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Conserved domains on  [gi|223029420|ref|NP_001138569|]
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ski-like protein isoform 2 [Homo sapiens]

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 ...
 137-236 1.94e-66

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


:

Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.51  E-value: 1.94e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 137 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 216
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 223029420 217 SCGLITLTDAQRLCNALLRP 236
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 ...
 261-356 8.02e-58

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


:

Pssm-ID: 198114  Cd Length: 95  Bit Score: 189.50  E-value: 8.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   261 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 340
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 223029420   341 EKKLKIILEEMKEKFS 356
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 490-638 6.17e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 490 RTYLKQQEKL-----NLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:COG1196  213 ERYRELKEELkeleaELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420 565 mkqkctcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG1196  291 ---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 137-236 1.94e-66

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.51  E-value: 1.94e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 137 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 216
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 223029420 217 SCGLITLTDAQRLCNALLRP 236
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 ...
 261-356 8.02e-58

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


Pssm-ID: 198114  Cd Length: 95  Bit Score: 189.50  E-value: 8.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   261 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 340
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 223029420   341 EKKLKIILEEMKEKFS 356
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 ...
 261-355 9.81e-56

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


Pssm-ID: 462602  Cd Length: 94  Bit Score: 184.01  E-value: 9.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  261 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 340
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 223029420  341 EKKLKIILEEMKEKF 355
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. ...
 136-235 5.17e-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: 163.22  E-value: 5.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  136 IPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 215
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 223029420  216 PSCGLITLTDAQRLCNALLR 235
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 490-638 6.17e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 490 RTYLKQQEKL-----NLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:COG1196  213 ERYRELKEELkeleaELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420 565 mkqkctcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG1196  291 ---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 504-638 6.18e-08

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: 55.80  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  504 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKdlEKKLEQIMKQKctcDSNLEKDKEAEy 583
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE--LEEK--QNEIEKLKKEN---QSYKQEIKNLE- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029420  584 aGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:TIGR04523 391 -SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
PRK12704 PRK12704
phosphodiesterase; Provisional
 493-638 2.73e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.63  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 493 LKQQEKlnlILQKKQQLQMEVKmlsssKSMKELTE-EQQNLQKElESLQNehaqRMEEFYVEQKDLEKKLEQIMKQKctc 571
Cdd:PRK12704  60 LEAKEE---IHKLRNEFEKELR-----ERRNELQKlEKRLLQKE-ENLDR----KLELLEKREEELEKKEKELEQKQ--- 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029420 572 dSNLEKdKEAEYAGQLAELRQRLDH-----AEADRQELQDELrqEREARQKLEMMIKELKLQI-LKSSKTAKE 638
Cdd:PRK12704 124 -QELEK-KEEELEELIEEQLQELERisgltAEEAKEILLEKV--EEEARHEAAVLIKEIEEEAkEEADKKAKE 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 478-629 1.16e-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: 51.07  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  478 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEV-KMLSSSKSMKELTEEQQNLQKE-LESLQNEHAQRMEEFYVEQK 555
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420  556 DLEKKLEQIMkQKCTCDSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:pfam13868 177 EIEEEKEREI-ARLRAQQEKAQDEKAE----RDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 478-626 1.92e-05

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.80  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 478 EDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQL-QMEVKMlsssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyvEQK 555
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420 556 DLEKKLEQimkqkctcdsnLEKDKEAEYAGQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 626
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 522-624 2.90e-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: 44.11  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   522 MKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQrldhaeaDR 601
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR-------KQ 78

                           90       100
                   ....*....|....*....|....
gi 223029420   602 QELQDELRQER-EARQKLEMMIKE 624
Cdd:smart00935  79 QKLQQDLQKRQqEELQKILDKINK 102
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 137-236 1.94e-66

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.51  E-value: 1.94e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 137 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 216
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 223029420 217 SCGLITLTDAQRLCNALLRP 236
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 ...
 261-356 8.02e-58

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


Pssm-ID: 198114  Cd Length: 95  Bit Score: 189.50  E-value: 8.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   261 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 340
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 223029420   341 EKKLKIILEEMKEKFS 356
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 ...
 261-355 9.81e-56

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


Pssm-ID: 462602  Cd Length: 94  Bit Score: 184.01  E-value: 9.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  261 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 340
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 223029420  341 EKKLKIILEEMKEKF 355
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 144-234 2.83e-52

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: 174.29  E-value: 2.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 144 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 223
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                         90
                 ....*....|.
gi 223029420 224 TDAQRLCNALL 234
Cdd:cd21079   81 TDAERLCSALL 91
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 137-234 7.36e-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: 165.63  E-value: 7.36e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 137 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 216
Cdd:cd21083    3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                         90
                 ....*....|....*...
gi 223029420 217 SCGLITLTDAQRLCNALL 234
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. ...
 136-235 5.17e-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: 163.22  E-value: 5.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  136 IPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 215
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 223029420  216 PSCGLITLTDAQRLCNALLR 235
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 144-231 7.83e-34

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


Pssm-ID: 410781  Cd Length: 88  Bit Score: 123.94  E-value: 7.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 144 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 223
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                 ....*...
gi 223029420 224 TDAQRLCN 231
Cdd:cd21074   81 SDAERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 144-234 4.42e-16

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


Pssm-ID: 410783  Cd Length: 91  Bit Score: 73.63  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 144 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 223
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                         90
                 ....*....|.
gi 223029420 224 TDAQRLCNALL 234
Cdd:cd21080   81 REAERLCKSFL 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 490-638 6.17e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 490 RTYLKQQEKL-----NLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:COG1196  213 ERYRELKEELkeleaELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420 565 mkqkctcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG1196  291 ---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
496-629 1.13e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  496 QEKLNLILQKKQQLQMEVKmlsssksmkELTEEQQNLQKELESLQN--EHAQRMEEFYVEQKD---LEKKLEQIMKQKct 570
Cdd:COG4913   609 RAKLAALEAELAELEEELA---------EAEERLEALEAELDALQErrEALQRLAEYSWDEIDvasAEREIAELEAEL-- 677

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420  571 cdSNLEKDKeaeyaGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:COG4913   678 --ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 504-638 6.18e-08

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: 55.80  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  504 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKdlEKKLEQIMKQKctcDSNLEKDKEAEy 583
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE--LEEK--QNEIEKLKKEN---QSYKQEIKNLE- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029420  584 aGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:TIGR04523 391 -SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 490-629 1.07e-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: 55.45  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   490 RTYLKQQEKLNLILQKKQQLQMEVKMLSSSKsmKELTEEQQNLQKELESLQnehaQRMEEFyveQKDLEKKLEQIMKQKC 569
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE----ELIEEL---ESELEALLNERASLEE 887

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   570 tcDSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:TIGR02168  888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK12704 PRK12704
phosphodiesterase; Provisional
 493-638 2.73e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.63  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 493 LKQQEKlnlILQKKQQLQMEVKmlsssKSMKELTE-EQQNLQKElESLQNehaqRMEEFYVEQKDLEKKLEQIMKQKctc 571
Cdd:PRK12704  60 LEAKEE---IHKLRNEFEKELR-----ERRNELQKlEKRLLQKE-ENLDR----KLELLEKREEELEKKEKELEQKQ--- 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029420 572 dSNLEKdKEAEYAGQLAELRQRLDH-----AEADRQELQDELrqEREARQKLEMMIKELKLQI-LKSSKTAKE 638
Cdd:PRK12704 124 -QELEK-KEEELEELIEEQLQELERisgltAEEAKEILLEKV--EEEARHEAAVLIKEIEEEAkEEADKKAKE 192
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
502-619 2.85e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  502 ILQKKQQLQmevKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDSNLEKDKEA 581
Cdd:COG4913   670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 223029420  582 EYAGQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 619
Cdd:COG4913   743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 503-631 3.12e-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: 51.85  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 503 LQKKQQLQMEVKmlssskSMKELteeqQNLQKELESLQNEhaqrmeefyveQKDLEKKLEQIMKQKCTCDSNLEKDKEae 582
Cdd:COG1579   75 IKKYEEQLGNVR------NNKEY----EALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEA-- 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029420 583 yagQLAELRQRLDHAEADRQELQDELRQEREA-RQKLEMMIKELKLQILK 631
Cdd:COG1579  132 ---ELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPELLA 178
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
496-628 3.16e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 3.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 496 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRmEEFYVEQKDLEKKLEQI---MKQKCTCD 572
Cdd:COG4717  108 EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELqeeLEELLEQL 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223029420 573 SNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 628
Cdd:COG4717  187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 484-626 1.06e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 51.75  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 484 IMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlsssksMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQ 563
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERE---------LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK 573

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223029420 564 IMKQKctcdsnLEKDKEaEYAGQLAELR--QRLDHAEADRQELQDELRQEREARQKLEMMIKELK 626
Cdd:PRK00409 574 EAQQA------IKEAKK-EADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQK 631
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 478-629 1.16e-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: 51.07  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  478 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEV-KMLSSSKSMKELTEEQQNLQKE-LESLQNEHAQRMEEFYVEQK 555
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKELEKEEEREEDErILEYLKEKAEREEEREAERE 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420  556 DLEKKLEQIMkQKCTCDSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:pfam13868 177 EIEEEKEREI-ARLRAQQEKAQDEKAE----RDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 478-632 1.16e-06

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: 51.99  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   478 EDDKGKIMEEVMRTYLK-QQEKLNLILQKKQQLQMEVKMLSSS-----KSMKELTEEQQNLQKELESLQnehaQRMEEFY 551
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARlreieQKLNRLTLEKEYLEKEIQELQ----EQRIDLK 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   552 VEQKDLEKKLEQIMKQKCTCDSNLEkdkeaEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLE-------MMIKE 624
Cdd:TIGR02169  847 EQIKSIEKEIENLNGKKEELEEELE-----ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSE 921

                          170
                   ....*....|
gi 223029420   625 L--KLQILKS 632
Cdd:TIGR02169  922 LkaKLEALEE 931
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 504-638 1.36e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   504 QKKQQLQMEVKMLSSSksMKELTEEQQNLQKELE-------SLQNEHAQRMEEFYV---EQKDLEKKLEQIMKQKctcdS 573
Cdd:TIGR02168  239 EELEELQEELKEAEEE--LEELTAELQELEEKLEelrlevsELEEEIEELQKELYAlanEISRLEQQKQILRERL----A 312

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223029420   574 NLEKDKEaEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL--KLQILKSSKTAKE 638
Cdd:TIGR02168  313 NLERQLE-ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaELEELESRLEELE 378
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
476-626 1.88e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 476 ICEDDKGKIMEE-------VMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRME 548
Cdd:PRK03918 445 LTEEHRKELLEEytaelkrIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA 524

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420 549 EFYVEqkdLEKKLEQIMKQKCTCDSNLEKDKEAEyaGQLAELRQRLDHAEADRQELQDELRQER-EARQKLEMMIKELK 626
Cdd:PRK03918 525 EEYEK---LKEKLIKLKGEIKSLKKELEKLEELK--KKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
494-629 2.36e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQnEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdS 573
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELEAEL----A 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223029420 574 NLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:COG4717  174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 513-624 3.14e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 50.47  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 513 VKMLSSSK--SMKELTEEQQNLQKELESLQNE----HAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnlekDKEAEYAGQ 586
Cdd:COG0542  402 VRMEIDSKpeELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEE 472

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 223029420 587 LAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 624
Cdd:COG0542  473 IQELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 494-630 3.24e-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: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKctcdS 573
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----A 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223029420 574 NLEKDKEAEYAgQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 630
Cdd:COG1196  327 ELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 494-635 3.27e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   494 KQQEKLNLILQKKQQ----LQMEVKMLSSS-----KSMKELTEEQQNLQKELESLQNEHA---QRMEEFYVEQKDLEKKL 561
Cdd:TIGR02168  239 EELEELQEELKEAEEeleeLTAELQELEEKleelrLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   562 EQIMKQKCTCDSNLEKDKE---------AEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 632
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEelaeleeklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398


                   ...
gi 223029420   633 SKT 635
Cdd:TIGR02168  399 NNE 401
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 520-632 4.46e-06

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: 49.85  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  520 KSMKELTEEQQNLQKELESLQneHAQRMEEFYVE-QKDLEKKLEQIMKQKCTCDSNLEKDKEA--EYAGQLAELRQRLDH 596
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLEELEKRYDEIVERLEEKEVAysELQEELEEILEQLEE 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 223029420  597 AEADRQELQDELR----QEREARQKLEMMIKEL---KLQILKS 632
Cdd:pfam06160 376 IEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVEKS 418
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
483-626 5.00e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 483 KIMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlsssksMKELTEEQQNLQKELESLqnEHAQRMEEFYVEQKDLEKKLE 562
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEE---------LEELEAELEELREELEKL--EKLLQLLPLYQELEALEAELA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420 563 QIMKQkctcdsnLEKDKEAEyaGQLAELRQRLDHAEADRQELQDELRQERE-----ARQKLEMMIKELK 626
Cdd:COG4717  143 ELPER-------LEELEERL--EELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELE 202
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
489-634 5.04e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  489 MRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSmkELTEEQQNLQKELESLQNEHAQ----RMEEFYVEQKDLEKKLEQI 564
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELE--RLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEER 357

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420  565 ------MKQKC-TCDSNLEKDkEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK--LQILKSSK 634
Cdd:COG4913   358 errrarLEALLaALGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeIASLERRK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 494-638 5.07e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEFY-----------VEQKDLEKK-- 560
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplallLSPEDFLDAvr 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 561 ----LEQIMKQKctcdsnleKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTA 636
Cdd:COG4942  137 rlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208


                 ..
gi 223029420 637 KE 638
Cdd:COG4942  209 AE 210
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
492-638 5.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 492 YLKQQEKLNLILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEfyVEQKDLEKKLEQIMKQKCT 570
Cdd:COG4717   59 FKPQGRKPELNLKELKELEEELKEAEEKeEEYAELQEELEELEEELEELEAELEELREE--LEKLEKLLQLLPLYQELEA 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029420 571 CDSNLekdkeAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4717  137 LEAEL-----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
PRK11637 PRK11637
AmiB activator; Provisional
 492-616 5.75e-06

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 49.31  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 492 YLKQ--QEKLNLILQKKQQLQMEVKMLsssksmkeltEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEqimkqkc 569
Cdd:PRK11637 163 YLNQarQETIAELKQTREELAAQKAEL----------EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLE------- 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029420 570 tcdSNLEKDKEaeyagQLAELRQ---RLDHAEAdRQELQDELRQEREARQ 616
Cdd:PRK11637 226 ---SSLQKDQQ-----QLSELRAnesRLRDSIA-RAEREAKARAEREARE 266
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 147-231 6.78e-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: 44.64  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 147 TVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDA 226
Cdd:cd21082    4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDV 83


                 ....*
gi 223029420 227 QRLCN 231
Cdd:cd21082   84 ERLYS 88
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 450-638 7.30e-06

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 49.29  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  450 NLVRDINKVgigLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQ-LQMEVKMLSSSKSMKELTEE 528
Cdd:pfam13166 287 RLQKLIEKV---ESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRaLEAKRKDPFKSIELDSVDAK 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  529 QQN---LQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctCDSNLEKDKEAeYAGqlaelrqrldhAEADRQELQ 605
Cdd:pfam13166 364 IESindLVASINELIAKHNEITDNFEEEKNKAKKKLRLHLVEE--FKSEIDEYKDK-YAG-----------LEKAINSLE 429

                         170       180       190
                  ....*....|....*....|....*....|...
gi 223029420  606 DELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:pfam13166 430 KEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 519-619 7.39e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 519 SKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnlekdkeAEYAGQLAELRQRLDHAE 598
Cdd:COG3883  128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLSAEEAAAE 195

                         90       100
                 ....*....|....*....|.
gi 223029420 599 ADRQELQDELRQEREARQKLE 619
Cdd:COG3883  196 AQLAELEAELAAAEAAAAAAA 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 485-638 7.42e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 7.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   485 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKsmKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   565 MKQKCTCDSNLEKDKEAE------------YAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 632
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEaeieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843


                   ....*.
gi 223029420   633 SKTAKE 638
Cdd:TIGR02168  844 EEQIEE 849
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 471-626 9.55e-06

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: 48.05  E-value: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  471 LVKDVICEDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQLQMEVKMLSSSKSMKELTEEQQnlqKELESLQNEHAQRMEE 549
Cdd:pfam02841 160 LEAKYNQVPRKGVKAEEVLQEFLQSKEAVeEAILQTDQALTAKEKAIEAERAKAEAAEAEQ---ELLREKQKEEEQMMEA 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420  550 FYVEQKDLEKKLEQIMkqkctcdsnlekdkEAEYAGQLAELRQRLDHaeaDRQElQDELRQE--REARQKLEMMIKELK 626
Cdd:pfam02841 237 QERSYQEHVKQLIEKM--------------EAEREQLLAEQERMLEH---KLQE-QEELLKEgfKTEAESLQKEIQDLK 297
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
490-630 9.94e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 490 RTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQimkqkc 569
Cdd:COG4717  395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE----LAELEAELEQ------ 464

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420 570 tcdsnLEKDkeaeyaGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 630
Cdd:COG4717  465 -----LEED------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
485-634 1.30e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 485 MEEVMRTYLKQQEKLNLILQKKQQLqmevkmlssSKSMKELTEEQQNLQKELESLQNEHAqRMEEFYVEQKDLEKKLEQI 564
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREI---------EKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEEL 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 565 ---------MKQKCTcdsNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI--LKSS 633
Cdd:PRK03918 358 eerhelyeeAKAKKE---ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeeLKKA 434


                 .
gi 223029420 634 K 634
Cdd:PRK03918 435 K 435
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 478-626 1.92e-05

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.80  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 478 EDDKGKIMEEVMRTYLKQQEKL-NLILQKKQQL-QMEVKMlsssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyvEQK 555
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420 556 DLEKKLEQimkqkctcdsnLEKDKEAEYAGQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 626
Cdd:cd16269  234 SYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 479-629 2.11e-05

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: 47.86  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   479 DDKGKIMEEVMRTYLKQQEKLNlilqkKQQLQMEVKMLSSSKSMKELTEEQQNLQKelesLQNEHAQRMEEFYVEQKDLE 558
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSK----LKNKHEAMISDLEERLKKEE 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420   559 K---KLEQImKQKCTCDSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:pfam01576  201 KgrqELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
mukB PRK04863
chromosome partition protein MukB;
527-638 2.32e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  527 EEQQNLQKELESLQNEHAqRMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLDHaeadrqeLQD 606
Cdd:PRK04863  506 REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKR-----LGKNLDDEDELEQLQEELEARLES-------LSE 572

                          90       100       110
                  ....*....|....*....|....*....|..
gi 223029420  607 ELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:PRK04863  573 SVSEARERRMALRQQLEQLQARIQRLAARAPA 604
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 494-638 2.60e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   494 KQQEKLNLILQKKQQ--LQMEVKMLSSSKSMKELTEEQQN-LQKELESLQNEHAQ--RMEEFYV-EQKDLEKKL----EQ 563
Cdd:TIGR02169  251 EELEKLTEEISELEKrlEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASleRSIAEKErELEDAEERLakleAE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   564 IMKQKCTCDS--------NLEKDK-EAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILK 631
Cdd:TIGR02169  331 IDKLLAEIEElereieeeRKRRDKlTEEYAElkeELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410


                   ....*..
gi 223029420   632 SSKTAKE 638
Cdd:TIGR02169  411 LQEELQR 417
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 522-624 2.90e-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: 44.11  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   522 MKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQrldhaeaDR 601
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR-------KQ 78

                           90       100
                   ....*....|....*....|....
gi 223029420   602 QELQDELRQER-EARQKLEMMIKE 624
Cdd:smart00935  79 QKLQQDLQKRQqEELQKILDKINK 102
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 487-632 3.03e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.14  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 487 EVMRTYLKQQEKLNlilqkkQQLQMEVKMLSSSK--SMKELtEEQQNLQKELESLQN---EHAQRME-------EFYVEQ 554
Cdd:PRK04778 313 DTLPDFLEHAKEQN------KELKEEIDRVKQSYtlNESEL-ESVRQLEKQLESLEKqydEITERIAeqeiaysELQEEL 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 555 KDLEKKLEQIMKQkctcdsnlekdkEAEYAGQLAELRQrldhaeadrqelqdelrQEREARQKLEMMIKEL---KLQILK 631
Cdd:PRK04778 386 EEILKQLEEIEKE------------QEKLSEMLQGLRK-----------------DELEAREKLERYRNKLheiKRYLEK 436


                 .
gi 223029420 632 S 632
Cdd:PRK04778 437 S 437
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
454-626 4.00e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.77  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 454 DINKVGIGLVAAASspllVKDVI---CEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKmlsssksmkelteeqq 530
Cdd:COG2433  364 DRDEVKARVIRGLS----IEEALeelIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------------- 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 531 NLQKELESLQNEHAQRMEEFyveqKDLEKKLEQIMKQKctcDSNLEKDKEAeyagqlaelrQRLDhAEADRqeLQDELRQ 610
Cdd:COG2433  424 RLEAEVEELEAELEEKDERI----ERLERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEE 483

                        170
                 ....*....|....*.
gi 223029420 611 EREARQKLEMMIKELK 626
Cdd:COG2433  484 ERERIEELKRKLERLK 499
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 482-614 4.08e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR 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: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 45.55  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 482 GKIMEEVMRTYLKQQEKL------NLI-LQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVE 553
Cdd:cd07647   17 GKKMCKELEDFLKQRAKAeedygkALLkLSKSAGPGDEIGTLKSSwDSLRKETENVANAHIQLAQSLREEAEKLEEFREK 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029420 554 QKDLEKKLEQIM----KQKCTCDSNL--------EKDKEAEYAGQLAElRQRLDHAEADRQELQDELRQEREA 614
Cdd:cd07647   97 QKEERKKTEDIMkrsqKNKKELYKKTmkakksyeQKCREKDKAEQAYE-KSSSGAQPKEAEKLKKKAAQCKTS 168
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
496-636 4.10e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 496 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQ----NEH--AQRMEEfyvEQKDLEKKLEQIMKQ-K 568
Cdd:COG3206  239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytPNHpdVIALRA---QIAALRAQLQQEAQRiL 315

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029420 569 CTCDSNLE--KDKEAEYAGQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQILKSSKTA 636
Cdd:COG3206  316 ASLEAELEalQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 478-638 4.99e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   478 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDL 557
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   558 EK----KLEQIMKQKCTCDSNLEK------DKEAEYAGQLAELRQRLDHAEADRQELQDELRQERE---ARQKLEMMIKE 624
Cdd:pfam02463  319 SEkekkKAEKELKKEKEEIEELEKelkeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlsSAAKLKEEELE 398

                          170
                   ....*....|....
gi 223029420   625 LKLQILKSSKTAKE 638
Cdd:pfam02463  399 LKSEEEKEAQLLLE 412
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 505-630 7.08e-05

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: 44.13  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  505 KKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNE------HAQRMEEFYVEQKDLEKKLeqimkqkctcdSNLEKD 578
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQlenyekDKQSLKNLKARLKVLEKEL-----------KDLKWE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029420  579 KEaeyagqlaELRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQIL 630
Cdd:pfam13851 108 HE--------VLEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQAL 154
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 487-619 7.14e-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: 46.10  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  487 EVMRTYLKQQeklnLILQKKQQLQMEvkmlsssksmkeLTEEQQNL--QKELESLQNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:COG3096   499 ELLRRYRSQQ----ALAQRLQQLRAQ------------LAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAEL 562

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029420  565 MKQKCTCDSNLEKDKEaeyagQLAELRQRLDHAEADRQELQDELRQEREARQKLE 619
Cdd:COG3096   563 EAQLEELEEQAAEAVE-----QRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
PRK12704 PRK12704
phosphodiesterase; Provisional
 484-629 8.01e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 484 IMEEVMRTYLKQ-QEKLNLILQKKQqlqMEVKMLSSSKsMKELTEEQQNLQKELEslqNEHAQRMEEFyveqKDLEKKL- 561
Cdd:PRK12704  24 VRKKIAEAKIKEaEEEAKRILEEAK---KEAEAIKKEA-LLEAKEEIHKLRNEFE---KELRERRNEL----QKLEKRLl 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 562 --EQIMKQKctcDSNLEKdKEAEYAGQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELK 626
Cdd:PRK12704  93 qkEENLDRK---LELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEAR 168


                 ...
gi 223029420 627 LQI 629
Cdd:PRK12704 169 HEA 171
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 499-628 9.24e-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: 9.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  499 LNLILQKKQQLQMEVKmlssSKSMKELTEeqqNLQK-ELESLQNEHAQRMEEfyVEQKDLEkkLEQiMKQKCTCDS---N 574
Cdd:pfam13870  13 LELITLKHTLAKIQEK----LEQKEELGE---GLTMiDFLQLQIENQALNEK--IEERNKE--LKR-LKLKVTNTVhalT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 223029420  575 LEKDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 628
Cdd:pfam13870  81 HLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ 134
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 485-638 9.36e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 485 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQ- 563
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALE--RRIAALARRIRALEQELAALE----AELAELEKEIAELRAELEAq 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 564 ----------------------IMKQkctcDSNLEKDKEAEYAGQLAE-LRQRLDHAEADRQELQDELRQEREARQKLEM 620
Cdd:COG4942  103 keelaellralyrlgrqpplalLLSP----EDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|
gi 223029420 621 MIKELK--LQILKSSKTAKE 638
Cdd:COG4942  179 LLAELEeeRAALEALKAERQ 198
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 483-638 9.66e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 9.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   483 KIMEEVMRTYLKQQEKLNLIlqKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLE 562
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGEL--EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   563 QIMKQKCTCDSNL----EKDKE-AEYAGQLAELRQRLDHAEADRQE-------LQDELRQEREARQKLEMMIKELKLQIL 630
Cdd:TIGR02169  358 EYAELKEELEDLRaeleEVDKEfAETRDELKDYREKLEKLKREINElkreldrLQEELQRLSEELADLNAAIAGIEAKIN 437


                   ....*...
gi 223029420   631 KSSKTAKE 638
Cdd:TIGR02169  438 ELEEEKED 445
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
472-626 1.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 472 VKDVICEddKGKIMEEVMRtylkqqeKLNLILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHA------ 544
Cdd:PRK03918 191 IEELIKE--KEKELEEVLR-------EINEISSELPELREELEKLEKEvKELEELKEEIEELEKELESLEGSKRkleeki 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 545 ----QRMEEFYVEQKDLEKKLEQI--MKQKCTCDSNLEKDKEaEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKL 618
Cdd:PRK03918 262 releERIEELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340


                 ....*...
gi 223029420 619 EMMIKELK 626
Cdd:PRK03918 341 EELKKKLK 348
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
478-638 1.34e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 478 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSmkelteEQQNLQKELESLQNEHAQRMEEFYVEQKDL 557
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK------ELEREEKELKKLEEELDKAFEELAETEKRL 642

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 558 EKKLEQI--MKQKCTCD-----SNLEKDKEAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMM------ 621
Cdd:PRK03918 643 EELRKELeeLEKKYSEEeyeelREEYLELSRELAGlraELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekaler 722

                        170
                 ....*....|....*..
gi 223029420 622 IKELKLQILKSSKTAKE 638
Cdd:PRK03918 723 VEELREKVKKYKALLKE 739
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 486-626 1.60e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.56  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 486 EEVMRTYLKQQEKLNLILQKKQQLQ-------MEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFY--VEQKD 556
Cdd:COG5185  295 KEKIAEYTKSIDIKKATESLEEQLAaaeaeqeLEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVgeVELSK 374

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029420 557 LEKKLEQIMKQ-KCTCDSNLEKDKEAEYAGQ--LAELRQRLDHAEADRQELQDELRQereARQKLEMMIKELK 626
Cdd:COG5185  375 SSEELDSFKDTiESTKESLDEIPQNQRGYAQeiLATLEDTLKAADRQIEELQRQIEQ---ATSSNEEVSKLLN 444
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 520-624 2.16e-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: 42.52  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 520 KSMKELTEEQQNLQKELESLQNEhAQRMeefyveQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQRldhaea 599
Cdd:COG2825   36 QESPEGKAAQKKLEKEFKKRQAE-LQKL------EKELQALQEKLQKEAATLSEEERQKKERELQKKQQELQRK------ 102

                         90       100
                 ....*....|....*....|....*.
gi 223029420 600 dRQELQDELRQER-EARQKLEMMIKE 624
Cdd:COG2825  103 -QQEAQQDLQKRQqELLQPILEKIQK 127
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 507-638 2.32e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 507 QQLQMEVKMLSssKSMKE----LTEEQQNLQKELESLQNEHAQ-RMEEFYVEQKDLEKKLEQIMKQkctCDSNLEkdkea 581
Cdd:PRK04778 201 DQLEEELAALE--QIMEEipelLKELQTELPDQLQELKAGYRElVEEGYHLDHLDIEKEIQDLKEQ---IDENLA----- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420 582 eyagQLAELrqRLDHAEADRQELQDE-------LRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:PRK04778 271 ----LLEEL--DLDEAEEKNEEIQERidqlydiLEREVKARKYVEKNSDTLPDFLEHAKEQNKE 328
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 516-638 2.40e-04

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: 43.98  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 516 LSSSKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLD 595
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERR-----IAALARRIRALEQELAALEAELA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 223029420 596 HAEADRQELQDELRQERE--ARQ--KLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4942   87 ELEKEIAELRAELEAQKEelAELlrALYRLGRQPPLALLLSPEDFLD 133
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 478-626 2.46e-04

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


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 42.73  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  478 EDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKE--LTEEQQNLQKELES---LQNEHAQRMEEFYV 552
Cdd:pfam15665  24 EEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  553 E----QKDLEKKLEQIMKQKctcdSNLEKDKE-------AEYAGQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQ 616
Cdd:pfam15665 104 EveeaKRAFEEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRK 179

                         170
                  ....*....|
gi 223029420  617 KLEMMIKELK 626
Cdd:pfam15665 180 EVEDLRKEKK 189
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 486-638 2.71e-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: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   486 EEVMRTYLKQQEKLNLIL----QKKQQLQMEVKMLSSSksMKELTEEQQNLQKELESLQNEHAQ---RMEEFYVEQKDLE 558
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKEE--LKALREALDELRAELTLLNEEAANlreRLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   559 KKLEQIMKQKctcdsnlekdkeAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:TIGR02168  838 RRLEDLEEQI------------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
458-626 2.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 458 VGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLI----LQKKQQLQMEVKMLSSSKSMKELTEEQQNLQ 533
Cdd:COG4717  281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalgLPPDLSPEELLELLDRIEELQELLREAEELE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 534 KELESLQNEHAQR----------MEEFYV------EQKDLEKKLEQIMKQkctCDSNLEKDKEAEYAGQLAELRQRLDHA 597
Cdd:COG4717  361 EELQLEELEQEIAallaeagvedEEELRAaleqaeEYQELKEELEELEEQ---LEELLGELEELLEALDEEELEEELEEL 437

                        170       180
                 ....*....|....*....|....*....
gi 223029420 598 EADRQELQDELRQEREARQKLEMMIKELK 626
Cdd:COG4717  438 EEELEELEEELEELREELAELEAELEQLE 466
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 485-629 3.22e-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: 42.60  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 485 MEEVMRTYLKQQEKLNLILQKKQQLqmevkmlsssksmKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQI 564
Cdd:COG1579    2 MPEDLRALLDLQELDSELDRLEHRL-------------KELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRL 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223029420 565 MKQKCTCDSNLEKDKEA--------EYAGQLAElrqrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:COG1579   65 ELEIEEVEARIKKYEEQlgnvrnnkEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 480-620 3.28e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.79  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  480 DKGKIMEEVMRtyLKQQEKLNLILQKKQQLQMEvkmlsssKSMKELTEEQQNLQKELEslQNEHAQRMEEFYVEQKDLEK 559
Cdd:pfam15709 369 ERAEKMREELE--LEQQRRFEEIRLRKQRLEEE-------RQRQEEEERKQRLQLQAA--QERARQQQEEFRRKLQELQR 437

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029420  560 KLEQIMKQKctcdSNLEKDKEAEYAGQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 620
Cdd:pfam15709 438 KKQQEEAER----AEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 514-621 3.54e-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: 42.66  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  514 KMLSSSKSMK---ELTEEQ-QNLQKELESLQNEHAQRMEEFYVEQKDLE----KKLEQIMKQkctcdsnlEKDKEAEYAG 585
Cdd:pfam12037  36 RELESSPHAKkalELMKKQeQTRQAELQAKIKEYEAAQEQLKIERQRVEyeerRKTLQEETK--------QKQQRAQYQD 107

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 223029420  586 QLAelRQRL-DHAEADRQELQDELRQEREARQKLEMM 621
Cdd:pfam12037 108 ELA--RKRYqDQLEAQRRRNEELLRKQEESVAKQEAM 142
DUF4175 pfam13779
Domain of unknown function (DUF4175);
522-624 3.74e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 43.82  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  522 MKELTEEQQNLQKELESLQNEHAQRMeefyvEQKDLEKKLEQImkqkctcdsnlekdKEAEYAGQLAELRQRLDHAE--- 598
Cdd:pfam13779 526 MQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRMLDRI--------------EELARSGRRAEAQQMLSQLQqml 586

                          90       100       110
                  ....*....|....*....|....*....|..
gi 223029420  599 -----ADRQELQDELRQE-REARQKLEMMIKE 624
Cdd:pfam13779 587 enlqaGQPQQQQQQGQSEmQQAMDELGDLLRE 618
mukB PRK04863
chromosome partition protein MukB;
487-633 3.81e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  487 EVMRTYLKQQEKLNLILQKKQQLQMEVKMLsssksmKELTEEQQNLQK-----------------ELESLQNEHAQRMEE 549
Cdd:PRK04863  496 DVARELLRRLREQRHLAEQLQQLRMRLSEL------EQRLRQQQRAERllaefckrlgknlddedELEQLQEELEARLES 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  550 FYVEQKDLEKK---LEQIMKQKCTCDSNLEKDKEAEYAGQ--LAELRQRLDHAEADRQEL----QDELRQEREARQ---K 617
Cdd:PRK04863  570 LSESVSEARERrmaLRQQLEQLQARIQRLAARAPAWLAAQdaLARLREQSGEEFEDSQDVteymQQLLERERELTVerdE 649

                         170
                  ....*....|....*.
gi 223029420  618 LEMMIKELKLQILKSS 633
Cdd:PRK04863  650 LAARKQALDEEIERLS 665
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
530-628 4.00e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 530 QNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQimkqkctcdsnlEKDKEAEYA---GQLAELRQRLDHAEADRQELQD 606
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKE------------AEEKEEEYAelqEELEELEEELEELEAELEELRE 116

                         90       100
                 ....*....|....*....|..
gi 223029420 607 ELRQEREARQKLEMMIKELKLQ 628
Cdd:COG4717  117 ELEKLEKLLQLLPLYQELEALE 138
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 480-629 4.79e-04

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. 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. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 41.56  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 480 DKGKIMEEVMRTYLKQQEKL---------NLILQKKQQLQMEVKMLSSS-KSMKELTEE--------QQNLQKELESLQN 541
Cdd:cd07610   10 ELGLDLLKDLREFLKKRAAIeeeyaknlqKLAKKFSKKPESGKTSLGTSwNSLREETESaatvheelSEKLSQLIREPLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 542 EHAQRMEEfyvEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAEL-RQRLDHAEADRQELQDELRQEREARQKLEM 620
Cdd:cd07610   90 KVKEDKEQ---ARKKELAEGEKLKKKLQELWAKLAKKADEEYREQVEKLnPAQSEYEEEKLNKIQAEQEREEERLEILKD 166


                 ....*....
gi 223029420 621 MIKELKLQI 629
Cdd:cd07610  167 NLKNYINAI 175
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 424-605 4.89e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 43.21  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  424 ELTKTEANASIS---NNSTSKRKSESATCNLVRDINKVGIGLVAaassplLVKDVicEDDKGKIMEEVMRTYLKQQEKLN 500
Cdd:pfam09731 262 ELVSIFPDIIPVlkeDNLLSNDDLNSLIAHAHREIDQLSKKLAE------LKKRE--EKHIERALEKQKEELDKLAEELS 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  501 LILQKKQQLQMEVKMLSSSKSMKELTEE-QQNLQKELESLQNEHAQRMEEFYVEQK-DLEKKLEQIMKQKCTCDSNLEKD 578
Cdd:pfam09731 334 ARLEEVRAADEAQLRLEFEREREEIRESyEEKLRTELERQAEAHEEHLKDVLVEQEiELQREFLQDIKEKVEEERAGRLL 413

                         170       180
                  ....*....|....*....|....*...
gi 223029420  579 KEAEYAGQLAEL-RQRLDHAEADRQELQ 605
Cdd:pfam09731 414 KLNELLANLKGLeKATSSHSEVEDENRK 441
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 528-638 5.49e-04

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: 40.24  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  528 EQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKqkctcdsnlekdkeaeyagQLAELRQRLDHAEADRQELQDE 607
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKE-------------------DLIKFDKFLKENDAKRRRALKK 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 223029420  608 LRQEREARQKLEMMIKELKLQI--LKSSKTAKE 638
Cdd:pfam13863  68 AEEETKLKKEKEKEIKKLTAQIeeLKSEISKLE 100
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 493-629 5.91e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  493 LKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDL----EKKLEQIMKQK 568
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420  569 CTcdSNLEKDKEAEYAGQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 494-638 6.91e-04

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: 42.44  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQK--KQQLQMEVKMLSSSKSMKELTEEQQNLQkeleSLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctc 571
Cdd:COG4942  101 AQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEELRADLAELAALRAELEAER--- 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420 572 dsnleKDKEAEYAgQLAELRQRLDHAEADRQELQDELRQEREARQK----LEMMIKELKLQILKSSKTAKE 638
Cdd:COG4942  174 -----AELEALLA-ELEEERAALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAAA 238
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
518-638 6.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 518 SSKSMKELTEEQQNLQKELESLQNEHAQRMEEFyveqKDLEKKLEQIMKQkctcdsnLEKDKEaeyagQLAELRQRLDHA 597
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREEL----EQLEEELEQARSE-------LEQLEE-----ELEELNEQLQAA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 223029420 598 EADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4372   93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 151-229 7.52e-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: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 151 GESISCFQVGGEKRLCLPQVLNSVLREFT--LQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 228
Cdd:cd21081   10 GAKVAAFTVDGEELICLPQAFELFLKHLVggLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                 .
gi 223029420 229 L 229
Cdd:cd21081   90 L 90
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 510-638 7.64e-04

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: 42.79  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  510 QMEVKMLSSSKSMKELTEEQQNLQKELESLQnehaQRMEEFYVEQKDLEKKLEQIMKQKCtcdsNLEKDKEAeyagQLAE 589
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIK----MSLQRSMSTQKALEEDLQIATKTIC----QLTEEKEA----QMEE 339

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 223029420  590 L-RQRLDHA------EADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:pfam05483 340 LnKAKAAHSfvvtefEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
486-634 8.05e-04

Microtubule associated protein (MAP65/ASE1 family);


Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 42.30  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  486 EEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKEL--TEEQQNLQKELESLQNEHAQRMEEFyveqKDLEKKLEQ 563
Cdd:pfam03999 100 EHLRKEKAPRLAEIKELLEQLQQLCEELGEEPLPLLIDPLpsLEELESFRKHLENLRNEKERRLEEV----NELKKQIKL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  564 IMKQ--------------------KCTCDSNLEKDKEA--EYAGQLAELRQRLDHAEADRQELQDELR-----QEREARQ 616
Cdd:pfam03999 176 LMEEldlvpgtdfeedllcesednFCLSRENIDKLRKLikQLEEQKAEREEKIDDLREKILELWNRLQvpqeeQESFVRE 255

                         170       180
                  ....*....|....*....|....*.
gi 223029420  617 ----KLEMMI---KEL-KLQILKSSK 634
Cdd:pfam03999 256 nnslSQDTIDalrEELqRLEELKKKN 281
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 478-604 8.78e-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: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  478 EDDKGKIMEEV------MRTYLKQQEKLNLILQKKQQLQMEVKMlssskSMKELTEEQQNLQKELESLQNEHA---QRME 548
Cdd:pfam13851  42 EERNEKLMSEIqqenkrLTEPLQKAQEEVEELRKQLENYEKDKQ-----SLKNLKARLKVLEKELKDLKWEHEvleQRFE 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  549 EFYVEQKDLEKKLEQIM---KQKCTCDSN-LEKdkeaeyagQLAELRQRLDHAEADRQEL 604
Cdd:pfam13851 117 KVERERDELYDKFEAAIqdvQQKTGLKNLlLEK--------KLQALGETLEKKEAQLNEV 168
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 497-638 9.73e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 9.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   497 EKLNLILQKK-QQLQMEVKMLSSSKS-----MKELTEEQQNLQ---KELESLQNEHAQRMEEFYVEQK-------DLEKK 560
Cdd:pfam01576  376 EKAKQALESEnAELQAELRTLQQAKQdsehkRKKLEGQLQELQarlSESERQRAELAEKLSKLQSELEsvssllnEAEGK 455

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   561 LEQIMKQKCTCDSNLEKDKE--AEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:pfam01576  456 NIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 517-610 1.13e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 517 SSSKSMKELTEEQQNLQKELESLQNEhAQRMEEfyvEQKDLEKKLEQIMKqkctcdsnlekdkeaeyagQLAELRQRLDH 596
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELEALQA-------------------EIDKLQAEIAE 76

                         90
                 ....*....|....
gi 223029420 597 AEADRQELQDELRQ 610
Cdd:COG3883   77 AEAEIEERREELGE 90
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
518-632 1.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  518 SSKSMKELTE-------EQQNLQKELESLQnEHAQRMEEFYVEQKDLEKK---LEQIMKQKCTCDSNLEKDKEAEYAG-- 585
Cdd:COG4913   202 SFKPIGDLDDfvreymlEEPDTFEAADALV-EHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRaa 280

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223029420  586 --------QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKS 632
Cdd:COG4913   281 lrlwfaqrRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
494-638 1.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQKKQ--QLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveqkdlEKKLEQIMKQKctc 571
Cdd:COG4372   80 EELEELNEQLQAAQaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER--- 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420 572 dsnlekdkeaeyAGQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4372  149 ------------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKEEELAEA 205
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 520-624 1.44e-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: 39.48  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  520 KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKctcdsnleKDKEAEYAGQLAELRQRldhaea 599
Cdd:pfam03938  12 EESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER--------EEKEQELQKKEQELQQL------ 77

                          90       100
                  ....*....|....*....|....*.
gi 223029420  600 dRQELQDELRQER-EARQKLEMMIKE 624
Cdd:pfam03938  78 -QQKAQQELQKKQqELLQPIQDKINK 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 451-625 1.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 451 LVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQ 530
Cdd:COG1196  623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 531 NLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAG---QLAELRQRLDHAEADRQEL--- 604
Cdd:COG1196  703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIEALgpv 782

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 223029420 605 --------------QDELRQER----EARQKLEMMIKEL 625
Cdd:COG1196  783 nllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
487-638 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 223029420 487 EVMRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELtEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMK 566
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420 567 QKCTC-------DSNLEKDKEAEYAGQLAELRQRLdhaeadrQELQDELRQEREARQKLEMMIKELKlQILKSSKTAKE 638
Cdd:PRK03918 434 AKGKCpvcgrelTEEHRKELLEEYTAELKRIEKEL-------KEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQ 504
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 493-624 1.60e-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: 41.18  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  493 LKQQEKLNLILQKKQ----QLQMEVKMLSSSKSMKELT----------EEQQNLQKELES----LQNEHAQRMEEFYVEQ 554
Cdd:pfam15558 145 LQLQERLEEACHKRQlkerEEQKKVQENNLSELLNHQArkvlvdcqakAEELLRRLSLEQslqrSQENYEQLVEERHREL 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420  555 KDLEKKLE-QIMKQKCTCDSNLEKDKE-AEYAGQLAE--LRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 624
Cdd:pfam15558 225 REKAQKEEeQFQRAKWRAEEKEEERQEhKEALAELADrkIQQARQVAHKTVQDKAQRARELNLEREKNHHILKL 298
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 479-638 1.66e-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: 41.54  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  479 DDKGKIMEEVMRTYLKQQEKLNLIL-QKKQQLQMEVKMLSSSKS-MKELTEEQQNLQKELESLQNehaqRMEEFYVEQKD 556
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLeQKQKELKSKEKELKKLNEeKKELEEKVKDLTKKISSLKE----KIEKLESEKKE 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  557 LEKKLEQIMKQKCTCDSNLEKDKeaeYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTA 636
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKEN---LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612


                  ..
gi 223029420  637 KE 638
Cdd:TIGR04523 613 SS 614
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
493-624 2.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 493 LKQQEKLNLILQKKQQLQMEVKM---------LSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQkdLEKKLEQ 563
Cdd:COG4717  359 LEEELQLEELEQEIAALLAEAGVedeeelraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEE 436

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420 564 IMKQKctcdSNLEKDKEAEYAgQLAELRQRLDHAEADRqELQDELRQEREARQKLEMMIKE 624
Cdd:COG4717  437 LEEEL----EELEEELEELRE-ELAELEAELEQLEEDG-ELAELLQELEELKAELRELAEE 491
PTZ00121 PTZ00121
MAEBL; Provisional
 478-624 2.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  478 EDDKGKIMEEVMRT-YLKQQEKLNLIlqKKQQLQMevKMLSSSKSMKELTEEQQNLQKELESL--QNEHAQRMEEFYVEQ 554
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAeELKKAEEENKI--KAAEEAK--KAEEDKKKAEEAKKAEEDEKKAAEALkkEAEEAKKAEELKKKE 1711

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029420  555 KDLEKKLEQIMKQKCTCDSNLE--KDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 624
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
496-625 2.27e-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: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 496 QEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELEslqnehaqrmeefyveqkDLEKKLEQIMKQKCTCDSNL 575
Cdd:COG3206  151 AAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELE------------------EAEAALEEFRQKNGLVDLSE 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 223029420 576 EKDKEAEyagQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 625
Cdd:COG3206  213 EAKLLLQ---QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
494-638 2.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 494 KQQEKLNLILQKKQQLQMEVKMLSssKSMKELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDS 573
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEE----LKELEEQLESLQEELAALEQ 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223029420 574 NLEKDKEAEYAGQLAELRQrldhaEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4372  172 ELQALSEAEAEQALDELLK-----EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
523-626 2.87e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 523 KELTEEQQNLQKELESLQN------EHAQRMEEFYVEQKDLEKKLEQIMKQKctcdSNLEKDKEA--EYAGQLAELRQRL 594
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENieelikEKEKELEEVLREINEISSELPELREEL----EKLEKEVKEleELKEEIEELEKEL 247

                         90       100       110
                 ....*....|....*....|....*....|..
gi 223029420 595 DHAEADRQELQDELRQEREARQKLEMMIKELK 626
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 479-620 3.14e-03

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: 40.49  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  479 DDKGKIMEEVMRTYLKQQEKLNLILQKKQQLQMEvkmlssSKSMKELTEEQQNLqKELESLQNEHAQRMEEFYVE----- 553
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQEERKRELE------RIRQEEIAMEISRM-RELERLQMERQQKNERVRQEleaar 402

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223029420  554 -QKDLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAELRQ-------RLDHAEADRQELQDELRQERE--ARQKLEM 620
Cdd:pfam17380 403 kVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEeraremeRVRLEEQERQQQVERLRQQEEerKRKKLEL 479
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 487-632 3.14e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.80  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  487 EVMRT-YLKQQE--------KLNLI-LQKKQQLQmevkmlssskSMKELTEEQQNLQKELESLqnehAQRMEEFYVEQKD 556
Cdd:pfam10168 542 QVFREeYLKKHDlareeiqkRVKLLkLQKEQQLQ----------ELQSLEEERKSLSERAEKL----AEKYEEIKDKQEK 607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  557 LEKKLEQIMKQKCTCDSNL---EKD--KEAE-YAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIL 630
Cdd:pfam10168 608 LMRRCKKVLQRLNSQLPVLsdaEREmkKELEtINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTI 687


                  ..
gi 223029420  631 KS 632
Cdd:pfam10168 688 KE 689
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 480-634 3.21e-03

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: 40.82  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   480 DKGKIMEEVMRTYLK--QQEKLNLI----LQKKQQlQMEVKMLSSSK-----SMKELTEEQQNLQKELESLQ---NEHAQ 545
Cdd:TIGR02169  187 ERLDLIIDEKRQQLErlRREREKAEryqaLLKEKR-EYEGYELLKEKealerQKEAIERQLASLEEELEKLTeeiSELEK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   546 RMEEfyveqkdLEKKLEQIMKQkctcdsnLEKDKEAEYAG---QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMI 622
Cdd:TIGR02169  266 RLEE-------IEQLLEELNKK-------IKDLGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331

                          170
                   ....*....|..
gi 223029420   623 KELKLQILKSSK 634
Cdd:TIGR02169  332 DKLLAEIEELER 343
mukB PRK04863
chromosome partition protein MukB;
590-638 3.26e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 223029420  590 LRQRLDHAEADRQELQDELRQ-EREARQKLEMMIKelklqiLKSSKTAKE 638
Cdd:PRK04863  990 LRQRLEQAEQERTRAREQLRQaQAQLAQYNQVLAS------LKSSYDAKR 1033
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 528-626 3.49e-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: 40.71  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  528 EQQNLQKELESLQNEHAQrMEEFYVEQKDLEKKLEQIMKQkctcdSNLEKDKEAEYAGQLAELRQRLDHAEADRQELQDE 607
Cdd:COG3096   506 SQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQR-----IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579

                          90
                  ....*....|....*....
gi 223029420  608 LRQEREARQKLEMMIKELK 626
Cdd:COG3096   580 RSELRQQLEQLRARIKELA 598
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
494-638 3.69e-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: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  494 KQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHA------QRMEEFYVEQKDLEKKLEQIMKQ 567
Cdd:COG4913   635 ALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDdlaaleEQLEELEAELEELEEELDELKGE 714

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223029420  568 KCTCDSNLEKDKEaeyagQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG4913   715 IGRLEKELEQAEE-----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 523-637 3.80e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.28  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  523 KELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEaEYAGQLAELRQRLDHAEADRQ 602
Cdd:pfam04012  25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNE-ELAREALAEKKSLEKQAEALE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 223029420  603 ELQDELR----QEREARQKLEMMIKEL--KLQILKS-SKTAK 637
Cdd:pfam04012 104 TQLAQQRsaveQLRKQLAALETKIQQLkaKKNLLKArLKAAK 145
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 483-624 3.99e-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: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 483 KIMEEVMRTYLKQQEKLN---LILQKKQQLQMEVKMLSSS-KSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLE 558
Cdd:cd07671   22 KDVEELLKQRAQAEERYGkelVQIARKAGGQTEINTLKASfDQLKQQIENIGNSHIQLAGMLREELKSLEEFRERQKEQR 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029420 559 KKLEQIMKQ---------KCTCDSNL---EKDKEAEYAGQLAELRQRLDHAEaDRQELQDELRQEREARQKLEMMIKE 624
Cdd:cd07671  102 KKYEAVMERvqkskvslyKKTMESKKtyeQRCREADEAEQTFERSSSTGNPK-QSEKSQNKAKQCRDAATEAERVYKQ 178
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 504-628 4.43e-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: 40.34  E-value: 4.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   504 QKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQ---RMEEFYVEQKDL---------EKKLEQIMKQKCTC 571
Cdd:TIGR00618  370 ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATidtRTSAFRDLQGQLahakkqqelQQRYAELCAAAITC 449

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 223029420   572 DSNLEKDKEAEyagqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 628
Cdd:TIGR00618  450 TAQCEKLEKIH----LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 478-634 4.48e-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: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   478 EDDKGKIME------EVMRTYLKQQEKLNlilqkkQQLQ-MEVKMLSSSKSMKELTEEQQNLQKELESLqnehAQRMEEF 550
Cdd:pfam01576  495 EDERNSLQEqleeeeEAKRNVERQLSTLQ------AQLSdMKKKLEEDAGTLEALEEGKKRLQRELEAL----TQQLEEK 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   551 YVEQKDLEK---KLEQ--------IMKQKCTCdSNLEKdKEAEYAGQLAELR-------QRLDHAEADRQE-------LQ 605
Cdd:pfam01576  565 AAAYDKLEKtknRLQQelddllvdLDHQRQLV-SNLEK-KQKKFDQMLAEEKaisaryaEERDRAEAEAREketralsLA 642

                          170       180       190
                   ....*....|....*....|....*....|.
gi 223029420   606 DELRQEREARQKLEMMIKELKLQI--LKSSK 634
Cdd:pfam01576  643 RALEEALEAKEELERTNKQLRAEMedLVSSK 673
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 489-629 4.59e-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: 40.32  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  489 MRTYLKQQEKLNLILQKKQQLQMEVKMLSSSKS-----MKELtEEQQNLQKELES-LQ--NEHAQRMEEFYVEQKDLEKk 560
Cdd:COG3096   274 MRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQEKIER- 351

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223029420  561 leqimkqkctcdsnlekdkeaeYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:COG3096   352 ----------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 498-629 4.76e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 38.17  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420   498 KLNLILQKKQQLQMEVKMLSSSKSM-KELTEEQQNLqkeLESLQNEhaqrmeEFYVEQKDLEKKLEQIMKQkctcdsnLE 576
Cdd:smart01071  33 KQRDIHQARVERMEEIKNLKYELIMnDHLNKRIDKL---LKGLREE------ELSPETPTYNEMLAELQDQ-------LK 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 223029420   577 KDKEAEYAGQLAELrqrlDHAEADRQELQDElrqEREARQKLEMMIKELKLQI 629
Cdd:smart01071  97 KELEEANGDSEGLL----EELKKHRDKLKKE---QKELRKKLDELEKEEKKKI 142
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
 480-628 4.77e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 38.98  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  480 DKGKIME---EVMRTYLKQQEKLN-LILQKKQQLQMEVKMLSSSKSMKELTEEQ----QNLQKELESLQNEHAQRMEE-- 549
Cdd:pfam14988  30 ECEEIERrrqELASRYTQQTAELQtQLLQKEKEQASLKKELQALRPFAKLKESQereiQDLEEEKEKVRAETAEKDREah 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  550 --FYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEAEyAGQLAELRQRLDHAE---ADRQELQDELRQE-------REARQK 617
Cdd:pfam14988 110 lqFLKEKALLEKQLQELRILELGERATRELKRKAQ-ALKLAAKQALSEFCRsikRENRQLQKELLQLiqetqalEAIKSK 188

                         170
                  ....*....|.
gi 223029420  618 LEMMIKELKLQ 628
Cdd:pfam14988 189 LENRKQRLKEE 199
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
523-619 4.95e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 523 KELTEEQQNLQKELESLQNEHAQRMEEfyveQKDLEKKLEQIMKQKCTCDSNLEK--DKEAEYAGQLAELRQRLDHAEAD 600
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREE----IEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELREREAELEAT 434

                         90
                 ....*....|....*....
gi 223029420 601 RQELQDELrqeREARQKLE 619
Cdd:PRK02224 435 LRTARERV---EEAEALLE 450
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 480-619 4.97e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 4.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 480 DKGKIMEEvmrtYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEK 559
Cdd:PRK09510  56 DPGAVVEQ----YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223029420 560 KLEQIMKQKCTCDSNLEKDKE----AEYAGQLAELRQRLDHAEADRQelqdelrQEREARQKLE 619
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEakraAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
DUF4472 pfam14739
Domain of unknown function (DUF4472); This family is specific to the Chordates. Some members ...
 528-626 5.12e-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: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  528 EQQNLQ--KELESLQNEHAQRMEEFYVEQKDLEKKLeqimkqkctcdSNLEkdkeaeyaGQLAELRQRLDHAEADRQELQ 605
Cdd:pfam14739   2 EEEKLQisKALVDLQIENNKLREQYEAEKFELKNKL-----------LNLE--------NRVLELELRLEKAAEEIQDLR 62

                          90       100
                  ....*....|....*....|.
gi 223029420  606 DELRQEREARQKLEMMIKELK 626
Cdd:pfam14739  63 ERLRELEDDRRELAEEFVALK 83
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 436-629 5.25e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.94  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 436 NNSTSKRKSESATCNLVRDINKVGIGLVAAASSpllvKDVICEDDKgKIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKM 515
Cdd:COG5185  173 NQNLKKLEIFGLTLGLLKGISELKKAEPSGTVN----SIKESETGN-LGSESTLLEKAKEIINIEEALKGFQDPESELED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 516 LSS-SKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQK----DLEKKLEQIMKQKCTCDSNLEKDKEAEYAGQLAEL 590
Cdd:COG5185  248 LAQtSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIkqfeNTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 223029420 591 RQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 629
Cdd:COG5185  328 EESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
PRK11281 PRK11281
mechanosensitive channel MscK;
516-608 5.35e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  516 LSSSKSMKELTEE----QQNLQKELESLQNehAQRMEEfyvEQKDLEKKLEQIMKQKCTCDSNLE--KDKEAEYAGQ--- 586
Cdd:PRK11281   45 LDALNKQKLLEAEdklvQQDLEQTLALLDK--IDRQKE---ETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETREtls 119

                          90       100
                  ....*....|....*....|....*
gi 223029420  587 ---LAELRQRLDHAEADRQELQDEL 608
Cdd:PRK11281  120 tlsLRQLESRLAQTLDQLQNAQNDL 144
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 490-637 5.93e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  490 RTYLKQQEKLNLILQKKQQLQMEVKMLSSSKSMKElTEEQQNLQKEleslQNEHAQRMEEfyveqkdlEKKLEQimkQKC 569
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAEMRRLEVERKRRE-QEEQRRLQQE----QLERAEKMRE--------ELELEQ---QRR 385

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223029420  570 TCDSNLEKDkeaeyagQLAELRQRLDHAEAdRQELQDELRQEREARQKLEMMIKELKLQILKSSKTAK 637
Cdd:pfam15709 386 FEEIRLRKQ-------RLEEERQRQEEEER-KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAE 445
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 485-620 6.87e-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: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  485 MEEVMRTYLKQQEKL----NLILQKKQQLQMEVKMLsssksMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKK 560
Cdd:pfam13868  82 IEEREQKRQEEYEEKlqerEQMDEIVERIQEEDQAE-----AEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223029420  561 LEQIMKQKctcdsnlekdkeaeyAGQLAELRQRLDHAEADRQELQDELR--QEREARQKLEM 620
Cdd:pfam13868 157 ILEYLKEK---------------AEREEEREAEREEIEEEKEREIARLRaqQEKAQDEKAER 203
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
533-625 6.96e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 533 QKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKE-----AEYAGQLAELRQRLDHAEADRQELQDE 607
Cdd:PRK02224 201 EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEErreelETLEAEIEDLRETIAETEREREELAEE 280

                         90
                 ....*....|....*...
gi 223029420 608 LRQEREARQKLEMMIKEL 625
Cdd:PRK02224 281 VRDLRERLEELEEERDDL 298
46 PHA02562
endonuclease subunit; Provisional
 509-608 7.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 509 LQMEVKMLSSSK-SMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDSNLEKDKEaEYAGQL 587
Cdd:PHA02562 179 LNQQIQTLDMKIdHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-DPSAAL 257

                         90       100
                 ....*....|....*....|.
gi 223029420 588 AELRQRLDHAEADRQELQDEL 608
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVI 278
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 483-603 7.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 483 KIMEEVMRTYLKQQEKLNLILQKKQQLQMEVKmlSSSKSMKELTEEQQNLQKELESLQNEHAQRMEEFYVEQKDLEKKLE 562
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELE--AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 223029420 563 QIMKQkctcdsnlekdkeaeyAGQLAELRQRLDHAEADRQE 603
Cdd:COG4942  217 ELQQE----------------AEELEALIARLEAEAAAAAE 241
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 485-631 7.70e-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: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  485 MEEVMRTYLKQQEKLNLILQKKQQLQMEVKmlsssksmkeltEEQQNLQKELEslqNEHAQRMEEFYVEQKDLEKKLEQI 564
Cdd:pfam13868 219 ERQKEREEAEKKARQRQELQQAREEQIELK------------ERRLAEEAERE---EEEFERMLRKQAEDEEIEQEEAEK 283

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223029420  565 MKQKctcdsnlekdKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQILK 631
Cdd:pfam13868 284 RRMK----------RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 420-619 7.93e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.17  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 420 SQSKELTKTEANASISNnstSKRKSESATCNLVRDINKVGIGLVAAASSPLLVKDVICEDDKGKIMEEVMRTYLKQQEKL 499
Cdd:COG5185  313 SLEEQLAAAEAEQELEE---SKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEST 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 500 NL-ILQKKQQLQMEVKMLSS--SKSMKELTEEQQNLQKELESLQNEhaqrMEEFYVEQKDLEKKLEQIMKQKctcDSNLE 576
Cdd:COG5185  390 KEsLDEIPQNQRGYAQEILAtlEDTLKAADRQIEELQRQIEQATSS----NEEVSKLLNELISELNKVMREA---DEESQ 462

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 223029420 577 KDKEAEYAGQLAELRQRLDHAEADRQELQDELRQEREARQKLE 619
Cdd:COG5185  463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLR 505
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 505-637 9.00e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.24  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  505 KKQQLQMEVKMLSSSKSMKELTEE--QQNLQKELESLQ---NEHAQRMEEFYVEQKDLEKKLEQIMKQKCTCDS-NLEKD 578
Cdd:pfam05667 304 EKLQFTNEAPAATSSPPTKVETEEelQQQREEELEELQeqlEDLESSIQELEKEIKKLESSIKQVEEELEELKEqNEELE 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420  579 KEAEYAGQLAELrqrLDHAEADRQELQ-------------------------DELR--------QEREARQKLEmMIKEL 625
Cdd:pfam05667 384 KQYKVKKKTLDL---LPDAEENIAKLQalvdasaqrlvelagqwekhrvpliEEYRalkeaksnKEDESQRKLE-EIKEL 459

                         170
                  ....*....|..
gi 223029420  626 KLQILKSSKTAK 637
Cdd:pfam05667 460 REKIKEVAEEAK 471
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
497-638 9.96e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 9.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 497 EKLNLILQKKQQLQMEVKMLSSSKsmKELTEEQQNLQKELESLQNEHAQRMEEFYvEQKDLEKKLEQIMKQKCTCDSNLE 576
Cdd:COG1340   57 EEAQELREKRDELNEKVKELKEER--DELNEKLNELREELDELRKELAELNKAGG-SIDKLRKEIERLEWRQQTEVLSPE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223029420 577 KDKE------------------AEYAGQLAELRQRLDhaeadrqELQDELRQEREARQKLEMMIKELKLQILKSSKTAKE 638
Cdd:COG1340  134 EEKElvekikelekelekakkaLEKNEKLKELRAELK-------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE 206
 
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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