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Conserved domains on  [gi|1958754287|ref|XP_038959534|]
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ski-like protein isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 134-233 2.93e-66

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


:

Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.90  E-value: 2.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 134 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 1958754287 214 SCGLITLTDAQRLCNALLRP 233
Cdd:cd21084    81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 258-353 6.92e-57

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


:

Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.58  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 1958754287  338 EKKLKIILEEMKEKFS 353
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 518-668 1.02e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  518 DDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQnehaqrmeefyIEQRDLE 597
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE-----------ELIEELE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287  598 KKLEQVMKQKCTCDSNVEKDKEAEY--AAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 134-233 2.93e-66

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.90  E-value: 2.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 134 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 1958754287 214 SCGLITLTDAQRLCNALLRP 233
Cdd:cd21084    81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 258-353 6.92e-57

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


Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.58  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 1958754287  338 EKKLKIILEEMKEKFS 353
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 258-352 4.88e-55

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


Pssm-ID: 462602  Cd Length: 94  Bit Score: 182.47  E-value: 4.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 1958754287 338 EKKLKIILEEMKEKF 352
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 133-232 1.17e-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: 165.53  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 133 IPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 1958754287 213 PSCGLITLTDAQRLCNALLR 232
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 518-668 1.02e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  518 DDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQnehaqrmeefyIEQRDLE 597
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE-----------ELIEELE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287  598 KKLEQVMKQKCTCDSNVEKDKEAEY--AAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
533-667 1.88e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRmEEFYIEQRDLEK---KLEQVMKQKCT 609
Cdd:COG4717   106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAelaELQEELEELLE 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958754287 610 CDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 667
Cdd:COG4717   185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 535-664 8.17e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQL--QMEVEMlsssKAMKELTEEQQNLQKELESLQNEHAQRMEEF------YI-------EQRDLEKK 599
Cdd:PRK04778  281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287 600 LEQVMKQKCTCDSNVEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELRQ----EREARQKLEMMIKEL 664
Cdd:PRK04778  357 LESLEKQYDEITERIAEQEIAysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKL 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 484-668 1.46e-06

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: 51.71  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  484 KKKCESTICDLVRDTDKQgSGASSPLVVRDVTCEDDKGKIVEDVMrTYVRQQEKLSsilQKKQQLQMEVEMLSSSKAMKE 563
Cdd:pfam01576   98 KKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDIL-LLEDQNSKLS---KERKLLEERISEFTSNLAEEE 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  564 ltEEQQNLQKelesLQNEHAQRMEEFYIEQRDLEK-KLEQV-MKQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQ 641
Cdd:pfam01576  173 --EKAKSLSK----LKNKHEAMISDLEERLKKEEKgRQELEkAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246

                          170       180
                   ....*....|....*....|....*..
gi 1958754287  642 ELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:pfam01576  247 AALARLEEETAQKNNALKKIRELEAQI 273
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 517-665 1.39e-05

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.57  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 517 EDDKGKIVEDVMRTYVRQQEKLS-SILQKKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQNEHAQRMEEfyiEQR 594
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAeAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287 595 DLEKKLEQVMKQkctcdsnvekdKEAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 665
Cdd:cd16269   234 SYEEHLRQLKEK-----------MEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 553-663 1.43e-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: 45.27  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  553 EMLSSSKAMKELTEEQQNLQKELESLQNEhaqrmeefyieqrdLEKKLEQVMKQKCTCDSNVEKDKEAEYAAQLAELRQr 632
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958754287  633 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 663
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 134-233 2.93e-66

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 212.90  E-value: 2.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 134 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21084     1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                          90       100
                  ....*....|....*....|
gi 1958754287 214 SCGLITLTDAQRLCNALLRP 233
Cdd:cd21084    81 SCGLITLTDAQRLCNALLRP 100
c-SKI_SMAD_bind smart01046
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 258-353 6.92e-57

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


Pssm-ID: 198114  Cd Length: 95  Bit Score: 187.58  E-value: 6.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYlGTPE 337
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 1958754287  338 EKKLKIILEEMKEKFS 353
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 258-352 4.88e-55

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


Pssm-ID: 462602  Cd Length: 94  Bit Score: 182.47  E-value: 4.88e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 258 AFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQkYLGTPE 337
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 1958754287 338 EKKLKIILEEMKEKF 352
Cdd:pfam08782  80 REKLEQLLEDLKAKF 94
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 141-231 6.86e-53

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


Pssm-ID: 410782  Cd Length: 91  Bit Score: 176.60  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 141 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21079     1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                          90
                  ....*....|.
gi 1958754287 221 TDAQRLCNALL 231
Cdd:cd21079    81 TDAERLCSALL 91
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 134-231 7.96e-49

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


Pssm-ID: 410786  Cd Length: 102  Bit Score: 166.01  E-value: 7.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 134 PSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 213
Cdd:cd21083     3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                          90
                  ....*....|....*...
gi 1958754287 214 SCGLITLTDAQRLCNALL 231
Cdd:cd21083    83 SCGLITKTDAERLCNALL 100
Ski_Sno pfam02437
SKI/SNO/DAC family; This family contains a presumed domain that is about 100 amino acids long. ...
 133-232 1.17e-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: 165.53  E-value: 1.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 133 IPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 212
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 1958754287 213 PSCGLITLTDAQRLCNALLR 232
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 141-228 4.02e-34

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


Pssm-ID: 410781  Cd Length: 88  Bit Score: 125.10  E-value: 4.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 141 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21074     1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                  ....*...
gi 1958754287 221 TDAQRLCN 228
Cdd:cd21074    81 SDAERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 141-231 2.22e-16

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


Pssm-ID: 410783  Cd Length: 91  Bit Score: 74.79  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 141 LTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 220
Cdd:cd21080     1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                          90
                  ....*....|.
gi 1958754287 221 TDAQRLCNALL 231
Cdd:cd21080    81 REAERLCKSFL 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 518-668 1.02e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  518 DDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKamKELTEEQQNLQKELESLQnehaqrmeefyIEQRDLE 597
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELE-----------ELIEELE 872

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287  598 KKLEQVMKQKCTCDSNVEKDKEAEY--AAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
533-667 1.88e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRmEEFYIEQRDLEK---KLEQVMKQKCT 609
Cdd:COG4717   106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAelaELQEELEELLE 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958754287 610 CDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 667
Cdd:COG4717   185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 524-677 2.36e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 524 VEDVMRTYVRQQEKL---SSILQKKQQLQME---VEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEfyieQRDLE 597
Cdd:COG1196   191 LEDILGELERQLEPLerqAEKAERYRELKEElkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 598 KKLEQVMKQKCTCDSNVEKDKEAEYAA---------QLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELlaelarleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346


                  ....*....
gi 1958754287 669 VKSSKTAKE 677
Cdd:COG1196   347 EEAEEELEE 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 533-668 1.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQNEHAQRMEEfyieQRDLEKKLEQVMKQKctcds 612
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELE--LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELEEEL----- 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 613 NVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
529-668 1.45e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  529 RTYVRQQ--------EKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQNEHAQRMEEfyIEQRDLEKKL 600
Cdd:COG4913    595 RRRIRSRyvlgfdnrAKLAALEAELAELEEELAEAE--ERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREI 670

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958754287  601 EQVMKQKctcdSNVEKDKeaeyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG4913    671 AELEAEL----ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 529-656 2.50e-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: 52.23  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 529 RTYVRQQEKLSSILQKKQQLQMEVEmlSSSKAMKELTEEQQNL--QKELESLQNEhaqrMEEFYIEQRDLEKKLEQVMKQ 606
Cdd:COG1579    45 ARLEAAKTELEDLEKEIKRLELEIE--EVEARIKKYEEQLGNVrnNKEYEALQKE----IESLKRRISDLEDEILELMER 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958754287 607 KctcDSNVEKDKEAEyaAQLAELRQRLDHAEADRQELQDELRQEREARQK 656
Cdd:COG1579   119 I---EELEEELAELE--AELAELEAELEEKKAELDEELAELEAELEELEA 163
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 543-677 2.55e-07

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: 53.87  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 543 QKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRmeefyieQRDLEKKLEQVMKQKCTCDSNVEKDKEAEy 622
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK-------QRELEEKQNEIEKLKKENQSYKQEIKNLE- 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287 623 aAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:TIGR04523 391 -SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
541-658 2.72e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 2.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  541 ILQKKQQLQmevEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEfyieQRDLEKKLEQVMKQKCTCDSNVEKDKEA 620
Cdd:COG4913    670 IAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDL 742

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958754287  621 EYAAQLAELRQRLDHAEAD------RQELQDELRQEREARQKLE 658
Cdd:COG4913    743 ARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 456-668 2.85e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  456 EEQEKMDLKTSRELYSCLDSSVSNNSTSKKKCESTICDLVRDTDKQGSGASSPLVVRDVTCEDDKGKIVEDVMRTYVRQQ 535
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  536 EKLSSILQKKQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEqvmkqkctcdsnve 615
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEI------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-------------- 871

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  616 kdkeaEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE-------MMIKELKLQI 668
Cdd:TIGR02169  872 -----ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiekkrKRLSELKAKL 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 533-677 7.58e-07

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: 51.69  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQR--------------DLEK 598
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVR 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958754287 599 KLeQVMKQKctcdSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG4942   137 RL-QYLKYL----APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 535-664 8.17e-07

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 52.15  E-value: 8.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQL--QMEVEMlsssKAMKELTEEQQNLQKELESLQNEHAQRMEEF------YI-------EQRDLEKK 599
Cdd:PRK04778  281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287 600 LEQVMKQKCTCDSNVEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELRQ----EREARQKLEMMIKEL 664
Cdd:PRK04778  357 LESLEKQYDEITERIAEQEIAysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKL 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 484-668 1.46e-06

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: 51.71  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  484 KKKCESTICDLVRDTDKQgSGASSPLVVRDVTCEDDKGKIVEDVMrTYVRQQEKLSsilQKKQQLQMEVEMLSSSKAMKE 563
Cdd:pfam01576   98 KKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDIL-LLEDQNSKLS---KERKLLEERISEFTSNLAEEE 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  564 ltEEQQNLQKelesLQNEHAQRMEEFYIEQRDLEK-KLEQV-MKQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQ 641
Cdd:pfam01576  173 --EKAKSLSK----LKNKHEAMISDLEERLKKEEKgRQELEkAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246

                          170       180
                   ....*....|....*....|....*..
gi 1958754287  642 ELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:pfam01576  247 AALARLEEETAQKNNALKKIRELEAQI 273
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 533-677 1.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEmlssskamkELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVmkqkctcdS 612
Cdd:COG1196   236 ELEAELEELEAELEELEAELE---------ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------A 298

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287 613 NVEKDKEAEyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG1196   299 RLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 531-668 1.82e-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: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  531 YVRQQEKLSSILQKKQQL--QMEVEMLSSSKAMKELTEEQQNLQKELESLQNE---HAQRMEEFYIEQRDLEKKLEQVMK 605
Cdd:TIGR02168  251 AEEELEELTAELQELEEKleELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287  606 QKCTCDSNVE--KDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:TIGR02168  331 KLDELAEELAelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 144-228 2.26e-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: 46.18  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 144 TVLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDA 223
Cdd:cd21082     4 EEVHGVELGYLYINGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDV 83


                  ....*
gi 1958754287 224 QRLCN 228
Cdd:cd21082    84 ERLYS 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 543-677 2.45e-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: 50.83  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  543 QKKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQNEHaQRMEEfyiEQRDLEKKLEQVMKQKCTCDSNVE------- 615
Cdd:TIGR02168  239 EELEELQEELKEAEEE--LEELTAELQELEEKLEELRLEV-SELEE---EIEELQKELYALANEISRLEQQKQilrerla 312

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754287  616 --KDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:TIGR02168  313 nlERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
529-668 2.50e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  529 RTYVRQQEKLssiLQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQ----RMEEFYIEQRDLEKKLEQV- 603
Cdd:COG4913    282 RLWFAQRRLE---LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERe 358

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287  604 -----MKQKC-TCDSNVEKDkEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG4913    359 rrrarLEALLaALGLPLPAS-AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 517-668 2.80e-06

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.92  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 517 EDDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMlssSKAMKELTEEQQNLQKELESL-----QNEHAQRMEEFYI 591
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE---FNEEQAEWKELEKEEEREEDErileyLKEKAEREEEREA 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958754287 592 EQRDLEKKLEQVMKQKCTcdsnvEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:pfam13868 174 EREEIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 517-667 3.64e-06

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: 47.60  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 517 EDDKGKIVEDVMRTYVRQQEKLSSILQKKQQlqmevemlssskaMKELTEeqqNLQK-ELESLQNEHAQRMEEfyIEQRD 595
Cdd:pfam13870   1 MRAKRNELSKLRLELITLKHTLAKIQEKLEQ-------------KEELGE---GLTMiDFLQLQIENQALNEK--IEERN 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287 596 LEKKleqVMKQKCTCDS---NVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQ 667
Cdd:pfam13870  63 KELK---RLKLKVTNTVhalTHLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ 134
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 523-665 3.79e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.21  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 523 IVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMlsssKAmkeltEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQ 602
Cdd:PRK00409  503 IIEEAKKLIGEDKEKLNELIASLEELERELEQ----KA-----EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK 573

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287 603 VMKQKctcdsnVEKDKEaEYAAQLAELR--QRLDHAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:PRK00409  574 EAQQA------IKEAKK-EADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQK 631
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
508-665 3.92e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 508 PLVVRDVTcEDDKGKI-------VEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQN 580
Cdd:PRK03918  439 PVCGRELT-EEHRKELleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 581 EHAQRMEEFYieqRDLEKKLEQVMKQKctcdSNVEKD--KEAEYAAQLAELRQRLDHAEADRQELQDELRQER-EARQKL 657
Cdd:PRK03918  518 EELEKKAEEY---EKLKEKLIKLKGEI----KSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEEL 590


                  ....*...
gi 1958754287 658 EMMIKELK 665
Cdd:PRK03918  591 EERLKELE 598
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
535-668 4.61e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQN--EHAQRMEEFYIEQRDLEKKLEQVMKQKctcds 612
Cdd:COG4717   101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELAEL----- 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 613 nvEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG4717   176 --QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 535-664 4.72e-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: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQL--QMEVEMLS----------SSKAMKELTEEQQNLQKELESLQneHAQRMEEFYIE-QRDLEKKLE 601
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELKEELERVQ--QSYTLNENELErVRGLEKQLE 339

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 602 QVMKQkctCDSNVEKDKE-----AEYAAQLAELRQRLDHAEADRQELQDELR----QEREARQKLEMMIKEL 664
Cdd:pfam06160 340 ELEKR---YDEIVERLEEkevaySELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLEL 408
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 552-663 4.73e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 50.08  E-value: 4.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 552 VEMLSSSKAMKELTEEQQNLQKELESLQNE----HAQRMEEFYIEQRDLEKKLEQVMKQKctcdsnvekDKEAEYAAQLA 627
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEEIQ 474

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958754287 628 ELRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 663
Cdd:COG0542   475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
535-677 5.62e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSSSkaMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKctcdsnv 614
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREE--LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ------- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 615 ekdkeaeyaAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG4372   101 ---------EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE 154
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
535-675 6.62e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQ----NEH--AQRMEEfyiEQRDLEKKLEQVMKQ-K 607
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytPNHpdVIALRA---QIAALRAQLQQEAQRiL 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 608 CTCDSNVE--KDKEAEYAAQLAELRQRLDHAEADRQELQdELRQERE-ARQKLEMMIKELK-LQIVKSSKTA 675
Cdd:COG3206   316 ASLEAELEalQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQRLEeARLAEALTVG 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 539-677 7.73e-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: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  539 SSILQKKQQL--------QMEVEMLSSSKAMKELTEEQQNLQKELESLQ---NEHAQRMEEFYIEQRDLEKKLEQVMKQK 607
Cdd:TIGR02168  670 SSILERRREIeeleekieELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  608 CTCDSNVEK--DKEAEYAAQLAELRQRLDHAEADRQ---------------------ELQDELRQEREARQKLEMMIKEL 664
Cdd:TIGR02168  750 AQLSKELTEleAEIEELEERLEEAEEELAEAEAEIEeleaqieqlkeelkalrealdELRAELTLLNEEAANLRERLESL 829

                          170
                   ....*....|...
gi 1958754287  665 KLQIVKSSKTAKE 677
Cdd:TIGR02168  830 ERRIAATERRLED 842
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 518-677 8.07e-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: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 518 DDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDL- 596
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELE--ALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVs 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 597 ----------------------------EKKLEQVMKQKctcdsNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELR 648
Cdd:COG3883   104 yldvllgsesfsdfldrlsalskiadadADLLEELKADK-----AELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                         170       180
                  ....*....|....*....|....*....
gi 1958754287 649 QEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG3883   179 EQEALLAQLSAEEAAAEAQLAELEAELAA 207
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
520-677 8.42e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 8.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 520 KGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLssskamKELTEEQQNLQKELESLQNEHAQRmeEFYIEQRDLEKK 599
Cdd:COG4717    62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL------EELEEELEELEAELEELREELEKL--EKLLQLLPLYQE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958754287 600 LEQVmkqkctcdsnvekdkeaeyAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG4717   134 LEAL-------------------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
mukB PRK04863
chromosome partition protein MukB;
566-677 8.91e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 8.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  566 EEQQNLQKELESLQNEHAqRMEEFYIEQRDLEKKLEQVMKQkctcdSNVEKDKEAEYAAQLAELRQRLDHaeadrqeLQD 645
Cdd:PRK04863   506 REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKR-----LGKNLDDEDELEQLQEELEARLES-------LSE 572

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958754287  646 ELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:PRK04863   573 SVSEARERRMALRQQLEQLQARIQRLAARAPA 604
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 552-658 9.37e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 552 VEMLSS-SKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKctcdsnvekdkeAEYAAQLAELR 630
Cdd:COG3883   121 LSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLS 188

                          90       100
                  ....*....|....*....|....*...
gi 1958754287 631 QRLDHAEADRQELQDELRQEREARQKLE 658
Cdd:COG3883   189 AEEAAAEAQLAELEAELAAAEAAAAAAA 216
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 525-668 1.09e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  525 EDVMRTYVRQQEKLssilqKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFyieqRDLEKKLEQVM 604
Cdd:TIGR02169  307 ERSIAEKERELEDA-----EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVD 377

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754287  605 KqkctcdsnvekdKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:TIGR02169  378 K------------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 517-665 1.39e-05

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 47.57  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 517 EDDKGKIVEDVMRTYVRQQEKLS-SILQKKQQL-QMEVEMlsssKAMKELTEEQQNLQKELESLQNEHAQRMEEfyiEQR 594
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAeAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKLED---QER 233

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287 595 DLEKKLEQVMKQkctcdsnvekdKEAEYAAQLAELRQRLDHAEADRQELQDElrQEREARQKLEMMIKELK 665
Cdd:cd16269   234 SYEEHLRQLKEK-----------MEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 553-663 1.43e-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: 45.27  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  553 EMLSSSKAMKELTEEQQNLQKELESLQNEhaqrmeefyieqrdLEKKLEQVMKQKCTCDSNVEKDKEAEYAAQLAELRQr 632
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958754287  633 ldhaeaDRQELQDELRQER-EARQKLEMMIKE 663
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
513-665 1.50e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 513 DVTCEDDKGKIVEDVmRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEefyiE 592
Cdd:COG4717   380 GVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE----E 454

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 593 QRDLEKKLEQvmkqkctcdsnVEKDKEaeyaaqLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:COG4717   455 LAELEAELEQ-----------LEEDGE------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 533-677 1.55e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  533 RQQEKLSSILQKKQQ--LQMEVEMLSSSKAMKELTEEQQN-LQKELESLQNEHAQ--RMEEFYI-EQRDLEKKL----EQ 602
Cdd:TIGR02169  251 EELEKLTEEISELEKrlEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASleRSIAEKErELEDAEERLakleAE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  603 VMKQKCTCDS--------NVEKDK-EAEYA---AQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVK 670
Cdd:TIGR02169  331 IDKLLAEIEElereieeeRKRRDKlTEEYAelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410


                   ....*..
gi 1958754287  671 SSKTAKE 677
Cdd:TIGR02169  411 LQEELQR 417
PRK12704 PRK12704
phosphodiesterase; Provisional
 535-670 1.81e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQqlqMEVEMLSSsKAMKELTEEQQNLQKELEslqNEHAQRMEEFYIEQRDLEKKLEQVMKQKctcdSNV 614
Cdd:PRK12704   37 EEEAKRILEEAK---KEAEAIKK-EALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLDRKL----ELL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958754287 615 EKdKEAEYAAQLAELRQRLDHAEADRQELQDELRQER------------EARQK-LEMMIKELKLQIVK 670
Cdd:PRK12704  106 EK-REEELEKKEKELEQKQQELEKKEEELEELIEEQLqelerisgltaeEAKEIlLEKVEEEARHEAAV 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
525-673 2.42e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  525 EDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKEL------TEEQQNLQKELESLQNEHAQRMEEfyieQRDLEK 598
Cdd:COG4913    241 HEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAELEELRAELARLEAE----LERLEA 316

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287  599 KLEQVmkqkctcdsnveKDKEAEYAAQLAEL-RQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSK 673
Cdd:COG4913    317 RLDAL------------REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 553-663 2.45e-05

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: 45.21  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 553 EMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFyieQRDlEKKLEQVMKQKctcdsnvekdKEAEYAAQLAELRQR 632
Cdd:COG2825    37 ESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKL---QKE-AATLSEEERQK----------KERELQKKQQELQRK 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958754287 633 ldhaeadRQELQDELRQER-EARQKLEMMIKE 663
Cdd:COG2825   103 -------QQEAQQDLQKRQqELLQPILEKIQK 127
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 519-658 3.09e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 519 DKGKIVEDvmrtYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEK 598
Cdd:PRK09510   56 DPGAVVEQ----YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754287 599 KLEQVMKQKCTCDSNVEKDKE----AEYAAQLAELRQRLDHAEADRQelqdelrQEREARQKLE 658
Cdd:PRK09510  132 KQAEEAAAKAAAAAKAKAEAEakraAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 519-665 3.20e-05

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 46.51  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 519 DKGKIVEDVMRTYVRQQEKLS-SILQKKQQLqmeVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLE 597
Cdd:pfam02841 169 RKGVKAEEVLQEFLQSKEAVEeAILQTDQAL---TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHV 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958754287 598 KKLEQVMkqkctcdsnvekdkEAEYAAQLAELRQRLDHaeaDRQELQDELRQEREAR-QKLEMMIKELK 665
Cdd:pfam02841 246 KQLIEKM--------------EAEREQLLAEQERMLEH---KLQEQEELLKEGFKTEaESLQKEIQDLK 297
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 522-658 5.85e-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: 46.48  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  522 KIVEDVMRTYVRQQEKlsSILQKKQQLQMEVEMLSSSKAmkELTEEQQNL--QKELESLQNEHAQRMEEFYIEQRDLEKK 599
Cdd:COG3096    483 KIAGEVERSQAWQTAR--ELLRRYRSQQALAQRLQQLRA--QLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEEL 558

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958754287  600 LEQVMKQKCTCDsnvekDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE 658
Cdd:COG3096    559 LAELEAQLEELE-----EQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 533-667 8.48e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLssiLQKKQQLQMEVEMLsssKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCDS 612
Cdd:pfam13868  96 KLQERE---QMDEIVERIQEEDQ---AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREE 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 613 NVE---KDKEAEYAAQLAELRQRLDHAEaDRQELQDELR-------QEREARQK-LEMMIKELKLQ 667
Cdd:pfam13868 170 EREaerEEIEEEKEREIARLRAQQEKAQ-DEKAERDELRaklyqeeQERKERQKeREEAEKKARQR 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 535-677 9.72e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 9.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  535 QEKLSSILQKKQQLQMEVEMLSSskAMKELTEEQQNLQKELESLQNEHAQ---RMEEFYIEQRDLEKKLEQVMKQKctcd 611
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKE--ELKALREALDELRAELTLLNEEAANlreRLESLERRIAATERRLEDLEEQI---- 847

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287  612 snvekdkeAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:TIGR02168  848 --------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
509-665 9.98e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.62  E-value: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 509 LVVRDVTCEDdkgkIVEDVMRTYvrQQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQNEHAQRMEE 588
Cdd:COG2433   371 RVIRGLSIEE----ALEELIEKE--LPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDER 442

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958754287 589 fyIEqrDLEKKLEQVMKQKctcDSNVEKDKEAeyaaqlaelrQRLDhAEADRqeLQDELRQEREARQKLEMMIKELK 665
Cdd:COG2433   443 --IE--RLERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEEERERIEELKRKLERLK 499
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 528-677 1.16e-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: 44.15  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 528 MRTYVRQQEKLSSILQKKQQLQmevemlsssKAMKELTEEQQNLQKELESLQNEHA---QRMEEFYIEQRDLEKKLEQVm 604
Cdd:COG1579     2 MPEDLRALLDLQELDSELDRLE---------HRLKELPAELAELEDELAALEARLEaakTELEDLEKEIKRLELEIEEV- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 605 kqkctcDSNVEKDKEA--------EYAAQLAELrqrlDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAK 676
Cdd:COG1579    72 ------EARIKKYEEQlgnvrnnkEYEALQKEI----ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141


                  .
gi 1958754287 677 E 677
Cdd:COG1579   142 E 142
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 534-677 1.30e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.40  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 534 QQEKLSSILQKKQQlqmevEMLSSSKAMKELTEEQQNLQKELESLQNEHAQR-MEEFYIEQRDLEKKLEQVMKQKCTCDS 612
Cdd:TIGR04523 261 EQNKIKKQLSEKQK-----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEIQNQISQNNK 335

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958754287 613 NVEKDKEaeyaaQLAELRQRLDHAEADRQELQDELRQE--------------REARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:TIGR04523 336 IISQLNE-----QISQLKKELTNSESENSEKQRELEEKqneieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQ 409
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
533-677 1.59e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSI---LQKKQ--QLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEfyieqrdlEKKLEQVMKQK 607
Cdd:COG4372    77 QLEEELEELneqLQAAQaeLAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ--------IAELQSEIAER 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 608 ctcdsnvekdkeaeyAAQLAELRQRLDHAEADRQELQDELRQ--EREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG4372   149 ---------------EEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKEEELAEA 205
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 526-668 1.68e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  526 DVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKA-----MKELtEEQQNLQKELES-LQ--NEHAQRMEEFYIEQrdle 597
Cdd:COG3096    272 DYMRHANERRELSERALELRRELFGARRQLAEEQYrlvemAREL-EELSARESDLEQdYQaaSDHLNLVQTALRQQ---- 346

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754287  598 KKLEQvmkqkctcdsnvekdkeaeYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI 668
Cdd:COG3096    347 EKIER-------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQL 398
PRK11637 PRK11637
AmiB activator; Provisional
 559-655 1.80e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 559 KAMKEL--TEEQQNLQK-ELESLQNEHAQRMeefyIEQRDLEKKLEQVM--KQKC--TCDSNVEKDKeaeyaAQLAELRQ 631
Cdd:PRK11637  170 ETIAELkqTREELAAQKaELEEKQSQQKTLL----YEQQAQQQKLEQARneRKKTltGLESSLQKDQ-----QQLSELRA 240

                          90       100
                  ....*....|....*....|....*..
gi 1958754287 632 ---RLDHAEAdRQELQDELRQEREARQ 655
Cdd:PRK11637  241 nesRLRDSIA-RAEREAKARAEREARE 266
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 533-658 2.05e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLsssKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQkctcds 612
Cdd:COG1196   666 SRRELLAALLEAEAELEELAERL---AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------ 736

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958754287 613 nvEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLE 658
Cdd:COG1196   737 --LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 533-659 2.21e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.17  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELES---LQNEHAQ-----RMEEFYIEQRDLEKKLEQV 603
Cdd:pfam15709 363 LQQEQLERAEKMREELELEQQRRFEEiRLRKQRLEEERQRQEEEERkqrLQLQAAQerarqQQEEFRRKLQELQRKKQQE 442

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958754287 604 MKQKctcdSNVEKDKEAEYAAQLAELRQRL-DHAEADRQELQDElRQEREARQKLEM 659
Cdd:pfam15709 443 EAER----AEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQRQ-KQEAEEKARLEA 494
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 532-677 2.56e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 532 VRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDL----EKKLEQVMKQK 607
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERIRQEE 357

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754287 608 CTcdSNVEKDKEAEYAAQLAELRQrLDHAEADRQELQDELRQEREARQKLEMMIKE----LKLQIVKSSKTAKE 677
Cdd:pfam17380 358 RK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEErqrkIQQQKVEMEQIRAE 428
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
557-677 2.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 557 SSKAMKELTEEQQNLQKELESLQNEHAQRMEEFyieqRDLEKKLEQvmkqkctcdsnvEKDKEAEYAAQLAELRQRLDHA 636
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREEL----EQLEEELEQ------------ARSELEQLEEELEELNEQLQAA 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958754287 637 EADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:COG4372    93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 559-677 3.12e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 559 KAMKELTEEQQNLQ----------KELESL--QNEHAQRmeefYIEQRDLEKKLE-QVMKQKctcDSNVEKDKEaEYAAQ 625
Cdd:COG1196   176 EAERKLEATEENLErledilgeleRQLEPLerQAEKAER----YRELKEELKELEaELLLLK---LRELEAELE-ELEAE 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958754287 626 LAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL--KLQIVKSSKTAKE 677
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAqaEEYELLAELARLE 301
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
536-665 3.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 536 EKLSSILQKKQQLQMEVEMLSSS-KAMKELTEEQQNLQKELESLQNEHA----------QRMEEFYIEQRDLEKKLEQVM 604
Cdd:PRK03918  207 REINEISSELPELREELEKLEKEvKELEELKEEIEELEKELESLEGSKRkleekireleERIEELKKEIEELEEKVKELK 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 605 KQKCTCDSNVEKDKE-AEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:PRK03918  287 ELKEKAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 533-665 4.25e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  533 RQQEKLSSILQKKQQLQM--------------------EVEMLSSSKAMKELTE---EQQNLQKELESLQNEHAQrMEEF 589
Cdd:COG3096    449 KEQQATEEVLELEQKLSVadaarrqfekayelvckiagEVERSQAWQTARELLRryrSQQALAQRLQQLRAQLAE-LEQR 527

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287  590 YIEQRDLEKKLEQVMKQkctcdSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:COG3096    528 LRQQQNAERLLEEFCQR-----IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 535-665 4.40e-04

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


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 41.48  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSS---SKAMKELTEEQQNLQKELESLQNEHAQRMEEFyieQRDLEKKLEQVmkqkctcd 611
Cdd:pfam01442   3 EDSLDELSTYAEELQEQLGPVAQelvDRLEKETEALRERLQKDLEEVRAKLEPYLEEL---QAKLGQNVEEL-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958754287 612 snvekdkEAEYAAQLAELRQRLdhaEADRQELQDELRQE-REARQKLEMMIKELK 665
Cdd:pfam01442  72 -------RQRLEPYTEELRKRL---NADAEELQEKLAPYgEELRERLEQNVDALR 116
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
534-677 4.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 534 QQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQ-------NEHAQRMEEFY---IEQRDLEKKLEQV 603
Cdd:PRK03918  540 EIKSLKKELEKLEELKKKLAELE--KKLDELEEELAELLKELEELGfesveelEERLKELEPFYneyLELKDAEKELERE 617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 604 MKQKCTCDSNVEK--DKEAEYAAQLAELRQRLDHAEADRQE-------------------LQDELRQEREARQKLEMMIK 662
Cdd:PRK03918  618 EKELKKLEEELDKafEELAETEKRLEELRKELEELEKKYSEeeyeelreeylelsrelagLRAELEELEKRREEIKKTLE 697

                         170
                  ....*....|....*
gi 1958754287 663 ELKLQIVKSSKTAKE 677
Cdd:PRK03918  698 KLKEELEEREKAKKE 712
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 544-667 4.50e-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: 41.82  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 544 KKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNE------HAQRMEEFYIEQRDLEKKLeqvmkqkctcdsnvekd 617
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQlenyekDKQSLKNLKARLKVLEKEL----------------- 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 618 KEAEYAAQLaeLRQRLDHAEADRQELQDELRQE-REARQK--LEMMIKELKLQ 667
Cdd:pfam13851 102 KDLKWEHEV--LEQRFEKVERERDELYDKFEAAiQDVQQKtgLKNLLLEKKLQ 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
565-677 4.53e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 565 TEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKctcdSNVEKDKEaeyaaQLAELRQRLDHAEADRQELQ 644
Cdd:PRK03918  188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKE-----EIEELEKELESLEGSKRKLE 258

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958754287 645 DELRQEREARQKLEMMIKELKlQIVKSSKTAKE 677
Cdd:PRK03918  259 EKIRELEERIEELKKEIEELE-EKVKELKELKE 290
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
533-669 5.49e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCDS 612
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQ--KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958754287 613 NVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIV 669
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
535-673 6.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQNEHaqrmeEFYIEQRDLEKKLEQVMKQKctcdsn 613
Cdd:PRK03918  313 EKRLSRLEEEINGIEERIKELEEKEErLEELKKKLKELEKRLEELEERH-----ELYEEAKAKKEELERLKKRL------ 381

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 614 veKDKEAEyaaqlaELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQI--VKSSK 673
Cdd:PRK03918  382 --TGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeeLKKAK 435
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
536-665 6.36e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 536 EKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLqkelesLQNEHAQRMEEFYI------EQRDLEKKLEQVMKQkct 609
Cdd:COG4717   340 LELLDRIEELQELLREAEELEEELQLEELEQEIAAL------LAEAGVEDEEELRAaleqaeEYQELKEELEELEEQ--- 410

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 610 CDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:COG4717   411 LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 554-670 7.54e-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: 41.89  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 554 MLSSSKAMKELTEeqqnLQKELES-LQNEHAQRMEEF--YIEQRDLEKKLEQVMKQKCTCDSNVE-KDKEAEYAAQLAel 629
Cdd:pfam12037  37 ELESSPHAKKALE----LMKKQEQtRQAELQAKIKEYeaAQEQLKIERQRVEYEERRKTLQEETKqKQQRAQYQDELA-- 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958754287 630 RQRL-DHAEADRQELQDELRQEREARQKLEMM-IKELKLQIVK 670
Cdd:pfam12037 111 RKRYqDQLEAQRRRNEELLRKQEESVAKQEAMrIQAQRRQTEE 153
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 535-587 7.58e-04

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


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 38.40  E-value: 7.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 535 QEKLSSILQKKQQLQMEVEMLSSSKAmkELTEEQQNLQKELESLQNEHAQRME 587
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENE--ELKEEANELEEENQQLKQERNQWQE 60
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 148-226 7.70e-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: 7.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 148 GESISCFQVGGEKRLCLPQVLNSVLREF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 225
Cdd:cd21081    10 GAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                  .
gi 1958754287 226 L 226
Cdd:cd21081    90 L 90
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 533-663 9.13e-04

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: 41.95  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQ----QLQMEVEMLSSSKAMKELT----------EEQQNLQKELES----LQNEHAQRMEEFYIEQR 594
Cdd:pfam15558 146 QLQERLEEACHKRQlkerEEQKKVQENNLSELLNHQArkvlvdcqakAEELLRRLSLEQslqrSQENYEQLVEERHRELR 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 595 DLEKKLE-QVMKQKCTCD-SNVEKDKEAEYAAQLAE--LRQRLDHAEADRQELQDELRQEREARQKLEMMIKE 663
Cdd:pfam15558 226 EKAQKEEeQFQRAKWRAEeKEEERQEHKEALAELADrkIQQARQVAHKTVQDKAQRARELNLEREKNHHILKL 298
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 533-670 9.39e-04

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: 41.83  E-value: 9.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSSSKAM---------KELTEEQQNLQKELESLQNEHAQRM--EEFYIEQRDLEKKLE 601
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQeeqerkerqKEREEAEKKARQRQELQQAREEQIElkERRLAEEAEREEEEF 263

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958754287 602 QVMKQKCTCDSNVEKDKEAEYAAQLAELRQ--------RLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVK 670
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRelekqieeREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 553-663 1.12e-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: 39.87  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 553 EMLSSSKAMKELTEEQQNLQKELESLQNEHaqrmeefyieqRDLEKKLEQVMKQKctcdSNVEKDKEAEYAAQLAELRQR 632
Cdd:pfam03938  13 ESPEGKAAQAQLEKKFKKRQAELEAKQKEL-----------QKLYEELQKDGALL----EEEREEKEQELQKKEQELQQL 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958754287 633 ldhaeadRQELQDELRQER-EARQKLEMMIKE 663
Cdd:pfam03938  78 -------QQKAQQELQKKQqELLQPIQDKINK 102
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 513-677 1.22e-03

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: 41.97  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 513 DVTCEDDKGKIVEDVMRTYVRQQEKLSSILQKKQQ-LQMEVEMLSSSKAMKELTEEQQNLQKELESL------QNEHAQR 585
Cdd:pfam13166 308 AVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRaLEAKRKDPFKSIELDSVDAKIESINDLVASIneliakHNEITDN 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 586 MEEfyiEQRDLEKKLEQVMKQKctCDSNVEKDKEAeYAAqlaelrqrldhAEADRQELQDELRQEREARQKLEMMIKELK 665
Cdd:pfam13166 388 FEE---EKNKAKKKLRLHLVEE--FKSEIDEYKDK-YAG-----------LEKAINSLEKEIKNLEAEIKKLREEIKELE 450

                         170
                  ....*....|..
gi 1958754287 666 LQIVKSSKTAKE 677
Cdd:pfam13166 451 AQLRDHKPGADE 462
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 526-665 1.27e-03

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: 40.80  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 526 DVMRTYvrqQEKLSSILQKKQQLQMEVEMLSSSKAMKE--LTEEQQNLQKELES---LQNEHAQRMEEFYIE----QRDL 596
Cdd:pfam15665  36 EKILQY---KSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEFEQYKRRVEERelkAEAEHRQRVVELSREveeaKRAF 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 597 EKKLEQVMKQKctcdSNVEKDKE-------AEYAAQLAELRQRLD--HAE--ADRQELQDELRQEREA-RQKLEMMIKEL 664
Cdd:pfam15665 113 EEKLESFEQLQ----AQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRKEVEDLRKEK 188


                  .
gi 1958754287 665 K 665
Cdd:pfam15665 189 K 189
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 522-665 1.34e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.76  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 522 KIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEfyieqrDLEKKLE 601
Cdd:pfam06160 200 PLYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALE------EIEERID 273

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 602 QVMKQkctcdsnVEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELRQ----------EREARQKLEMMIKELK 665
Cdd:pfam06160 274 QLYDL-------LEKEVDAkkYVEKNLPEIEDYLEHAEEQNKELKEELERvqqsytlnenELERVRGLEKQLEELE 342
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 532-677 1.39e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 40.86  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 532 VRQQEKLSSILQKKQQLQMEVEMLSSSKamkeLTEEQQNLQKELESLQN----EHAQRMEEFYIEQRDLEK---KLEQVM 604
Cdd:pfam06008  92 KNLIDNIKEINEKVATLGENDFALPSSD----LSRMLAEAQRMLGEIRSrdfgTQLQNAEAELKAAQDLLSriqTWFQSP 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958754287 605 KQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQD-----ELRQEREARQKLEmmIKELKLQIVKSSKTAKE 677
Cdd:pfam06008 168 QEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRlnlanQANLREFQRKKEE--VSEQKNQLEETLKTARD 243
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 543-667 1.42e-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: 41.44  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 543 QKKQQLQMEVEMLSSSKAMKEltEEQQNLQKELESLQNEHAQrmeefyIEQRDLEKKLEQVMKQKCTCdsNVEKDKEAEY 622
Cdd:pfam13868  42 ERRLDEMMEEERERALEEEEE--KEEERKEERKRYRQELEEQ------IEEREQKRQEEYEEKLQERE--QMDEIVERIQ 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958754287 623 AAQLAELRQRLDHAEADRQELQD--ELRQEREARQKLEMMIKELKLQ 667
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEfnEEQAEWKELEKEEEREEDERIL 158
PTZ00121 PTZ00121
MAEBL; Provisional
 519-677 1.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  519 DKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEV-EMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLE 597
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  598 KKLEQVMKQKctCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:PTZ00121  1647 KKAEELKKAE--EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
522-664 2.17e-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: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 522 KIVEDVMRTYVRQQeklssiLQKKQQlqmevemlSSSKAMKELTEEQQNLQKELESLQnehaQRMEEFYIEQRDLEkkLE 601
Cdd:COG3206   152 AVANALAEAYLEQN------LELRRE--------EARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVD--LS 211

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 602 QVMKQkctcdsnvekdkeaeYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 664
Cdd:COG3206   212 EEAKL---------------LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
HAUS5 pfam14817
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ...
 535-676 2.20e-03

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464332 [Multi-domain]  Cd Length: 643  Bit Score: 41.18  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQLQMEVEmlssskamkELTEEQQNLQKELESlqnehaqRMEEFYIEQRDLEKKLEQVMKQKCTcdsnv 614
Cdd:pfam14817  69 AESRQSAAARRLELQKEIE---------RLRAEISRLDKQLEA-------RELELSREEAERERALDEISDSRHR----- 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 615 ekdkeaeyAAQLAELRQRLDHAE----ADRQELQDELRQEREARQKLEmmiKELKLQIVKSSKTAK 676
Cdd:pfam14817 128 --------QLLLEAYDQQCEEARkilaEDHQRLQGQLQQLRDAARKAE---KEVVFGDSKGSKSSV 182
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 551-649 2.71e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 551 EVEMLSSSKAMKELTEEQQNLQKELESLQNEhAQRMEEfyiEQRDLEKKLEqvmkqkctcdsnvekdkEAEyaAQLAELR 630
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNE---EYNELQAELE-----------------ALQ--AEIDKLQ 71

                          90
                  ....*....|....*....
gi 1958754287 631 QRLDHAEADRQELQDELRQ 649
Cdd:COG3883    72 AEIAEAEAEIEERREELGE 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
534-666 2.89e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 534 QQEKLSSILQKKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMeefyieqrdleKKLEQVMKQKCTC--- 610
Cdd:PRK03918  373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK-----------KAIEELKKAKGKCpvc 441

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 611 ----DSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKL 666
Cdd:PRK03918  442 grelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 528-677 2.91e-03

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: 41.11  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  528 MRTYVRQQEKLSSILQKKQQ--LQMEVEMLSS------SKAMKELTEEQQNLQKELESLQNEHAQR---MEEFYIEQRDL 596
Cdd:pfam02463  134 AYNFLVQGGKIEIIAMMKPErrLEIEEEAAGSrlkrkkKEALKKLIEETENLAELIIDLEELKLQElklKEQAKKALEYY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  597 EKKL-EQVMKQKCTCDS--NVEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREarqKLEMMIKELKLQIVKSSK 673
Cdd:pfam02463  214 QLKEkLELEEEYLLYLDylKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK---ENKEEEKEKKLQEEELKL 290


                   ....
gi 1958754287  674 TAKE 677
Cdd:pfam02463  291 LAKE 294
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 567-668 3.00e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 567 EQQNLQKELESLQNEHAQRMEEFYIEQRDLEKkleqvmkqkctcdsnvekdKEAEYAAQLAELRQRLDHAEADRQELQDE 646
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEK-------------------KEQELKEDLIKFDKFLKENDAKRRRALKK 67

                          90       100
                  ....*....|....*....|..
gi 1958754287 647 LRQEREARQKLEMMIKELKLQI 668
Cdd:pfam13863  68 AEEETKLKKEKEKEIKKLTAQI 89
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 493-677 3.37e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  493 DLVRDTDKQGSgASSPLVVRDVTCEDDKGKIVED----VMRTYVRQQEKLSSILQKKQQLQMEVEMLSssKAMKELTEEQ 568
Cdd:smart00787  84 DLFKEIEEETL-INNPPLFKEYFSASPDVKLLMDkqfqLVKTFARLEAKKMWYEWRMKLLEGLKEGLD--ENLEGLKEDY 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  569 QNLQKELESLQNEHAQRMEEF--YIEQRDLEKKLEQVMKQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQELQDE 646
Cdd:smart00787 161 KLLMKELELLNSIKPKLRDRKdaLEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESK 240

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958754287  647 LRQEREARQKLEMMIKELKLQIVKSSK-TAKE 677
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKKLEQCRGfTFKE 272
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 538-600 3.45e-03

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


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 37.99  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 538 LSSILQK-KQQLQMEVEMLSSSKamkeltEEQQNLQKELESLQ--NEHAQRMEEFYIEQRDLEKKL 600
Cdd:cd14798     5 VSFLLEKlGELLEQEADLLSGVK------EEIESLKDELESMQafLKDADAKQDEDEELKDWVKQV 64
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 504-676 3.50e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 504 GASSPLVVRDVT--CEDDKGKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSSSKAMKElTEEQQNLQKEleslQNE 581
Cdd:pfam15709 295 GRSSPTQTFVVTgnMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRRE-QEEQRRLQQE----QLE 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 582 HAQRM-EEFYIEQRdleKKLEQVMKQKctcdsnvekdkeaeyaAQLAELRQRLDHAEAdRQELQDELRQEREARQKLEMM 660
Cdd:pfam15709 370 RAEKMrEELELEQQ---RRFEEIRLRK----------------QRLEEERQRQEEEER-KQRLQLQAAQERARQQQEEFR 429

                         170
                  ....*....|....*.
gi 1958754287 661 IKELKLQIVKSSKTAK 676
Cdd:pfam15709 430 RKLQELQRKKQQEEAE 445
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 521-651 3.54e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 38.78  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 521 GKIVEDvmrtyvRQQEKLSSILQKKQQLQmevemlsssKAMKELTEEQQNL---QKELESLQNEHAQRMEEfyIEQrDLE 597
Cdd:PRK07352   45 GKILEE------RREAILQALKEAEERLR---------QAAQALAEAQQKLaqaQQEAERIRADAKARAEA--IRA-EIE 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754287 598 KKLEQVM---KQkctcdsNVEKDKEAEYAAQLAELRQR-----LDHAEADRQELQDELRQER 651
Cdd:PRK07352  107 KQAIEDMarlKQ------TAAADLSAEQERVIAQLRREaaelaIAKAESQLPGRLDEDAQQR 162
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 460-664 3.76e-03

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


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 40.40  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 460 KMDLKTSRELYsclDSSVSNNSTSKKKCESTICDLvRDTDKQgsgassplvVRDVTCEDDKGKIVEDVMRT--------- 530
Cdd:pfam05701 144 KEELESLRKEY---ASLVSERDIAIKRAEEAVSAS-KEIEKT---------VEELTIELIATKESLESAHAahleaeehr 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 531 ----YVRQQEKLSsiLQKK-QQLQMEVEML----SSSKAMKELTEE----QQNLQKEL----ESLQNEHAQRMEEFYIEQ 593
Cdd:pfam05701 211 igaaLAREQDKLN--WEKElKQAEEELQRLnqqlLSAKDLKSKLETasalLLDLKAELaaymESKLKEEADGEGNEKKTS 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 594 RDLEKKLEQVMKQKCTCDSNVEKDK-EAEY---------------AAQLAELRQRLDHAEADRQELQDELR--------- 648
Cdd:pfam05701 289 TSIQAALASAKKELEEVKANIEKAKdEVNClrvaaaslrselekeKAELASLRQREGMASIAVSSLEAELNrtkseialv 368

                         250
                  ....*....|....*...
gi 1958754287 649 --QEREARQKLEMMIKEL 664
Cdd:pfam05701 369 qaKEKEAREKMVELPKQL 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 532-653 4.05e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  532 VRQQEKLSSILQKKQQLQMEVEMLS---SSKAMKELTEEQQNLQKELESLQNEHAqRMEEFYIEQRDLEKKLEQVMKQkc 608
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLkklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA-- 479

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958754287  609 tcdsnvekdkeaeYAAQLAELRQRLDHAEADRQELQDELRQEREA 653
Cdd:TIGR02168  480 -------------AERELAQLQARLDSLERLQENLEGFSEGVKAL 511
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 533-628 4.05e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 533 RQQEKLSSILQKKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCD 611
Cdd:COG3883   130 ADADLLEELKADKAELEAKKAELEAKLAeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209

                          90
                  ....*....|....*..
gi 1958754287 612 SNVEKDKEAEYAAQLAE 628
Cdd:COG3883   210 AAAAAAAAAAAAAAAAA 226
DUF4175 pfam13779
Domain of unknown function (DUF4175);
561-663 4.06e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 40.36  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 561 MKELTEEQQNLQKELESLQNEHAQRMeefyiEQRDLEK---KLEQVMKQkctcdsnveKDKEAeyAAQ-LAELRQRLDHA 636
Cdd:pfam13779 526 MQALAEQAQQNPQDLQQPDDPNAQEM-----TQQDLQRmldRIEELARS---------GRRAE--AQQmLSQLQQMLENL 589

                          90       100
                  ....*....|....*....|....*....
gi 1958754287 637 E-ADRQELQDELRQE-REARQKLEMMIKE 663
Cdd:pfam13779 590 QaGQPQQQQQQGQSEmQQAMDELGDLLRE 618
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
562-665 4.10e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 562 KELTEEQQNLQKELESLQNEHAQRMEEfyieQRDLEKKLEQVMKQkcTCDSNVEKDKEAEYaaqLAELRQRLDHAEADRQ 641
Cdd:PRK02224  359 EELREEAAELESELEEAREAVEDRREE----IEELEEEIEELRER--FGDAPVDLGNAEDF---LEELREERDELREREA 429

                          90       100
                  ....*....|....*....|....
gi 1958754287 642 ELQDELRQEREARQKLEMMIKELK 665
Cdd:PRK02224  430 ELEATLRTARERVEEAEALLEAGK 453
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 522-606 4.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 522 KIVEDVMRTYVRQQEKLSSILQKKQQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKL 600
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229


                  ....*.
gi 1958754287 601 EQVMKQ 606
Cdd:COG4942   230 ARLEAE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
534-664 4.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 534 QQEKLSSilqKKQQLQMEVEmlSSSKAMKELTEEQQNLQKELESLQnEHAQRMEEfyiEQRDLEKKLEqvmkqkcTCDSN 613
Cdd:PRK02224  315 RREELED---RDEELRDRLE--ECRVAAQAHNEEAESLREDADDLE-ERAEELRE---EAAELESELE-------EAREA 378

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958754287 614 VEKDKE--AEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKEL 664
Cdd:PRK02224  379 VEDRREeiEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL 431
mukB PRK04863
chromosome partition protein MukB;
526-668 5.38e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  526 DVMRTYVRQQEKLSSILQKKQQLQMEVemlsssKAMKELTEEQQNLQK-----------------ELESLQNEHAQRME- 587
Cdd:PRK04863   496 DVARELLRRLREQRHLAEQLQQLRMRL------SELEQRLRQQQRAERllaefckrlgknlddedELEQLQEELEARLEs 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  588 ---------EFYIEQRDLEKKLEQVMKQkctcdsnVEKDKEAEYAAQ--LAELRQRLDHAEADR-------QELQDELRQ 649
Cdd:PRK04863   570 lsesvsearERRMALRQQLEQLQARIQR-------LAARAPAWLAAQdaLARLREQSGEEFEDSqdvteymQQLLERERE 642

                          170
                   ....*....|....*....
gi 1958754287  650 EREARQKLEMMIKELKLQI 668
Cdd:PRK04863   643 LTVERDELAARKQALDEEI 661
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 544-676 5.56e-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: 40.01  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 544 KKQQLQMEVEMLSSSKAMKELTEE--QQNLQKELESLQ---NEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCDS-NVEKD 617
Cdd:pfam05667 304 EKLQFTNEAPAATSSPPTKVETEEelQQQREEELEELQeqlEDLESSIQELEKEIKKLESSIKQVEEELEELKEqNEELE 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 618 KEAEYAAQLAELrqrLDHAEADRQELQ-------------------------DELR--------QEREARQKLEmMIKEL 664
Cdd:pfam05667 384 KQYKVKKKTLDL---LPDAEENIAKLQalvdasaqrlvelagqwekhrvpliEEYRalkeaksnKEDESQRKLE-EIKEL 459

                         170
                  ....*....|..
gi 1958754287 665 KLQIVKSSKTAK 676
Cdd:pfam05667 460 REKIKEVAEEAK 471
mukB PRK04863
chromosome partition protein MukB;
531-677 5.71e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 5.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  531 YVRQQ----EKLSSILQKKQQLQMEVEMLSssKAMKELTEEQQNLQKELESLqNEHAQRMEEF-YIE-QRDLEKKleqvm 604
Cdd:PRK04863   912 FVQQHgnalAQLEPIVSVLQSDPEQFEQLK--QDYQQAQQTQRDAKQQAFAL-TEVVQRRAHFsYEDaAEMLAKN----- 983

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754287  605 kqkctcDSNVEKdkeaeyaaqlaeLRQRLDHAEADRQELQDELRQ-EREARQKLEMMIKelklqiVKSSKTAKE 677
Cdd:PRK04863   984 ------SDLNEK------------LRQRLEQAEQERTRAREQLRQaQAQLAQYNQVLAS------LKSSYDAKR 1033
valS PRK05729
valyl-tRNA synthetase; Reviewed
 564-634 5.96e-03

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 40.09  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 564 LTEEQQNLQKELESLQNEhaqrmeefyIEQrdLEKKL----------EQVMKQkctcdsnvEKDKEAEYAAQLAELRQRL 633
Cdd:PRK05729  809 VEAELARLEKELAKLEKE---------IER--VEKKLsnegfvakapEEVVEK--------EREKLAEYEEKLAKLKERL 869


                  .
gi 1958754287 634 D 634
Cdd:PRK05729  870 A 870
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 562-676 6.80e-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: 38.51  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 562 KELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKLEQVMKQKCTCDSNVEKDKEaEYAAQLAELRQRLDHAEADRQ 641
Cdd:pfam04012  25 KMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNE-ELAREALAEKKSLEKQAEALE 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958754287 642 ELQDELR----QEREARQKLEMMIKEL--KLQIVKS-SKTAK 676
Cdd:pfam04012 104 TQLAQQRsaveQLRKQLAALETKIQQLkaKKNLLKArLKAAK 145
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 489-672 7.14e-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: 39.56  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 489 STICDLVRDTDKQGSGASSPLVVRDVTCEDDKgKIVEDVMRTYVRQQEKLSSILQKKQQLQMEVEMLSS-SKAMKELTEE 567
Cdd:COG5185   183 GLTLGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQtSDKLEKLVEQ 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 568 QQNLQKELESLQNEHAQRMEEFYIEQ----RDLEKKLEQVMKQKCTCDSNVEKDKEAEYAAQLAELRQRLDHAEADRQEL 643
Cdd:COG5185   262 NTDLRLEKLGENAESSKRLNENANNLikqfENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNL 341

                         170       180
                  ....*....|....*....|....*....
gi 1958754287 644 QDELRQEREARQKLEMMIKELKLQIVKSS 672
Cdd:COG5185   342 TAEIEQGQESLTENLEAIKEEIENIVGEV 370
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 543-665 7.80e-03

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 37.23  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 543 QKKQQLQMEVEMLSSSKAmkELTEEQQNLQKELESlQNEHAQRMEEFYiEQrdlekkleQVMKQkctcdsnvekdkeAEY 622
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAA--DAEAQLQKLQEDLEK-QAEIAREAQQNY-ER--------ELVLH-------------AED 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958754287 623 AAQLAELRQRLDHAEADRQELQDELRQER-----------EARQKLEMMIKELK 665
Cdd:pfam07926  56 IKALQALREELNELKAEIAELKAEAESAKaeleeseesweEQKKELEKELSELE 109
46 PHA02562
endonuclease subunit; Provisional
 522-647 7.87e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 522 KIVEDVMRTYV-RQQEKL--SSILQKKQQLQMeVEMLSSSkaMKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEK 598
Cdd:PHA02562  154 KLVEDLLDISVlSEMDKLnkDKIRELNQQIQT-LDMKIDH--IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958754287 599 KLEQVMKQKCTCDSNVEKDKEaEYAAQLAELRQRLDHAEADRQELQDEL 647
Cdd:PHA02562  231 TIKAEIEELTDELLNLVMDIE-DPSAALNKLNTAAAKIKSKIEQFQKVI 278
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 546-601 7.99e-03

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


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 35.72  E-value: 7.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754287 546 QQLQMEVEMLSSSKamKELTEEQQNLQKELESLQNEHaqrmEEFYIEQRDLEKKLE 601
Cdd:COG3074    21 ELLQMEVEELKEKN--EELEQENEELQSENEELQSEN----EQLKTENAEWQERIR 70
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 534-677 8.55e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 8.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  534 QQEKLSSILQKK---QQLQ-MEVEMLSSSKAMKELTEEQQNLQKELESLQNEHAQrmeefyieqrdLEKKLEQVMKQKCT 609
Cdd:pfam01576  397 QQAKQDSEHKRKkleGQLQeLQARLSESERQRAELAEKLSKLQSELESVSSLLNE-----------AEGKNIKLSKDVSS 465

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287  610 CDSNVEKDKE--AEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIVKSSKTAKE 677
Cdd:pfam01576  466 LESQLQDTQEllQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 522-667 9.42e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 38.86  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 522 KIVEDVMRTyvRQQEKLSSILQKKQQLQMEVEMLSSSKA-MKELTEEQQNLQKELESLQNEHAQRMEEFYIEQRDLEKKL 600
Cdd:pfam15558   8 KIAALMLAR--HKEEQRMRELQQQAALAWEELRRRDQKRqETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 601 EQVMKQKCTCDSNVEKDKEA------EYAAQLAELR-----QRLDHAEADRQELQDE---LRQEREARQKLEMMIKELKL 666
Cdd:pfam15558  86 EKQVIEKESRWREQAEDQENqrqeklERARQEAEQRkqcqeQRLKEKEEELQALREQnslQLQERLEEACHKRQLKEREE 165


                  .
gi 1958754287 667 Q 667
Cdd:pfam15558 166 Q 166
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 535-672 9.92e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.59  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 535 QEKLSSILQKKQQL-------------------QMEVEMLSSSKAMkeLTEEQQNLQKELESLQNEhAQRMEEFYIEQ-R 594
Cdd:pfam09787  13 KQKAARILQSKEKLiaslkegsgvegldsstalTLELEELRQERDL--LREEIQKLRGQIQQLRTE-LQELEAQQQEEaE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754287 595 DLEKKLEQVMKQKCTcdsnvEKDKEAEYAAQLAELRQRLDHAEadrqelqDELRQEREARQ----KLEMMIKELKLQIVK 670
Cdd:pfam09787  90 SSREQLQELEEQLAT-----ERSARREAEAELERLQEELRYLE-------EELRRSKATLQsrikDREAEIEKLRNQLTS 157


                  ..
gi 1958754287 671 SS 672
Cdd:pfam09787 158 KS 159
 
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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