 2168696487 586 D 586
Cdd:PRK05729  870 A 870
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 474-615 3.96e-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: 39.56  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 474 KIMEDVMRTYVRQQEKLNSIL---QRKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLE 549
Cdd:cd07671    22 KDVEELLKQRAQAEERYGKELvqiARKAGGQTEINTLKASfDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168696487 550 KKLEQVMQQ---------KCTCDSTL---EKDREAEYAAQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKE 615
Cdd:cd07671   102 KKYEAVMERvqkskvslyKKTMESKKtyeQRCREADEAEQTFERSSSTGNPK-QSEKSQNKAKQCRDAATEAERVYKQ 178
PTZ00121 PTZ00121
MAEBL; Provisional
 416-629 4.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  416 ASQSKEATKAETNSSISNNSTSRKKSESAVCSLVRGTS-KRDSEDSSPLLVRDGEDDKG---KIMEDVMRTY-------V 484
Cdd:PTZ00121  1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEeAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYeeekkmkA 1609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  485 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDS 564
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487  565 TLEK-DREAEYAAQLAELRQRldhaEADRQELQDELRQEREARQ-KLEMMIKELKLQIGKSSKPSKD 629
Cdd:PTZ00121  1690 AAEAlKKEAEEAKKAEELKKK----EAEEKKKAEELKKAEEENKiKAEEAKKEAEEDKKKAEEAKKD 1752
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
515-622 4.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  515 ELTEEQQNLQKELESLQSEHAQRMEEfYIEQRDLEKKLEQVMQQKCtcdSTLEKDREAEYAAQLAELRQRLDHAEADRQE 594
Cdd:COG4913    245 EDAREQIELLEPIRELAERYAAARER-LAELEYLRAALRLWFAQRR---LELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2168696487  595 LQDELRQEREARQK--------LEMMIKELKLQIGK 622
Cdd:COG4913    321 LREELDELEAQIRGnggdrleqLEREIERLERELEE 356
PRK09039 PRK09039
peptidoglycan -binding protein;
485-596 4.13e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSIL----QRKQQLQMEVEMLSSSKAMKELTEEQ-QNLQKELESLQSEHAQRM--------EEFYIEQR----- 546
Cdd:PRK09039   60 SQIAELADLLslerQGNQDLQDSVANLRASLSAAEAERSRlQALLAELAGAGAAAEGRAgelaqeldSEKQVSARalaqv 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2168696487 547 -DLEKKLEQVMQQKCTCDSTLE--KDREAEYAAQLAELRQRLDHAEADR-QELQ 596
Cdd:PRK09039  140 eLLNQQIAALRRQLAALEAALDasEKRDRESQAKIADLGRRLNVALAQRvQELN 193
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 485-614 4.28e-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: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 485 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEfyIEQRDLEKKLEQVMQQKCTCDS 564
Cdd:pfam05672  20 RRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEE--ERQRKAEEEAEEREQREQEEQE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2168696487 565 TLEKDRE-AEYAAQLAELRQRLdhaEADRQELQDElrQEREARQK-LEMMIK 614
Cdd:pfam05672  98 RLQKQKEeAEAKAREEAERQRQ---EREKIMQQEE--QERLERKKrIEEIMK 144
PRK09039 PRK09039
peptidoglycan -binding protein;
516-621 4.35e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 516 LTEEQQNLQKELESLQSEHAQRMEEFYIEQR---DLEKKLEQVMQQKctcdSTLEKDReAEYAAQLAELRQRLDHAEADR 592
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADLLSLERQgnqDLQDSVANLRASL----SAAEAER-SRLQALLAELAGAGAAAEGRA 118

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2168696487 593 QELQDELRQER----EARQKLEMM---IKELKLQIG 621
Cdd:PRK09039  119 GELAQELDSEKqvsaRALAQVELLnqqIAALRRQLA 154
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 544-622 4.44e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168696487 544 EQRDLEKKLEQVMQQKctcdSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGK 622
Cdd:COG0542   412 ELDELERRLEQLEIEK----EALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
PTZ00121 PTZ00121
MAEBL; Provisional
 466-615 4.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  466 RDGEDDKGKIMEDVMRT-YVRQQEKLNSIlqRKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESL--QSEHAQRMEEFY 542
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAeELKKAEEENKI--KAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELK 1708

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487  543 IEQRDLEKKLEQVMQQKCTCDSTLEK-DREAEYAAQLAElRQRLDHAEADR--QELQDELRQEREARQKLEMMIKE 615
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAE-EAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 474-585 5.30e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 474 KIMEDVMRTYVRQQEKLNSILQRKQQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKL 552
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2168696487 553 EQVMQQkctcdstLEKDREAEYAAQLAELRQRL 585
Cdd:COG4942   230 ARLEAE-------AAAAAERTPAAGFAALKGKL 255
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 486-625 5.39e-03

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: 40.16  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  486 QQEKLNSILQRKQ------QLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRmEEFYIEQRDLEKKLEQVMQQ- 558
Cdd:pfam01576  230 QIAELRAQLAKKEeelqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR-NKAEKQRRDLGEELEALKTEl 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  559 KCTCDST-----LEKDREAEYA--------------AQLAELRQR-----------LDHA--------------EADRQE 594
Cdd:pfam01576  309 EDTLDTTaaqqeLRSKREQEVTelkkaleeetrsheAQLQEMRQKhtqaleelteqLEQAkrnkanlekakqalESENAE 388

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2168696487  595 LQDELR------QERE-ARQKLEMMIKELKLQIGKSSK 625
Cdd:pfam01576  389 LQAELRtlqqakQDSEhKRKKLEGQLQELQARLSESER 426
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
 519-599 5.56e-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: 36.90  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 519 EQQNLQ--KELESLQSEHAQRMEEFYIEQRDLEKK---LEQVMQQkctcdstLEKDREaEYAAQLAELRQRLDHAEADRQ 593
Cdd:pfam14739   2 EEEKLQisKALVDLQIENNKLREQYEAEKFELKNKllnLENRVLE-------LELRLE-KAAEEIQDLRERLRELEDDRR 73


                  ....*.
gi 2168696487 594 ELQDEL 599
Cdd:pfam14739  74 ELAEEF 79
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
486-610 6.50e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.64  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 486 QQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELE----SLQSEHAQRMEEFYIEQRDLEKKLEQvmqqkct 561
Cdd:COG3064    23 AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqraaELAAEAAKKLAEAEKAAAEAEKKAAA------- 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2168696487 562 cdstlEKDREAEYAAQLAELRQRLDHAEADRQElQDELRQEREARQKLE 610
Cdd:COG3064    96 -----EKAKAAKEAEAAAAAEKAAAAAEKEKAE-EAKRKAEEEAKRKAE 138
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 519-622 6.58e-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: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 519 EQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKleqvmqqkctcdstlekdrEAEYAAQLAELRQRLDHAEADRQELQDE 598
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKK-------------------EQELKEDLIKFDKFLKENDAKRRRALKK 67

                          90       100
                  ....*....|....*....|....
gi 2168696487 599 LRQEREARQKLEMMIKELKLQIGK 622
Cdd:pfam13863  68 AEEETKLKKEKEKEIKKLTAQIEE 91
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 485-619 6.66e-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: 39.57  E-value: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  485 RQQEKLNSILQRKQQLQMEVEMLSSSKAMKE-LTEEQQnlqKELESLQSEHAQRMEEFYIE-QRDLEKKLEQVMQQKCTC 562
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDiLQREQA---TIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITC 449

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487  563 DSTLEKDREAEyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 619
Cdd:TIGR00618  450 TAQCEKLEKIH----LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 495-620 7.24e-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: 39.13  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 495 QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYieQRDLEKKLEQVMQQKCTCDSTLEKDRE-AE 573
Cdd:pfam13868 216 ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--ERMLRKQAEDEEIEQEEAEKRRMKRLEhRR 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2168696487 574 YAAQLAELRQRLdhAEADRQELQDELRQEREARQKLEMMIKELKLQI 620
Cdd:pfam13868 294 ELEKQIEEREEQ--RAAEREEELEEGERLREEEAERRERIEEERQKK 338
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 486-625 8.12e-03

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: 39.39  E-value: 8.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487  486 QQEKLNSILQRK---QQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQrmeefyieqrdLEKKLEQVMQQKCT 561
Cdd:pfam01576  397 QQAKQDSEHKRKkleGQLQeLQARLSESERQRAELAEKLSKLQSELESVSSLLNE-----------AEGKNIKLSKDVSS 465

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487  562 CDSTLEKDRE--AEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:pfam01576  466 LESQLQDTQEllQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 496-617 9.00e-03

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: 39.07  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 496 RKQQLQMEVEMLSSSKAMKE----LTEEQQNLQKELESLQSEHAQRMEE-FYIEQRDLEKKLEQVMQQ---------KCT 561
Cdd:pfam06160 178 REVLEKLEEETDALEELMEDipplYEELKTELPDQLEELKEGYREMEEEgYALEHLNVDKEIQQLEEQleenlalleNLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 562 CDSTLEKDR-------------EAEYAA------QLAELRQRLDHAEADRQELQDELRQ----------EREARQKLEMM 612
Cdd:pfam06160 258 LDEAEEALEeieeridqlydllEKEVDAkkyvekNLPEIEDYLEHAEEQNKELKEELERvqqsytlnenELERVRGLEKQ 337


                  ....*
gi 2168696487 613 IKELK 617
Cdd:pfam06160 338 LEELE 342
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 501-620 9.27e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 38.86  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 501 QMEVEMLSSSKAMKELT---EEQQNLQKELESLQSEH---AQRMEEFYIEQRDLEKKLEqvmqqkctcDSTLE-----KD 569
Cdd:pfam05701 125 QLEVAKARHAAAVAELKsvkEELESLRKEYASLVSERdiaIKRAEEAVSASKEIEKTVE---------ELTIEliatkES 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2168696487 570 REAEYAAQLAELRQRLDHAEADRqelQDELRQEREARQkLEMMIKELKLQI 620
Cdd:pfam05701 196 LESAHAAHLEAEEHRIGAALARE---QDKLNWEKELKQ-AEEELQRLNQQL 242
PRK01156 PRK01156
chromosome segregation protein; Provisional
 489-625 9.32e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 9.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 489 KLNSILQRKQQLQMEVEMLSS--SKAMKELTEEQQNLQKELESLQSEHAQRMEefyieqrdLEKKLEQVMQQKCTCDSTl 566
Cdd:PRK01156  595 QLNDLESRLQEIEIGFPDDKSyiDKSIREIENEANNLNNKYNEIQENKILIEK--------LRGKIDNYKKQIAEIDSI- 665

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168696487 567 eKDREAEYAAQLAE-------LRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSK 625
Cdd:PRK01156  666 -IPDLKEITSRINDiednlkkSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 497-617 9.40e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.85  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 497 KQQLQMEVEMLSSSKAmkELTEEQQNLQKELESlQSEHAQRMEEFYieqrdlekklEQVMQQKCTCDSTLEKDREaeyaa 576
Cdd:pfam07926   3 LSSLQSEIKRLKEEAA--DAEAQLQKLQEDLEK-QAEIAREAQQNY----------ERELVLHAEDIKALQALRE----- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2168696487 577 QLAELRQRLDHAEADRQELQDELRQER----EARQKLEMMIKELK 617
Cdd:pfam07926  65 ELNELKAEIAELKAEAESAKAELEESEesweEQKKELEKELSELE 109
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
495-615 9.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168696487 495 QRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHA---QRMEEFYIEQRDLEKKLEQVMQ----QKC-TC---- 562
Cdd:PRK02224  382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrEREAELEATLRTARERVEEAEAlleaGKCpECgqpv 461

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168696487 563 -DS----TLEKDRE--AEYAAQLAELR-------QRLDHAEaDRQELQDELRQEREARQKLEMMIKE 615
Cdd:PRK02224  462 eGSphveTIEEDRErvEELEAELEDLEeeveeveERLERAE-DLVEAEDRIERLEERREDLEELIAE 527
 
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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