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Conserved domains on  [gi|669266302|ref|XP_008642677|]
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PREDICTED: ski-like protein [Corvus brachyrhynchos]

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 ...
 140-239 3.07e-67

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


:

Pssm-ID: 410787  Cd Length: 100  Bit Score: 215.60  E-value: 3.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 140 PPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 219
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 669266302 220 SCGLITLTDAQRLCNALLRP 239
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 ...
 264-359 3.54e-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: 198114  Cd Length: 95  Bit Score: 183.34  E-value: 3.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   264 AFEVEHECLGKCQGLFAPQFYLAPDDPCIQCLECYGMFSPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHINQKYlGTSE 343
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 669266302   344 ERELKHLLEEMKEKFS 359
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
548-681 1.71e-09

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKeleclQAEHAQRMEEFYFEQRD---LEKKLDQVMKQKcscd 624
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAE--ERLEALEAELDALQE-----RREALQRLAEYSWDEIDvasAEREIAELEAEL---- 677

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302  625 SNLEKDKeaeyaAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG4913   678 ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
PTZ00121 super family cl31754
MAEBL; Provisional
 419-672 1.55e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  419 ASQYKDVAKATVKASEVNKSSpgqsEKKLSSGKHKKAASYPELSLEEQEKIDLKTGVEQPHKRLDPPVSTRSARGGKSER 498
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  499 VSSKTTRDSGRGEggADARTLSPTLMKdiSCEDDKGRIME----EVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAM 574
Cdd:PTZ00121 1374 EEAKKKADAAKKK--AEEKKKADEAKK--KAEEDKKKADElkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  575 KELTEEQ---QNLQKELE-CLQAEHAQRMEEFYFEQRDLEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAE 650
Cdd:PTZ00121 1450 KKKAEEAkkaEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                         250       260
                  ....*....|....*....|..
gi 669266302  651 ADRQELQDELRQEREAREKLEL 672
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADEL 1551
 
Name Accession Description Interval E-value
DHD_Sno cd21084
Dachshund-homology domain found in Ski-like protein (Sno) and similar proteins; Ski-like ...
 140-239 3.07e-67

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 215.60  E-value: 3.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 140 PPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 219
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 669266302 220 SCGLITLTDAQRLCNALLRP 239
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 ...
 264-359 3.54e-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: 198114  Cd Length: 95  Bit Score: 183.34  E-value: 3.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   264 AFEVEHECLGKCQGLFAPQFYLAPDDPCIQCLECYGMFSPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHINQKYlGTSE 343
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 669266302   344 ERELKHLLEEMKEKFS 359
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 ...
 264-358 1.93e-52

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: 175.92  E-value: 1.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  264 AFEVEHECLGKCQGLFAPQFYLAPDDPCIQCLECYGMFSPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHINQkYLGTSE 343
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 669266302  344 ERELKHLLEEMKEKF 358
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. ...
 139-238 3.59e-49

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: 167.07  E-value: 3.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  139 IPPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 218
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 669266302  219 PSCGLITLTDAQRLCNALLR 238
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
548-681 1.71e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKeleclQAEHAQRMEEFYFEQRD---LEKKLDQVMKQKcscd 624
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAE--ERLEALEAELDALQE-----RREALQRLAEYSWDEIDvasAEREIAELEAEL---- 677

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302  625 SNLEKDKeaeyaAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG4913   678 ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
530-678 8.18e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 8.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 530 EDDKGRIMEE-------VMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEF 602
Cdd:PRK03918 447 EEHRKELLEEytaelkrIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302 603 YfeqRDLEKKLDQVMKQKCSCDSNLEKDKEAEyaAQLAELRQRLDHAEADRQELQDELRQER-EAREKLELMIKELK 678
Cdd:PRK03918 527 Y---EKLKEKLIKLKGEIKSLKKELEKLEELK--KKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 546-681 1.60e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   546 KQQEKLNTILRRKQQLQMEVEMLSNSKamKELTEEQQNLQKELECLQAEhaqrmeefyfeQRDLEKKLDQVMKQKCSCDS 625
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEEL-----------IEELESELEALLNERASLEE 887

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 669266302   626 NLEKDKEAEY--AAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:TIGR02168  888 ALALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 522-678 3.08e-07

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: 52.58  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 522 TLMKDISCEDDKGRIMEEVMKTYIKQQEKL-NTILRRKQQL-QMEVEMlsnsKAMKELTEEQQNLQKELECLQAEHAQRM 599
Cdd:cd16269  153 KLVEKYRQVPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKL 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302 600 EEfyfEQRDLEKKLDQvmkqkcscdsnLEKDKEAEYAAQLAELRQRLDHAEADRQELQDElrQEREAREKLELMIKELK 678
Cdd:cd16269  229 ED---QERSYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 548-684 1.64e-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: 51.39  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQL--QMEVEMLSNS---KAMKELTEEQQNLQKELECLQAEHAQRMEEFYF------EQRDLEKKLDQV 616
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAKKyveKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLneneleRVRGLEKQLEEL 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302  617 MKQKCSCDSNLEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELR----QEREAREKLELMIKEL---KLQILKS 684
Cdd:pfam06160 342 EKRYDEIVERLEEKEVAysELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVEKS 418
PTZ00121 PTZ00121
MAEBL; Provisional
 419-686 1.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  419 ASQYKDVAKATVKASEVNKSSPGQSEKKLSSGKHKKAASYPELSLEEQEKIDLKTGVEQPHKrldppvstrsarggkSER 498
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK---------------ADE 1395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  499 VSSKTTRDSGRGE---GGADARTLSPTLMKdiscEDDKGRIMEEVMKtyiKQQEKlntilRRKQQLQMEVEMLSNSKAMK 575
Cdd:PTZ00121 1396 AKKKAEEDKKKADelkKAAAAKKKADEAKK----KAEEKKKADEAKK---KAEEA-----KKADEAKKKAEEAKKAEEAK 1463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  576 ELTEEQQNLQKELEclQAEHAQRMEEFYFEQRDLEKKLDQvMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAEADRQE 655
Cdd:PTZ00121 1464 KKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540

                         250       260       270
                  ....*....|....*....|....*....|.
gi 669266302  656 LQDELRQEREAREKLELMIKELKLQILKSSK 686
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
PTZ00121 PTZ00121
MAEBL; Provisional
 419-672 1.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  419 ASQYKDVAKATVKASEVNKSSpgqsEKKLSSGKHKKAASYPELSLEEQEKIDLKTGVEQPHKRLDPPVSTRSARGGKSER 498
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  499 VSSKTTRDSGRGEggADARTLSPTLMKdiSCEDDKGRIME----EVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAM 574
Cdd:PTZ00121 1374 EEAKKKADAAKKK--AEEKKKADEAKK--KAEEDKKKADElkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  575 KELTEEQ---QNLQKELE-CLQAEHAQRMEEFYFEQRDLEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAE 650
Cdd:PTZ00121 1450 KKKAEEAkkaEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                         250       260
                  ....*....|....*....|..
gi 669266302  651 ADRQELQDELRQEREAREKLEL 672
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADEL 1551
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 566-676 3.50e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   566 EMLSNSKAMKELTEEQQNLQKELECLQAEhaqrmeefyfeqrdLEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAELRQr 645
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 669266302   646 ldhaeaDRQELQDELRQER-EAREKLELMIKE 676
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 ...
 140-239 3.07e-67

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


Pssm-ID: 410787  Cd Length: 100  Bit Score: 215.60  E-value: 3.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 140 PPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 219
Cdd:cd21084    1 PSDSSTELTQTVLEGESISCFMVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 80

                         90       100
                 ....*....|....*....|
gi 669266302 220 SCGLITLTDAQRLCNALLRP 239
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 ...
 264-359 3.54e-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: 198114  Cd Length: 95  Bit Score: 183.34  E-value: 3.54e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   264 AFEVEHECLGKCQGLFAPQFYLAPDDPCIQCLECYGMFSPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHINQKYlGTSE 343
Cdd:smart01046   1 SFRVYHECFGKCQGLFVPELYSSPDAPCIQCLECRGMFSPQKFVMHSHRSPEKRTCHWGFDSANWRSYLHVAKDY-GTEE 79

                           90
                   ....*....|....*.
gi 669266302   344 ERELKHLLEEMKEKFS 359
Cdd:smart01046  80 REKLEQLLEEMKEKFN 95
DHD_Ski_Sno cd21079
Dachshund-homology domain found in Ski, Ski-like protein (Sno), and similar proteins; Ski may ...
 147-237 2.73e-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: 178.14  E-value: 2.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 147 LTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 226
Cdd:cd21079    1 LKETLLEGETIACFVVGGEKRLCLPQILNTVLRDFSLQQINRVCDDLHIYCSRCTPEQLETLKLAGILPPSAPSCGLITK 80

                         90
                 ....*....|.
gi 669266302 227 TDAQRLCNALL 237
Cdd:cd21079   81 TDAERLCSALL 91
c-SKI_SMAD_bind pfam08782
c-SKI Smad4 binding domain; c-SKI is an oncoprotein that inhibits TGF-beta signaling through ...
 264-358 1.93e-52

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: 175.92  E-value: 1.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  264 AFEVEHECLGKCQGLFAPQFYLAPDDPCIQCLECYGMFSPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHINQkYLGTSE 343
Cdd:pfam08782   1 SFEVYHECFGKCRGLFVPELYTSPRAACIQCLECRLMFSPQKFVFHSHRSPENRTCHWGFDSANWRAYLHLAR-YLDTPD 79

                          90
                  ....*....|....*
gi 669266302  344 ERELKHLLEEMKEKF 358
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. ...
 139-238 3.59e-49

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: 167.07  E-value: 3.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  139 IPPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNA 218
Cdd:pfam02437   1 TNTDTNNERMETMLEGEVISCFMVGGEERLCLPQILNTLLKDFSLTQINTVCDELIITCVRCTPEQLEILKLLGILPPSV 80

                          90       100
                  ....*....|....*....|
gi 669266302  219 PSCGLITLTDAQRLCNALLR 238
Cdd:pfam02437  81 RRCGLITKTDAERLCDALLH 100
DHD_Ski cd21083
Dachshund-homology domain found in Ski and similar proteins; Ski may play a role in terminal ...
 140-237 5.98e-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: 166.78  E-value: 5.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 140 PPDSSTELTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAP 219
Cdd:cd21083    3 PSDRSTERCETILEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAP 82

                         90
                 ....*....|....*...
gi 669266302 220 SCGLITLTDAQRLCNALL 237
Cdd:cd21083   83 SCGLITKTDAERLCNALL 100
DHD_Ski_Sno_Dac cd21074
Dachshund-homology domain found in the Ski/Sno/Dac family of transcriptional regulators; The ...
 147-234 2.14e-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: 125.87  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 147 LTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 226
Cdd:cd21074    1 LVTSTLEGKRIAGFEIDGEERLCLPQILNLVLKDFVQTQIHNRCTKLKIICTRCDQEQLKILKRLGILPPKAKSCGLISK 80


                 ....*...
gi 669266302 227 TDAQRLCN 234
Cdd:cd21074   81 SDAERLLN 88
DHD_Skor cd21080
Dachshund-homology domain found in SKI family transcriptional corepressors, Skor1, Skor2 and ...
 147-237 5.93e-17

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: 76.33  E-value: 5.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 147 LTQTLLEGESISCFKVGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITL 226
Cdd:cd21080    1 VGTVILYGVPIVSLVIDGQERLCLAQISNTLLKDYSYNEIHNRRVALGITCVQCTPVQLEILRRAGAMPISSRRCGMITK 80

                         90
                 ....*....|.
gi 669266302 227 TDAQRLCNALL 237
Cdd:cd21080   81 REAERLCKSFL 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
548-681 1.71e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKeleclQAEHAQRMEEFYFEQRD---LEKKLDQVMKQKcscd 624
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAE--ERLEALEAELDALQE-----RREALQRLAEYSWDEIDvasAEREIAELEAEL---- 677

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302  625 SNLEKDKeaeyaAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG4913   678 ERLDASS-----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
530-678 8.18e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 8.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 530 EDDKGRIMEE-------VMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEF 602
Cdd:PRK03918 447 EEHRKELLEEytaelkrIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE 526

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302 603 YfeqRDLEKKLDQVMKQKCSCDSNLEKDKEAEyaAQLAELRQRLDHAEADRQELQDELRQER-EAREKLELMIKELK 678
Cdd:PRK03918 527 Y---EKLKEKLIKLKGEIKSLKKELEKLEELK--KKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELE 598
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 546-681 1.60e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   546 KQQEKLNTILRRKQQLQMEVEMLSNSKamKELTEEQQNLQKELECLQAEhaqrmeefyfeQRDLEKKLDQVMKQKCSCDS 625
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEEL-----------IEELESELEALLNERASLEE 887

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 669266302   626 NLEKDKEAEY--AAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:TIGR02168  888 ALALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 522-678 3.08e-07

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: 52.58  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 522 TLMKDISCEDDKGRIMEEVMKTYIKQQEKL-NTILRRKQQL-QMEVEMlsnsKAMKELTEEQQNLQKELECLQAEHAQRM 599
Cdd:cd16269  153 KLVEKYRQVPRKGVKAEEVLQEFLQSKEAEaEAILQADQALtEKEKEI----EAERAKAEAAEQERKLLEEQQRELEQKL 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302 600 EEfyfEQRDLEKKLDQvmkqkcscdsnLEKDKEAEYAAQLAELRQRLDHAEADRQELQDElrQEREAREKLELMIKELK 678
Cdd:cd16269  229 ED---QERSYEEHLRQ-----------LKEKMEEERENLLKEQERALESKLKEQEALLEE--GFKEQAELLQEEIRSLK 291
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 537-681 5.34e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 5.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   537 MEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKELECLQAEHA---QRMEEFYFEQRDLEKKL 613
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302   614 DQVMKQKCSCDSNLEKDKE---------AEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEelaeleeklEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
546-680 1.18e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 546 KQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQA---EHAQRMEEFYFEQRDLEK------KLDQV 616
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErleELEERLEELRELEEELEEleaelaELQEE 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669266302 617 MKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQ 680
Cdd:COG4717  179 LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 548-684 1.36e-06

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 51.38  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 548 QEKLNTILRRKQQL--QMEVEMlsnsKAMKELTEEQQNLQKELECLQAEHAQRMEEF------YF-------EQRDLEKK 612
Cdd:PRK04778 281 EEKNEEIQERIDQLydILEREV----KARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsYTlneseleSVRQLEKQ 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 613 LDQVMKQKCSCDSNLEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELRQ----EREAREKLELMIKEL---KLQILK 683
Cdd:PRK04778 357 LESLEKQYDEITERIAEQEIAysELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdELEAREKLERYRNKLheiKRYLEK 436


                 .
gi 669266302 684 S 684
Cdd:PRK04778 437 S 437
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 548-684 1.64e-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: 51.39  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQL--QMEVEMLSNS---KAMKELTEEQQNLQKELECLQAEHAQRMEEFYF------EQRDLEKKLDQV 616
Cdd:pfam06160 262 EEALEEIEERIDQLydLLEKEVDAKKyveKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLneneleRVRGLEKQLEEL 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302  617 MKQKCSCDSNLEKDKEA--EYAAQLAELRQRLDHAEADRQELQDELR----QEREAREKLELMIKEL---KLQILKS 684
Cdd:pfam06160 342 EKRYDEIVERLEEKEVAysELQEELEEILEQLEEIEEEQEEFKESLQslrkDELEAREKLDEFKLELreiKRLVEKS 418
DHD_SKIDA1 cd21082
Dachshund-homology domain found in SKI/DACH domain-containing protein 1 (SKIDA1) and similar ...
 162-234 2.78e-06

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


Pssm-ID: 410785  Cd Length: 91  Bit Score: 45.80  E-value: 2.78e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302 162 VGGEKRLCLPQVLNSVLRDFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCN 234
Cdd:cd21082   16 INGKQMFALSQVFTDLLPNTPRTTVHKRMDRLKVKKHHCDLEELRKLKALNGIAFHAAKCTLISREDVERLYS 88
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 542-683 4.45e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 542 KTYIKQQEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNL--QKELECLQAE--HAQRmeefyfEQRDLEKKLDQVM 617
Cdd:COG1579   45 ARLEAAKTELEDLEKEIKRLELEIEEVE--ARIKKYEEQLGNVrnNKEYEALQKEieSLKR------RISDLEDEILELM 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 669266302 618 KQKcscdSNLEKDKEAEyAAQLAELRQRLDHAEADRQELQDELRQEREA-REKLELMIKELKLQILK 683
Cdd:COG1579  117 ERI----EELEEELAEL-EAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKIPPELLA 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
553-671 7.86e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  553 TILRRKQQLQmevEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEfyfeQRDLEKKLDQVMKQKCSCDSNLEKDKE 632
Cdd:COG4913   669 EIAELEAELE---RLDASSDDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAED 741

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 669266302  633 AEYAAQLAELRQRLDHAEAD------RQELQDELRQEREAREKLE 671
Cdd:COG4913   742 LARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAE 786
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 542-686 8.98e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  542 KTYIKQQEKlntilrRKQQLQMEVEmlSNSKAMKELTEEQQNLQKELECLQAEHAQRmeefyfeQRDLEKKLDQVMKQKC 621
Cdd:TIGR04523 313 KSELKNQEK------KLEEIQNQIS--QNNKIISQLNEQISQLKKELTNSESENSEK-------QRELEEKQNEIEKLKK 377

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302  622 SCDSNLEKDKEAEyaAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQILKSSK 686
Cdd:TIGR04523 378 ENQSYKQEIKNLE--SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
547-687 1.23e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  547 QQEKLNTILRRKQQLQMEVEmlSNSKAMKELTEEQQNLQKELECLQAEHAQ----RMEEFYFEQRDLEKKLDQVMKQKCS 622
Cdd:COG4913   286 AQRRLELLEAELEELRAELA--RLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRAR 363

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302  623 CDSNLEK------DKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELK--LQILKSSKN 687
Cdd:COG4913   364 LEALLAAlglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeIASLERRKS 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 530-684 1.35e-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: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   530 EDDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEmlsnsKAMKELTEEQQNLQKELECLQaehaQRMEEFYFEQRDL 609
Cdd:TIGR02169  782 NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE-----QKLNRLTLEKEYLEKEIQELQ----EQRIDLKEQIKSI 852

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302   610 EKKLDQVMKQKCSCDSNLEK--DKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKEL--KLQILKS 684
Cdd:TIGR02169  853 EKEIENLNGKKEELEEELEEleAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkaKLEALEE 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 572-681 1.52e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 572 KAMKELTEEQQNLQ-------------KELEcLQAEHAQRmeefYFEQRDLEKKLDQVMKqkcscdsnLEKDKEAEyaAQ 638
Cdd:COG1196  176 EAERKLEATEENLErledilgelerqlEPLE-RQAEKAER----YRELKEELKELEAELL--------LLKLRELE--AE 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 669266302 639 LAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 530-678 2.37e-05

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: 45.81  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  530 EDDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKE--LTE---EQQNLQKELECLQAEHAQRMEEFYF 604
Cdd:pfam15665  24 EEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRqaLTEfeqYKRRVEERELKAEAEHRQRVVELSR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  605 EQRDLEKKLDQVMKQKCSCDSNLEKDKE-------AEYAAQLAELRQRLD--HAE--ADRQELQDELRQEREA-REKLEL 672
Cdd:pfam15665 104 EVEEAKRAFEEKLESFEQLQAQFEQEKRkaleelrAKHRQEIQELLTTQRaqSASslAEQEKLEELHKAELESlRKEVED 183


                  ....*.
gi 669266302  673 MIKELK 678
Cdd:pfam15665 184 LRKEKK 189
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 546-687 2.46e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 546 KQQEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKELECLQAEHAQRMEEFY-----------FEQRDLEKK-- 612
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALE--AELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplallLSPEDFLDAvr 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302 613 ----LDQVMKQKcscdsnleKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQILKSSKN 687
Cdd:COG4942  137 rlqyLKYLAPAR--------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 565-676 2.74e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 47.38  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 565 VEMLSNSKAMKELTEEQQNLQKELECLQAE----HAQRMEEFYFEQRDLEKKLDQVMKQKcscdsnlekDKEAEYAAQLA 640
Cdd:COG0542  404 MEIDSKPEELDELERRLEQLEIEKEALKKEqdeaSFERLAELRDELAELEEELEALKARW---------EAEKELIEEIQ 474

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 669266302 641 ELRQRLDHAEADRQELQDELRQEREAREKLELMIKE 676
Cdd:COG0542  475 ELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-682 2.89e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 538 EEVMKTYIKQQEKLNTILRRKQQLQMEVEmlsnsKAMKELTEEQQNLQKELECLQAEHAQRMEEfyfeQRDLEKKLDQVM 617
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELE-----LELEEAQAEEYELLAELARLEQDIARLEER----RRELEERLEELE 322

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302 618 KQKcscdsNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQIL 682
Cdd:COG1196  323 EEL-----AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
mukB PRK04863
chromosome partition protein MukB;
579-681 3.02e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.64  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  579 EEQQNLQKELECLQAEHAqRMEEFYFEQRDLEKKLDQVMKQkcscdSNLEKDKEAEYAAQLAELRQRLDHaeadrqeLQD 658
Cdd:PRK04863  506 REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKR-----LGKNLDDEDELEQLQEELEARLES-------LSE 572

                          90       100
                  ....*....|....*....|...
gi 669266302  659 ELRQEREAREKLELMIKELKLQI 681
Cdd:PRK04863  573 SVSEARERRMALRQQLEQLQARI 595
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
454-678 3.63e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.16  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 454 KAASY-PELSLEEQEKIDL--KTGVEQPHKR--LDPPVSTRSARGGKSERVSSKTTRDSGRGEGGADA---RTLSPTLMK 525
Cdd:COG2433  305 NAVLYtPKEDLSVEEKLHLarEYGYDNDHERdaLAAALKAYDAYKNKFERVEKKVPPDVDRDEVKARVirgLSIEEALEE 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 526 DIscEDDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEmlsnskamkELTEEQQNLQKELEclqaEHAQRMEEfyfe 605
Cdd:COG2433  385 LI--EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELE----EKDERIER---- 445

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302 606 qrdLEKKLDQVMKQKcscDSNLEKDKEAeyaaqlaelrQRLDhAEADRqeLQDELRQEREAREKLELMIKELK 678
Cdd:COG2433  446 ---LERELSEARSEE---RREIRKDREI----------SRLD-REIER--LERELEEERERIEELKRKLERLK 499
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 535-671 3.93e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 535 RIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMlsNSKAMKELTEEQQNLQKELEclqaehaQRMEEFYFEQRDLEKKLD 614
Cdd:PRK00409 502 NIIEEAKKLIGEDKEKLNELIASLEELERELEQ--KAEEAEALLKEAEKLKEELE-------EKKEKLQEEEDKLLEEAE 572

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302 615 QVMKQKcscdsnLEKDKEaEYAAQLAELR--QRLDHAEADRQELQDELRQEREAREKLE 671
Cdd:PRK00409 573 KEAQQA------IKEAKK-EADEIIKELRqlQKGGYASVKAHELIEARKRLNKANEKKE 624
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 565-671 5.98e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 565 VEMLSN-SKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRDLEKKLDQVMKQKcscdsnlekdkeAEYAAQLAELR 643
Cdd:COG3883  121 LSALSKiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ------------AEQEALLAQLS 188

                         90       100
                 ....*....|....*....|....*...
gi 669266302 644 QRLDHAEADRQELQDELRQEREAREKLE 671
Cdd:COG3883  189 AEEAAAEAQLAELEAELAAAEAAAAAAA 216
DUF4201 pfam13870
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ...
 554-680 7.59e-05

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


Pssm-ID: 464008 [Multi-domain]  Cd Length: 177  Bit Score: 43.75  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  554 ILRRKQQLQMeveMLSNSKAMKELTEeqqNLQK-ELECLQAEHAQRMEEFyfEQRDLEKKldqVMKQKCSCDS---NLEK 629
Cdd:pfam13870  15 LITLKHTLAK---IQEKLEQKEELGE---GLTMiDFLQLQIENQALNEKI--EERNKELK---RLKLKVTNTVhalTHLK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 669266302  630 DKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQ 680
Cdd:pfam13870  84 EKLHFLSAELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQNKKLRQQ 134
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
548-690 9.22e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 9.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 548 QEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQA----EH--AQRMEEfyfEQRDLEKKLDQVMKQ-K 620
Cdd:COG3206  239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpNHpdVIALRA---QIAALRAQLQQEAQRiL 315

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302 621 CSCDSNLE--KDKEAEYAAQLAELRQRLDHAEADRQELQdELRQERE-AREKLELMIKelKLQILKSSKNGKG 690
Cdd:COG3206  316 ASLEAELEalQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEvARELYESLLQ--RLEEARLAEALTV 385
mukB PRK04863
chromosome partition protein MukB;
548-685 1.14e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  548 QEKLNTILRRKQQLQMEVEMLSN----SKAMKELTEEQQNLQKELECLQAEHAQRMEEF---YFEQRDLEKKLDQVMKQk 620
Cdd:PRK04863  519 RMRLSELEQRLRQQQRAERLLAEfckrLGKNLDDEDELEQLQEELEARLESLSESVSEArerRMALRQQLEQLQARIQR- 597

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669266302  621 cscdsnLEKDKEAEYAAQ--LAELRQRLDHAEADRQEL----QDELRQEREA---REKLELMIKELKLQILKSS 685
Cdd:PRK04863  598 ------LAARAPAWLAAQdaLARLREQSGEEFEDSQDVteymQQLLERERELtveRDELAARKQALDEEIERLS 665
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 530-681 1.25e-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: 44.91  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  530 EDDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEV-EMLSNSKAMKELtEEQQNLQKELECL--QAEHAQRMEEFYFEQ 606
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdEFNEEQAEWKEL-EKEEEREEDERILeyLKEKAEREEEREAER 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302  607 RDLEKKLDQVMKQKCScdsnlEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:pfam13868 176 EEIEEEKEREIARLRA-----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 556-678 1.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 556 RRKQQLQME---VEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEfyfeQRDLEKKLDQVMKQKCSCDSNLEKDKE 632
Cdd:COG1196  213 ERYRELKEElkeLEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQA 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 669266302 633 AEYA--AQLAELRQRLDHAEADRQELQ---DELRQER-EAREKLELMIKELK 678
Cdd:COG1196  289 EEYEllAELARLEQDIARLEERRRELEerlEELEEELaELEEELEELEEELE 340
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 530-678 1.40e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   530 EDDKGRIMEEVMKtyiKQQEKLNTILRRKQQLQMEVEMLSNSKA-----MKELTEEQQNLQKELECLQAEHaqrmeefyf 604
Cdd:TIGR02169  271 EQLLEELNKKIKD---LGEEEQLRVKEKIGELEAEIASLERSIAekereLEDAEERLAKLEAEIDKLLAEI--------- 338

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669266302   605 eqRDLEKKLDQVMKQKCSCDSNLEKDKEaeyaaQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELK 678
Cdd:TIGR02169  339 --EELEREIEEERKRRDKLTEEYAELKE-----ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
PRK11637 PRK11637
AmiB activator; Provisional
 560-668 1.51e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.68  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 560 QLQMEVEMLSNSKAMKElteEQQNLQKELECLQAEHAQRMEefyfeQRDLEKKldqvmKQKCSCDSNLEKDKeaeyaAQL 639
Cdd:PRK11637 174 ELKQTREELAAQKAELE---EKQSQQKTLLYEQQAQQQKLE-----QARNERK-----KTLTGLESSLQKDQ-----QQL 235

                         90       100       110
                 ....*....|....*....|....*....|..
gi 669266302 640 AELRQ---RLDHAEAdRQELQDELRQEREARE 668
Cdd:PRK11637 236 SELRAnesRLRDSIA-RAEREAKARAEREARE 266
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 538-687 1.69e-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: 45.01  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  538 EEVMKTYIKQQEKLNTILRRKQQlqmevEMLSNSKAMKELTEEQQNLQKELECLQAEHAQR-MEEFYFEQRDLEKKLDQV 616
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQK-----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEEI 326

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302  617 MKQKCSCDSNLEKDKEaeyaaQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI--LKSSKN 687
Cdd:TIGR04523 327 QNQISQNNKIISQLNE-----QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIknLESQIN 394
DHD_Dac cd21081
Dachshund-homology domain found in the retinal determination protein Dachshund and similar ...
 154-232 2.26e-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: 40.81  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 154 GESISCFKVGGEKRLCLPQVLNSVLRDF--SLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQR 231
Cdd:cd21081   10 GAKVAAFTVDGEELICLPQAFELFLKHLvgGLHTVYTKLKRLDITPVVCNVEQVRILRGLGAIQPGVNRCKLISRKDFDT 89


                 .
gi 669266302 232 L 232
Cdd:cd21081   90 L 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 531-681 2.37e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 531 DDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKELECLQAEHAQRMEEFY------- 603
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--AEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvs 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 604 -----FEQRDLE-----------------KKLDQVMKQKcscdSNLEKDKeAEYAAQLAELRQRLDHAEADRQELQDELR 661
Cdd:COG3883  104 yldvlLGSESFSdfldrlsalskiadadaDLLEELKADK----AELEAKK-AELEAKLAELEALKAELEAAKAELEAQQA 178

                        170       180
                 ....*....|....*....|
gi 669266302 662 QEREAREKLELMIKELKLQI 681
Cdd:COG3883  179 EQEALLAQLSAEEAAAEAQL 198
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 534-671 2.46e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 534 GRIMEEVM-------KTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQ 606
Cdd:PRK09510  47 GSVIDAVMvdpgavvEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302 607 RDLEKKLDQVMKQKCSCDSNLEKDKE----AEYAAQLAELRQRLDHAEADRQelqdelrQEREAREKLE 671
Cdd:PRK09510 127 AALKQKQAEEAAAKAAAAAKAKAEAEakraAAAAKKAAAEAKKKAEAEAAKK-------AAAEAKKKAE 188
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 460-691 3.25e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   460 ELSLEEQEKIDLKTGVEQPHKRLDPPVSTRSARGGKSERVSSKTTRDSGRGEGGAD--------ARTLSPTLMKDISCED 531
Cdd:pfam01576  388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvssllneAEGKNIKLSKDVSSLE 467

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   532 DKGRIMEEVMKTYIKQQEKLNTILRrkqqlQMEVEMLSNSKAMKELTEEQQNLQKELECLQA---EHAQRMEEFYFE--- 605
Cdd:pfam01576  468 SQLQDTQELLQEETRQKLNLSTRLR-----QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAqlsDMKKKLEEDAGTlea 542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   606 --------QRDLEKKLDQVMKQKCSCD---------------------------SNLEKDK---------EAEYAAQLAE 641
Cdd:pfam01576  543 leegkkrlQRELEALTQQLEEKAAAYDklektknrlqqelddllvdldhqrqlvSNLEKKQkkfdqmlaeEKAISARYAE 622

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302   642 LRqrlDHAEADRQE-------LQDELRQEREAREKLELMIKELKLQI--LKSSKNGKGK 691
Cdd:pfam01576  623 ER---DRAEAEAREketralsLARALEEALEAKEELERTNKQLRAEMedLVSSKDDVGK 678
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 541-681 4.14e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 541 MKTYIKQQEKLNTILRRKQQLQmevemlsnsKAMKELTEEQQNLQKELECLQAEHA---QRMEEFYFEQRDLEKKLDQVm 617
Cdd:COG1579    2 MPEDLRALLDLQELDSELDRLE---------HRLKELPAELAELEDELAALEARLEaakTELEDLEKEIKRLELEIEEV- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 669266302 618 kqkcscDSNLEKDKEA--------EYAAQLAElrqrLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG1579   72 ------EARIKKYEEQlgnvrnnkEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 578-689 4.19e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 578 TEEQQNLQKELECLQAEHAQrmeefyfeqrdLEKKLDQVMKQKcscDSNLEKDKEAEyaAQLAELRQRLDHAEADRQELQ 657
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAE-----------LEKELAALKKEE---KALLKQLAALE--RRIAALARRIRALEQELAALE 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 669266302 658 DELR----QEREAREKLELMIKELKLQILKSSKNGK 689
Cdd:COG4942   83 AELAelekEIAELRAELEAQKEELAELLRALYRLGR 118
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
545-671 4.44e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 545 IKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEfYFEQRDLEKKLDQVMKQKcscD 624
Cdd:COG2268  216 IAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAE-ANAEREVQRQLEIAERER---E 291

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 669266302 625 SNL-EKDKEAEYAAQLAELRQRldhAEADRQELQDELRQEREA-REKLE 671
Cdd:COG2268  292 IELqEKEAEREEAELEADVRKP---AEAEKQAAEAEAEAEAEAiRAKGL 337
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 530-683 5.70e-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: 42.60  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  530 EDDKGRIMEEV-MKTYIKQQEKLNtilRRKQQLQMEVEMlsnsKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRD 608
Cdd:pfam13868 196 AQDEKAERDELrAKLYQEEQERKE---RQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLR 268

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302  609 LEKKLDQVMKQKcscDSNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQILK 683
Cdd:pfam13868 269 KQAEDEEIEQEE---AEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 554-671 6.03e-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: 43.40  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  554 ILRRKQQLQMEVEMLSNSKAmkELTEEQQNL--QKELECLQAEHAQRMEEFYFEQRDLEKKLDQVMKQKCSCDsnlekDK 631
Cdd:COG3096   500 LLRRYRSQQALAQRLQQLRA--QLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE-----EQ 572

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 669266302  632 EAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLE 671
Cdd:COG3096   573 AAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
523-678 6.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 523 LMKDISCEDDKGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLS-NSKAMKELTEEQQNLQKELECLQAEHA----- 596
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkEVKELEELKEEIEELEKELESLEGSKRkleek 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 597 -----QRMEEFYFEQRDLEKKLDQV--MKQKCSCDSNLEKDKEaEYAAQLAELRQRLDHAEADRQELQDELRQEREAREK 669
Cdd:PRK03918 261 ireleERIEELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339


                 ....*....
gi 669266302 670 LELMIKELK 678
Cdd:PRK03918 340 LEELKKKLK 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 513-681 7.14e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 7.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   513 GADARTLSPTLMKDISCEDDKGRImEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSnsKAMKELTEEQQNLQKELECLQ 592
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLR--KELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   593 AEHAQRMEEFYFEQRDLEKKLDQVMKQKCSCDSNLEKDKEAEyaAQLAELRQRLDHAEADRQ-------ELQDELRQERE 665
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKalrealdELRAELTLLNE 817

                          170
                   ....*....|....*.
gi 669266302   666 AREKLELMIKELKLQI 681
Cdd:TIGR02168  818 EAANLRERLESLERRI 833
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
533-684 8.10e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 8.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 533 KGRIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLsnskamKELTEEQQNLQKELECLQA-----EHAQRMEEFYFEQR 607
Cdd:COG4717   62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL------EELEEELEELEAELEELREeleklEKLLQLLPLYQELE 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 608 DLEKKLdqvmkqkcscdsnlekdkeAEYAAQLAELRQRLD---HAEADRQELQDELRQEREAREKLELMIKELKLQILKS 684
Cdd:COG4717  136 ALEAEL-------------------AELPERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 546-677 8.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 546 KQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEfyfEQRDLEKKLDQVMKQKCSCDS 625
Cdd:COG1196  670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA---LEEQLEAEREELLEELLEEEE 746

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302 626 NLEKDKEAEYA--AQLAELRQRLDHAEADRQEL-----------------QDELRQER----EAREKLELMIKEL 677
Cdd:COG1196  747 LLEEEALEELPepPDLEELERELERLEREIEALgpvnllaieeyeeleerYDFLSEQRedleEARETLEEAIEEI 821
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
546-681 9.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  546 KQQEKLNTILRRKQQLQMEVEMLS---NSKAMKELTEEQQNLQKELECLQAEHAQrmeefyfeqrdLEKKLDQVmkqkcs 622
Cdd:COG4913   259 ELAERYAAARERLAELEYLRAALRlwfAQRRLELLEAELEELRAELARLEAELER-----------LEARLDAL------ 321

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  623 cdsnleKDKEAEYAAQLAEL-RQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG4913   322 ------REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 571-680 9.85e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 9.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 571 SKAMKELTEEQQNLQKELECLQAEHAQrmeefyfEQRDLEKKLDQVMKQKcscdSNLEKDKeAEYAAQLAELRQRLdhaE 650
Cdd:COG4942  145 APARREQAEELRADLAELAALRAELEA-------ERAELEALLAELEEER----AALEALK-AERQKLLARLEKEL---A 209

                         90       100       110
                 ....*....|....*....|....*....|
gi 669266302 651 ADRQELQDELRQEREAREKLELMIKELKLQ 680
Cdd:COG4942  210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
537-686 9.87e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 537 MEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNS-KAMKELTEEQQNLQKELECLQaEHAQRMEEFYFEQRDLEKKLDQ 615
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEERIKELEEKEERLEELK-KKLKELEKRLEELEERHELYEE 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 669266302 616 VMKQKcscdSNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI--LKSSK 686
Cdd:PRK03918 367 AKAKK----EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeeLKKAK 435
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 580-678 1.04e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  580 EQQNLQKELECLQAEHAQrMEEFYFEQRDLEKKLDQVMKQkcscdSNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDE 659
Cdd:COG3096   506 SQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEEFCQR-----IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579

                          90
                  ....*....|....*....
gi 669266302  660 LRQEREAREKLELMIKELK 678
Cdd:COG3096   580 RSELRQQLEQLRARIKELA 598
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 522-678 1.36e-03

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: 41.12  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  522 TLMKDISCEDDKGRIMEEVMKTYIKQQEKL-NTILRRKQQLqmeVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRME 600
Cdd:pfam02841 159 KLEAKYNQVPRKGVKAEEVLQEFLQSKEAVeEAILQTDQAL---TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMME 235

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669266302  601 EfyfEQRDLEKKLDQvMKQKcscdsnLEKDKEaeyaaQLAELRQRLdhAEADRQELQDELRQEREAR-EKLELMIKELK 678
Cdd:pfam02841 236 A---QERSYQEHVKQ-LIEK------MEAERE-----QLLAEQERM--LEHKLQEQEELLKEGFKTEaESLQKEIQDLK 297
PTZ00121 PTZ00121
MAEBL; Provisional
 419-686 1.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  419 ASQYKDVAKATVKASEVNKSSPGQSEKKLSSGKHKKAASYPELSLEEQEKIDLKTGVEQPHKrldppvstrsarggkSER 498
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK---------------ADE 1395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  499 VSSKTTRDSGRGE---GGADARTLSPTLMKdiscEDDKGRIMEEVMKtyiKQQEKlntilRRKQQLQMEVEMLSNSKAMK 575
Cdd:PTZ00121 1396 AKKKAEEDKKKADelkKAAAAKKKADEAKK----KAEEKKKADEAKK---KAEEA-----KKADEAKKKAEEAKKAEEAK 1463

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  576 ELTEEQQNLQKELEclQAEHAQRMEEFYFEQRDLEKKLDQvMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAEADRQE 655
Cdd:PTZ00121 1464 KKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540

                         250       260       270
                  ....*....|....*....|....*....|.
gi 669266302  656 LQDELRQEREAREKLELMIKELKLQILKSSK 686
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 572-663 1.42e-03

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: 40.20  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 572 KAMKELTEEQQNLQKELECLQAEHAQRMEEFyfeQRDlEKKLDQVMKQKcscdsnlekdKEAEYAAQLAELRQRLDHAEA 651
Cdd:COG2825   43 AAQKKLEKEFKKRQAELQKLEKELQALQEKL---QKE-AATLSEEERQK----------KERELQKKQQELQRKQQEAQQ 108

                         90
                 ....*....|..
gi 669266302 652 DRQELQDELRQE 663
Cdd:COG2825  109 DLQKRQQELLQP 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
523-682 1.49e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 523 LMKDISCEDDKG-RIMEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEe 601
Cdd:COG4717  375 LLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE- 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 602 fyfEQRDLEKKLDQvmkqkcscdsnLEKDKEaeyaaqLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:COG4717  454 ---ELAELEAELEQ-----------LEEDGE------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513


                 .
gi 669266302 682 L 682
Cdd:COG4717  514 L 514
PTZ00121 PTZ00121
MAEBL; Provisional
 419-672 1.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  419 ASQYKDVAKATVKASEVNKSSpgqsEKKLSSGKHKKAASYPELSLEEQEKIDLKTGVEQPHKRLDPPVSTRSARGGKSER 498
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  499 VSSKTTRDSGRGEggADARTLSPTLMKdiSCEDDKGRIME----EVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAM 574
Cdd:PTZ00121 1374 EEAKKKADAAKKK--AEEKKKADEAKK--KAEEDKKKADElkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  575 KELTEEQ---QNLQKELE-CLQAEHAQRMEEFYFEQRDLEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAE 650
Cdd:PTZ00121 1450 KKKAEEAkkaEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                         250       260
                  ....*....|....*....|..
gi 669266302  651 ADRQELQDELRQEREAREKLEL 672
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADEL 1551
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 544-681 1.58e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  544 YIKQQEKlnTILRRKQQ---LQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRDL----EKKLDQV 616
Cdd:pfam17380 276 HIVQHQK--AVSERQQQekfEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamerERELERI 353

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302  617 MKQKCScdSNLEKDKEAEYAAQLAELRQrLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:pfam17380 354 RQEERK--RELERIRQEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
555-678 1.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 555 LRRKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRDLEKKLDQVMKQkcsCDSNLEKDKEAE 634
Cdd:COG4717  346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ---LEELLGELEELL 422

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 669266302 635 YAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELK 678
Cdd:COG4717  423 EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
DUF2046 pfam09755
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ...
 506-672 1.77e-03

Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.


Pssm-ID: 401633 [Multi-domain]  Cd Length: 304  Bit Score: 40.97  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  506 DSGRGEGGADARTLSPT----LMKDISCEDDKGRIMEEVMKTY---IKQQEKLNTILRR-----KQQLQMEVEMLSNSka 573
Cdd:pfam09755   5 DTSSVDGGPTLAPPSPVtreqLQKRIESLQQENRVLKMELETYklrCKALQEENRALRQasvniQAKAEQEEEFISNT-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  574 mkeLTEEQQNLQKELECLqAEHAQRMEEFYfeQRDLEKKLDQVMKQKCSCDSNLEKDKEaeyaAQLAELRQRLDHAEADR 653
Cdd:pfam09755  83 ---LLKKIQALKKEKETL-AMNYEQEEEFL--TNDLSRKLTQLRQEKVELEQTLEQEQE----YQVNKLMRKIEKLEAET 152

                         170
                  ....*....|....*....
gi 669266302  654 QELQDELRQEReaREKLEL 672
Cdd:pfam09755 153 LNKQTNLEQLR--REKVEL 169
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 557-682 3.05e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.50  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  557 RKQQLQMEVEMLSNSKAMKELTEEQQNLQKELECLQAE------HAQRMEEFYFEQRDLEKKLdqvmkqkcscdSNLEKD 630
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQlenyekDKQSLKNLKARLKVLEKEL-----------KDLKWE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 669266302  631 KEaeyaaqlaELRQRLDHAEADRQELQDELRQE-REAREKLEL--MIKELKLQIL 682
Cdd:pfam13851 108 HE--------VLEQRFEKVERERDELYDKFEAAiQDVQQKTGLknLLLEKKLQAL 154
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 531-681 3.13e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   531 DDKGRIMEEVMKTYIKQQEKLNtilrrKQQLQMEVEMLSNSKAMKELTEEQQNLQK---ELECLQAEHAQRMEEFYFEQR 607
Cdd:pfam01576  130 EAKIKKLEEDILLLEDQNSKLS-----KERKLLEERISEFTSNLAEEEEKAKSLSKlknKHEAMISDLEERLKKEEKGRQ 204

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 669266302   608 DLEKkldqvMKQKCSCDSNLEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELKLQI 681
Cdd:pfam01576  205 ELEK-----AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQI 273
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 566-676 3.50e-03

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   566 EMLSNSKAMKELTEEQQNLQKELECLQAEhaqrmeefyfeqrdLEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAELRQr 645
Cdd:smart00935  12 ESPAGKAAQKQLEKEFKKRQAELEKLEKE--------------LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQR- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 669266302   646 ldhaeaDRQELQDELRQER-EAREKLELMIKE 676
Cdd:smart00935  77 ------KQQKLQQDLQKRQqEELQKILDKINK 102
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
574-684 4.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  574 MKELTEEQQNLQKELEclQAEHAQRMEEFYfeqRDLEKKLDQVMKQKcSCDSNLEKdkeaeYAAQ--LAELRQRLDHAEA 651
Cdd:COG4913   234 FDDLERAHEALEDARE--QIELLEPIRELA---ERYAAARERLAELE-YLRAALRL-----WFAQrrLELLEAELEELRA 302

                          90       100       110
                  ....*....|....*....|....*....|...
gi 669266302  652 DRQELQDELRQEREAREKLELMIKELKLQILKS 684
Cdd:COG4913   303 ELARLEAELERLEARLDALREELDELEAQIRGN 335
46 PHA02562
endonuclease subunit; Provisional
 521-631 5.68e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 521 PTLMKDISCEDDKGRIMEEVMKTYIKQQEKLNTilRRKQQLQMEVEMLSNSKAMKEL-----TEEQQ---------NLQK 586
Cdd:PHA02562 288 PTCTQQISEGPDRITKIKDKLKELQHSLEKLDT--AIDELEEIMDEFNEQSKKLLELknkisTNKQSlitlvdkakKVKA 365

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 669266302 587 ELECLQAEHAQRMEEFyfeqRDLEKKLDQVMKQKcscdSNLEKDK 631
Cdd:PHA02562 366 AIEELQAEFVDNAEEL----AKLQDELDKIVKTK----SELVKEK 402
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
528-678 6.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 528 SCEDDKGRI--MEEVMKTYIKQQEKLNTILRRKQQLQMEVEMLSNSKAMKELTE-EQQNLQKELECLQAEHAQrmEEFyf 604
Cdd:PRK03918 586 SVEELEERLkeLEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEkRLEELRKELEELEKKYSE--EEY-- 661

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 669266302 605 eqRDLEKKLdqvmkqkcscdsnLEKDKE-AEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLELMIKELK 678
Cdd:PRK03918 662 --EELREEY-------------LELSRElAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
582-680 6.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 582 QNLQKELECLQAEHAQRMEEFYFEQRDLEKKLDQvmkqkcscdsnlEKDKEAEYAA---QLAELRQRLDHAEADRQELQD 658
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKE------------AEEKEEEYAElqeELEELEEELEELEAELEELRE 116

                         90       100
                 ....*....|....*....|..
gi 669266302 659 ELRQEREAREKLELMIKELKLQ 680
Cdd:COG4717  117 ELEKLEKLLQLLPLYQELEALE 138
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
537-691 6.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 537 MEEVMKTYIKQQEKLNTILRRKQQLQMEV-----EMLSNSKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRDLE- 610
Cdd:COG4372   40 LDKLQEELEQLREELEQAREELEQLEEELeqarsELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEe 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 611 --KKLDQVMKQKCSCDSNLEKDKE--AEYAAQLAELRQRLDHAEADRQELQDELRQ--EREAREKLELMIKELKLQILKS 684
Cdd:COG4372  120 lqKERQDLEQQRKQLEAQIAELQSeiAEREEELKELEEQLESLQEELAALEQELQAlsEAEAEQALDELLKEANRNAEKE 199


                 ....*..
gi 669266302 685 SKNGKGK 691
Cdd:COG4372  200 EELAEAE 206
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 556-670 6.50e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 37.76  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302  556 RRKQQLQMEVEMLSnSKAMKELTEEQQNLQK-ELECLQAEH---AQRMEEFyFEQRDLEKKLDQVmkqkcscdsNLEKDK 631
Cdd:pfam07321  13 DRAEKAVKRQEQAL-AAARAAHQQAQASLQDyRAWRPQEEQrlyAEIQGKL-VLLKELEKVKQQV---------ALLREN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 669266302  632 EAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKL 670
Cdd:pfam07321  82 EADLEKQVAEARQQLEAEREALRQARQALAEARRAVEKF 120
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
535-666 6.84e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 535 RIMEEVMKTYIKQQeklntiLRRKQQlqmevemlSNSKAMKELTEEQQNLQKELEclQAEhaQRMEEfyFEQR----DLE 610
Cdd:COG3206  152 AVANALAEAYLEQN------LELRRE--------EARKALEFLEEQLPELRKELE--EAE--AALEE--FRQKnglvDLS 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 669266302 611 KKLDQVMKQKcscdsnlekdkeAEYAAQLAELRQRLDHAEADRQELQDELRQEREA 666
Cdd:COG3206  212 EEAKLLLQQL------------SELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 548-600 8.44e-03

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


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 35.70  E-value: 8.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 669266302  548 QEKLNTILRRKQQLQMEVEMLSNSKAmkELTEEQQNLQKELECLQAEHAQRME 600
Cdd:pfam06005  10 ETKIQAAVDTIALLQMENEELKEENE--ELKEEANELEEENQQLKQERNQWQE 60
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 541-671 9.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302 541 MKTYIKQQEKLNTILRRKQQLQMEVEMLsnsKAMKELTEEQQNLQKELECLQAEHAQRMEEFYFEQRDLEKKLDQVMKQk 620
Cdd:COG1196  661 SLTGGSRRELLAALLEAEAELEELAERL---AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE- 736

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 669266302 621 cscdsnlEKDKEAEYAAQLAELRQRLDHAEADRQELQDELRQEREAREKLE 671
Cdd:COG1196  737 -------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 597-681 9.35e-03

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


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.40  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669266302   597 QRMEEF--YFEQRD----LEKKLDQVMKQKCSCDSNLEKDKEAEYAAQLAE-LRQRLDHAEADRQELQDELRQER----- 664
Cdd:smart01071  43 ERMEEIknLKYELImndhLNKRIDKLLKGLREEELSPETPTYNEMLAELQDqLKKELEEANGDSEGLLEELKKHRdklkk 122

                           90       100
                   ....*....|....*....|
gi 669266302   665 ---EAREKLELMIKELKLQI 681
Cdd:smart01071 123 eqkELRKKLDELEKEEKKKI 142
 
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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