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Conserved domains on  [gi|1799133487|ref|NP_001364775|]
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Nipped-B-like protein scc-2 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCC2 cd23958
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid ...
 743-2069 0e+00

Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid cohesion protein 2 (Scc2) and its homolog (Scc2 homolog, also called Nipped-B-like protein or NIPBL). Scc2/NIPBL and Scc4 form a complex that is responsible for loading the cohesin protein onto sister chromatids during mitosis and meiosis. Cohesin is a ring-shaped protein complex that encircles the sister chromatids and helps to hold them together until they are ready to be separated during cell division. In addition to its role in chromosome segregation, cohesin also plays important roles in other cellular processes such as transcription, chromosome condensation, and DNA repair.


:

Pssm-ID: 467937 [Multi-domain]  Cd Length: 1197  Bit Score: 1061.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  743 KLLKLVAMLDRNIRDAISADnqrllvpCDDDVDVGDVLEKEICEERVKRASDAAVVALNIMSSHRMHKQVIIEDVIDRCV 822
Cdd:cd23958      1 KLVRLLTILERNIRDGESLD-------LDLDESQEDDEERLWLLERIDRALEAADASLTILTSPGLPKQLYSEDLIERVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  823 GLTRLLLIHLIYPASDSIYKSVNSKKkdrapeEARRRKKAGVCTRDKFSEYIYERITEAIGLLAVLVKSESMTDTSVHNV 902
Cdd:cd23958     74 DFLKFQLENTIYPAYDPVYRSDSSAK------AGKKKRAKASSKKKKSVSTLLNKLCELLSLLAELLSLQSLTDSVILQL 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  903 ASVALTPFFV----ANVGSLQITAMLLASNIFSRAEDsLRFSMITDLLSSLHRAPqfTQKNSNNGYSLPDGSWISTTTAL 978
Cdd:cd23958    148 VYLAISPFFVenavSNVDELQLSALKLLTSIFSRYPD-QRQFIIEEILSSLAKLP--SSKRNLRQFRLNDGKSIQMVTAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  979 FIQLVQSTIKIPKFKKHADEDELAKRS-----KKEEAMVKEGFLKASKVTNAFLNGFLAKCSQKgnKMDGEEDYRILFSN 1053
Cdd:cd23958    225 LLQLVQSSVKLPNLEKESSRDKSLEEDsdellEDEESALAKSYESAVRIASYFLSFLLQKCTKK--KKEKDTDYRPLFEN 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1054 FLQELLSALYSPEWPAAEMILTALGSLLVKNFRSKSSDMTIRQASLDYLGNITAKLRKDQKEaiagerrldavvkksfll 1133
Cdd:cd23958    303 FVQDLLTVLNLPEWPAAELLLSLLGRLLVSIFSNKKTDANARVMALDLLGLIAARLRKDALA------------------ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1134 lsdkgvedyesvdisnlkqndklKVLETSLIDYLVITNSSDI-IVYACNFYVGEWYKEVAEDLESARSKLKqtvdtnESE 1212
Cdd:cd23958    365 -----------------------EELQKALLDYLAENSSSDPsLESARGFYLAQWLRDLSNELEKAEKAAE------EED 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1213 KDVKKaerkyekiqyrgaEMKVFLSKILDKKEIKRRLEKSNkvkMLDSDAFWAVKFLAQSREFTHSFDTYLKHIVFGAGs 1292
Cdd:cd23958    416 TILKL-------------ELSELRKKFLDSKILSKEEEASP---LSREDAKLLYRALASQRPLSQSFDPILKQLLSSLD- 478

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1293 ETIVALRSKALKCLSSIIEADSSVLILEDVQQAVHTRMVDSHAQVRESAVELIGRFVLYDEEYVRKYYSQIAERILDTGV 1372
Cdd:cd23958    479 EPAVTLRTKALKALSLVVEADPSILGDPDVQRAVEGRLLDSSASVREAAVELVGKYISSRPDLAEQYYEMIAERILDTGV 558

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1373 AVRKRVIRIMREICEKFPTFEMIPDMLARMIRRVTD-EEGVKKLVFETFTTLWFQPVDTRI----YTNAVATKVTTMCSV 1447
Cdd:cd23958    559 SVRKRVIKILRDIYLRTPDFEIKVDICVRLLRRINDeEESIKDLARKTFQELWFTPFPESSspaqDKESLAERVLLIVDV 638

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1448 AQHCIKdaMSDYLEQLILHIVKN--GQEGSGMSVAVKQIIDSLVDHILNLEQHKSSENVSEVelmrrkeqeekyMAYLST 1525
Cdd:cd23958    639 VAACRK--GLDLLEQLLKRLLKSkeDKEDKSVRKACKQLVDCLVELILELEEDDDESSESDL------------VACLST 704

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1526 LAVFSKIRP-LLLTSHVEVLLPYLTfSGAKTNAENQVTKEMIGMLERVIPLVPFPSNIVLDSIDENLCKVIMFNGMALVV 1604
Cdd:cd23958    705 LHLFAKADPkLLLVEHAETLQPYLK-SKCSTREDQQVLRYVLRILRSVLPLLSHPSESFLEELEEDLLKLLLKHSVTVLQ 783

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1605 SAVSCVASIYKKFKRGATKTIDVFSTYLKHLEVIKRNFDSNPrydLDPKLFPILSRSIFTLGVLSRYFQFEEFVKEDPTE 1684
Cdd:cd23958    784 EAIACLCAVVNKLTKNYERLRKALQSCLKLLRKYKRQANLDP---SSLKEDPKLLRLLYILGLLARYCDFDSERDDFEKA 860

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1685 --EKVEALKEKVFITLEFFSRYHKGG-LRQKALTAMGHFCAQHSTYLTKRQLTNTYLEILNaansPQQQQQRILVLQNLE 1761
Cdd:cd23958    861 plKTKESVKELVFDLLLFFTKPPIDEdVRKKALQALGFLCIAHPKLFLSPEVLKLLDEILA----SGSLKLKLQVLRNLQ 936

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1762 MFLQCEEQKLAASHDKWDENKEA-----QNLKEMELSGSGLGSSVIQKYWKAVLESYVDADIQLRRAAVQVVWLTLNQGL 1836
Cdd:cd23958    937 EFLQAEEKRMEAADAEWKKNSKAadvkvLDGKEMGDADSGVASSIMQRYLKDILELCLSSDSQVRLAALKVLELILRQGL 1016

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1837 VTPGASIPTLIAMTTDPVDVIRNRIDILLKEIDSKYSGMVQSKAMQGVRLSYKLHLKLRMLQQEKFVRgfrfcdfhlntl 1916
Cdd:cd23958   1017 VHPIQCVPTLIALETDPNPAIRKLALRLLKELHEKYESLVESKYLEGVRLAFQYQKRLAGDTRGRGFR------------ 1084

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1917 pnalpeKTHDGMAVLSGLYQSLRTNRQQRRSFLQSMVKLFSEEF---SHDKPQLMEYIFIADNLAMFPYQMIDEPLYVMR 1993
Cdd:cd23958   1085 ------TDSPPTALLGRLYSLLRGNRKSRRKFLKSLLKLFDFDLkksSDSPSDLDFLLFLAENLAFLPYQTQDEPLFVIH 1158

                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799133487 1994 QIDQNIAQTGQSLLvqyklqlrmqesededivfldenmmsrlsqlgqietfHQLFLDSQVPSLLLYVRTFLMQLYG 2069
Cdd:cd23958   1159 TIDRILSVTGSSLL-------------------------------------QAIAKASQALLLLLLLKQHLKRLYG 1197
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 219-302 1.05e-07

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


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 53.51  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  219 EELKRL-----RIAEEKRLLEEQQRlREQMERERLaeikRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAEVE 293
Cdd:pfam05672   10 EEAARIlaekrRQAREQREREEQER-LEKEEEERL----RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEE 84


                   ....*....
gi 1799133487  294 RQRSELEER 302
Cdd:pfam05672   85 AEEREQREQ 93
 
Name Accession Description Interval E-value
SCC2 cd23958
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid ...
 743-2069 0e+00

Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid cohesion protein 2 (Scc2) and its homolog (Scc2 homolog, also called Nipped-B-like protein or NIPBL). Scc2/NIPBL and Scc4 form a complex that is responsible for loading the cohesin protein onto sister chromatids during mitosis and meiosis. Cohesin is a ring-shaped protein complex that encircles the sister chromatids and helps to hold them together until they are ready to be separated during cell division. In addition to its role in chromosome segregation, cohesin also plays important roles in other cellular processes such as transcription, chromosome condensation, and DNA repair.


Pssm-ID: 467937 [Multi-domain]  Cd Length: 1197  Bit Score: 1061.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  743 KLLKLVAMLDRNIRDAISADnqrllvpCDDDVDVGDVLEKEICEERVKRASDAAVVALNIMSSHRMHKQVIIEDVIDRCV 822
Cdd:cd23958      1 KLVRLLTILERNIRDGESLD-------LDLDESQEDDEERLWLLERIDRALEAADASLTILTSPGLPKQLYSEDLIERVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  823 GLTRLLLIHLIYPASDSIYKSVNSKKkdrapeEARRRKKAGVCTRDKFSEYIYERITEAIGLLAVLVKSESMTDTSVHNV 902
Cdd:cd23958     74 DFLKFQLENTIYPAYDPVYRSDSSAK------AGKKKRAKASSKKKKSVSTLLNKLCELLSLLAELLSLQSLTDSVILQL 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  903 ASVALTPFFV----ANVGSLQITAMLLASNIFSRAEDsLRFSMITDLLSSLHRAPqfTQKNSNNGYSLPDGSWISTTTAL 978
Cdd:cd23958    148 VYLAISPFFVenavSNVDELQLSALKLLTSIFSRYPD-QRQFIIEEILSSLAKLP--SSKRNLRQFRLNDGKSIQMVTAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  979 FIQLVQSTIKIPKFKKHADEDELAKRS-----KKEEAMVKEGFLKASKVTNAFLNGFLAKCSQKgnKMDGEEDYRILFSN 1053
Cdd:cd23958    225 LLQLVQSSVKLPNLEKESSRDKSLEEDsdellEDEESALAKSYESAVRIASYFLSFLLQKCTKK--KKEKDTDYRPLFEN 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1054 FLQELLSALYSPEWPAAEMILTALGSLLVKNFRSKSSDMTIRQASLDYLGNITAKLRKDQKEaiagerrldavvkksfll 1133
Cdd:cd23958    303 FVQDLLTVLNLPEWPAAELLLSLLGRLLVSIFSNKKTDANARVMALDLLGLIAARLRKDALA------------------ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1134 lsdkgvedyesvdisnlkqndklKVLETSLIDYLVITNSSDI-IVYACNFYVGEWYKEVAEDLESARSKLKqtvdtnESE 1212
Cdd:cd23958    365 -----------------------EELQKALLDYLAENSSSDPsLESARGFYLAQWLRDLSNELEKAEKAAE------EED 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1213 KDVKKaerkyekiqyrgaEMKVFLSKILDKKEIKRRLEKSNkvkMLDSDAFWAVKFLAQSREFTHSFDTYLKHIVFGAGs 1292
Cdd:cd23958    416 TILKL-------------ELSELRKKFLDSKILSKEEEASP---LSREDAKLLYRALASQRPLSQSFDPILKQLLSSLD- 478

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1293 ETIVALRSKALKCLSSIIEADSSVLILEDVQQAVHTRMVDSHAQVRESAVELIGRFVLYDEEYVRKYYSQIAERILDTGV 1372
Cdd:cd23958    479 EPAVTLRTKALKALSLVVEADPSILGDPDVQRAVEGRLLDSSASVREAAVELVGKYISSRPDLAEQYYEMIAERILDTGV 558

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1373 AVRKRVIRIMREICEKFPTFEMIPDMLARMIRRVTD-EEGVKKLVFETFTTLWFQPVDTRI----YTNAVATKVTTMCSV 1447
Cdd:cd23958    559 SVRKRVIKILRDIYLRTPDFEIKVDICVRLLRRINDeEESIKDLARKTFQELWFTPFPESSspaqDKESLAERVLLIVDV 638

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1448 AQHCIKdaMSDYLEQLILHIVKN--GQEGSGMSVAVKQIIDSLVDHILNLEQHKSSENVSEVelmrrkeqeekyMAYLST 1525
Cdd:cd23958    639 VAACRK--GLDLLEQLLKRLLKSkeDKEDKSVRKACKQLVDCLVELILELEEDDDESSESDL------------VACLST 704

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1526 LAVFSKIRP-LLLTSHVEVLLPYLTfSGAKTNAENQVTKEMIGMLERVIPLVPFPSNIVLDSIDENLCKVIMFNGMALVV 1604
Cdd:cd23958    705 LHLFAKADPkLLLVEHAETLQPYLK-SKCSTREDQQVLRYVLRILRSVLPLLSHPSESFLEELEEDLLKLLLKHSVTVLQ 783

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1605 SAVSCVASIYKKFKRGATKTIDVFSTYLKHLEVIKRNFDSNPrydLDPKLFPILSRSIFTLGVLSRYFQFEEFVKEDPTE 1684
Cdd:cd23958    784 EAIACLCAVVNKLTKNYERLRKALQSCLKLLRKYKRQANLDP---SSLKEDPKLLRLLYILGLLARYCDFDSERDDFEKA 860

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1685 --EKVEALKEKVFITLEFFSRYHKGG-LRQKALTAMGHFCAQHSTYLTKRQLTNTYLEILNaansPQQQQQRILVLQNLE 1761
Cdd:cd23958    861 plKTKESVKELVFDLLLFFTKPPIDEdVRKKALQALGFLCIAHPKLFLSPEVLKLLDEILA----SGSLKLKLQVLRNLQ 936

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1762 MFLQCEEQKLAASHDKWDENKEA-----QNLKEMELSGSGLGSSVIQKYWKAVLESYVDADIQLRRAAVQVVWLTLNQGL 1836
Cdd:cd23958    937 EFLQAEEKRMEAADAEWKKNSKAadvkvLDGKEMGDADSGVASSIMQRYLKDILELCLSSDSQVRLAALKVLELILRQGL 1016

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1837 VTPGASIPTLIAMTTDPVDVIRNRIDILLKEIDSKYSGMVQSKAMQGVRLSYKLHLKLRMLQQEKFVRgfrfcdfhlntl 1916
Cdd:cd23958   1017 VHPIQCVPTLIALETDPNPAIRKLALRLLKELHEKYESLVESKYLEGVRLAFQYQKRLAGDTRGRGFR------------ 1084

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1917 pnalpeKTHDGMAVLSGLYQSLRTNRQQRRSFLQSMVKLFSEEF---SHDKPQLMEYIFIADNLAMFPYQMIDEPLYVMR 1993
Cdd:cd23958   1085 ------TDSPPTALLGRLYSLLRGNRKSRRKFLKSLLKLFDFDLkksSDSPSDLDFLLFLAENLAFLPYQTQDEPLFVIH 1158

                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799133487 1994 QIDQNIAQTGQSLLvqyklqlrmqesededivfldenmmsrlsqlgqietfHQLFLDSQVPSLLLYVRTFLMQLYG 2069
Cdd:cd23958   1159 TIDRILSVTGSSLL-------------------------------------QAIAKASQALLLLLLLKQHLKRLYG 1197
Nipped-B_C pfam12830
Sister chromatid cohesion C-terminus; This domain lies towards the C-terminus of nipped-B or ...
 1798-1997 2.32e-57

Sister chromatid cohesion C-terminus; This domain lies towards the C-terminus of nipped-B or sister chromatid cohesion proteins.


Pssm-ID: 463722  Cd Length: 180  Bit Score: 196.60  E-value: 2.32e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1798 GSSVIQKYWKAVLESYVDADIQLRRAAVQVVWLTLNQGLVTPGASIPTLIAMTTDPVDVIRNRIDILLKEIDSKYSGMVQ 1877
Cdd:pfam12830    1 CSALVQRYLKHILEICLSSDDQVRLLALEVLALILRQGLVHPKECIPTLIALETSPNPYIRKLAFELHKELHEKHESLLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1878 SKAMQGVRLSYKLHLKLrmlqqekfVRGFRFcdfhlntlpnalpektHDGMAVLSGLYQSLRTNRQQRRSFLQSMVKLF- 1956
Cdd:pfam12830   81 SRYMEGIRLAFEYQRRV--------LSGATL----------------EPPTSFLSLLYSLLRSNKKSRKKFLKSLVKLFf 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1799133487 1957 --SEEFSHDKPQLMEYIFIADNLAMFPYQMIDEPLYVMRQIDQ 1997
Cdd:pfam12830  137 dlDLSSESSPSDLDFLRFLAENLAFLPYQTQDEVLFLIHHIDR 179
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 219-302 1.05e-07

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 53.51  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  219 EELKRL-----RIAEEKRLLEEQQRlREQMERERLaeikRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAEVE 293
Cdd:pfam05672   10 EEAARIlaekrRQAREQREREEQER-LEKEEEERL----RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEE 84


                   ....*....
gi 1799133487  294 RQRSELEER 302
Cdd:pfam05672   85 AEEREQREQ 93
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-300 1.54e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEElkrlRIAEEKR--LLEEQQRLREQmERERLAE---IKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQN 286
Cdd:PRK09510    78 EEQRKKKEQ----QQAEELQqkQAAEQERLKQL-EKERLAAqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE 152

                           90
                   ....*....|....
gi 1799133487  287 KHIAEVERQRSELE 300
Cdd:PRK09510   153 AKRAAAAAKKAAAE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-308 2.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIA 290
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                           90
                   ....*....|....*...
gi 1799133487  291 EVERQRSELEERFARVSQ 308
Cdd:COG1196    380 ELEELAEELLEALRAAAE 397
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 212-300 7.58e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERlaeiKRLEEAAR-LEDERRIAADIEAQKQAMLQKMQAEQN-KHI 289
Cdd:TIGR02794  107 AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER----KAKEEAAKqAEEEAKAKAAAEAKKKAEEAKKKAEAEaKAK 182

                           90
                   ....*....|.
gi 1799133487  290 AEVERQRSELE 300
Cdd:TIGR02794  183 AEAEAKAKAEE 193
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 211-284 4.32e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLE---EQQRLREQMERERLAEIKRLEEAARLEDERRIA---ADIEAQKQAMLQKMQAE 284
Cdd:cd06503     39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIEEARKEAEKIKEEILAEAKEEAERILEqakAEIEQEKEKALAELRKE 118
 
Name Accession Description Interval E-value
SCC2 cd23958
Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid ...
 743-2069 0e+00

Sister chromatid cohesion protein 2 and homologs; This family includes Sister chromatid cohesion protein 2 (Scc2) and its homolog (Scc2 homolog, also called Nipped-B-like protein or NIPBL). Scc2/NIPBL and Scc4 form a complex that is responsible for loading the cohesin protein onto sister chromatids during mitosis and meiosis. Cohesin is a ring-shaped protein complex that encircles the sister chromatids and helps to hold them together until they are ready to be separated during cell division. In addition to its role in chromosome segregation, cohesin also plays important roles in other cellular processes such as transcription, chromosome condensation, and DNA repair.


Pssm-ID: 467937 [Multi-domain]  Cd Length: 1197  Bit Score: 1061.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  743 KLLKLVAMLDRNIRDAISADnqrllvpCDDDVDVGDVLEKEICEERVKRASDAAVVALNIMSSHRMHKQVIIEDVIDRCV 822
Cdd:cd23958      1 KLVRLLTILERNIRDGESLD-------LDLDESQEDDEERLWLLERIDRALEAADASLTILTSPGLPKQLYSEDLIERVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  823 GLTRLLLIHLIYPASDSIYKSVNSKKkdrapeEARRRKKAGVCTRDKFSEYIYERITEAIGLLAVLVKSESMTDTSVHNV 902
Cdd:cd23958     74 DFLKFQLENTIYPAYDPVYRSDSSAK------AGKKKRAKASSKKKKSVSTLLNKLCELLSLLAELLSLQSLTDSVILQL 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  903 ASVALTPFFV----ANVGSLQITAMLLASNIFSRAEDsLRFSMITDLLSSLHRAPqfTQKNSNNGYSLPDGSWISTTTAL 978
Cdd:cd23958    148 VYLAISPFFVenavSNVDELQLSALKLLTSIFSRYPD-QRQFIIEEILSSLAKLP--SSKRNLRQFRLNDGKSIQMVTAL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  979 FIQLVQSTIKIPKFKKHADEDELAKRS-----KKEEAMVKEGFLKASKVTNAFLNGFLAKCSQKgnKMDGEEDYRILFSN 1053
Cdd:cd23958    225 LLQLVQSSVKLPNLEKESSRDKSLEEDsdellEDEESALAKSYESAVRIASYFLSFLLQKCTKK--KKEKDTDYRPLFEN 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1054 FLQELLSALYSPEWPAAEMILTALGSLLVKNFRSKSSDMTIRQASLDYLGNITAKLRKDQKEaiagerrldavvkksfll 1133
Cdd:cd23958    303 FVQDLLTVLNLPEWPAAELLLSLLGRLLVSIFSNKKTDANARVMALDLLGLIAARLRKDALA------------------ 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1134 lsdkgvedyesvdisnlkqndklKVLETSLIDYLVITNSSDI-IVYACNFYVGEWYKEVAEDLESARSKLKqtvdtnESE 1212
Cdd:cd23958    365 -----------------------EELQKALLDYLAENSSSDPsLESARGFYLAQWLRDLSNELEKAEKAAE------EED 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1213 KDVKKaerkyekiqyrgaEMKVFLSKILDKKEIKRRLEKSNkvkMLDSDAFWAVKFLAQSREFTHSFDTYLKHIVFGAGs 1292
Cdd:cd23958    416 TILKL-------------ELSELRKKFLDSKILSKEEEASP---LSREDAKLLYRALASQRPLSQSFDPILKQLLSSLD- 478

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1293 ETIVALRSKALKCLSSIIEADSSVLILEDVQQAVHTRMVDSHAQVRESAVELIGRFVLYDEEYVRKYYSQIAERILDTGV 1372
Cdd:cd23958    479 EPAVTLRTKALKALSLVVEADPSILGDPDVQRAVEGRLLDSSASVREAAVELVGKYISSRPDLAEQYYEMIAERILDTGV 558

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1373 AVRKRVIRIMREICEKFPTFEMIPDMLARMIRRVTD-EEGVKKLVFETFTTLWFQPVDTRI----YTNAVATKVTTMCSV 1447
Cdd:cd23958    559 SVRKRVIKILRDIYLRTPDFEIKVDICVRLLRRINDeEESIKDLARKTFQELWFTPFPESSspaqDKESLAERVLLIVDV 638

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1448 AQHCIKdaMSDYLEQLILHIVKN--GQEGSGMSVAVKQIIDSLVDHILNLEQHKSSENVSEVelmrrkeqeekyMAYLST 1525
Cdd:cd23958    639 VAACRK--GLDLLEQLLKRLLKSkeDKEDKSVRKACKQLVDCLVELILELEEDDDESSESDL------------VACLST 704

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1526 LAVFSKIRP-LLLTSHVEVLLPYLTfSGAKTNAENQVTKEMIGMLERVIPLVPFPSNIVLDSIDENLCKVIMFNGMALVV 1604
Cdd:cd23958    705 LHLFAKADPkLLLVEHAETLQPYLK-SKCSTREDQQVLRYVLRILRSVLPLLSHPSESFLEELEEDLLKLLLKHSVTVLQ 783

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1605 SAVSCVASIYKKFKRGATKTIDVFSTYLKHLEVIKRNFDSNPrydLDPKLFPILSRSIFTLGVLSRYFQFEEFVKEDPTE 1684
Cdd:cd23958    784 EAIACLCAVVNKLTKNYERLRKALQSCLKLLRKYKRQANLDP---SSLKEDPKLLRLLYILGLLARYCDFDSERDDFEKA 860

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1685 --EKVEALKEKVFITLEFFSRYHKGG-LRQKALTAMGHFCAQHSTYLTKRQLTNTYLEILNaansPQQQQQRILVLQNLE 1761
Cdd:cd23958    861 plKTKESVKELVFDLLLFFTKPPIDEdVRKKALQALGFLCIAHPKLFLSPEVLKLLDEILA----SGSLKLKLQVLRNLQ 936

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1762 MFLQCEEQKLAASHDKWDENKEA-----QNLKEMELSGSGLGSSVIQKYWKAVLESYVDADIQLRRAAVQVVWLTLNQGL 1836
Cdd:cd23958    937 EFLQAEEKRMEAADAEWKKNSKAadvkvLDGKEMGDADSGVASSIMQRYLKDILELCLSSDSQVRLAALKVLELILRQGL 1016

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1837 VTPGASIPTLIAMTTDPVDVIRNRIDILLKEIDSKYSGMVQSKAMQGVRLSYKLHLKLRMLQQEKFVRgfrfcdfhlntl 1916
Cdd:cd23958   1017 VHPIQCVPTLIALETDPNPAIRKLALRLLKELHEKYESLVESKYLEGVRLAFQYQKRLAGDTRGRGFR------------ 1084

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1917 pnalpeKTHDGMAVLSGLYQSLRTNRQQRRSFLQSMVKLFSEEF---SHDKPQLMEYIFIADNLAMFPYQMIDEPLYVMR 1993
Cdd:cd23958   1085 ------TDSPPTALLGRLYSLLRGNRKSRRKFLKSLLKLFDFDLkksSDSPSDLDFLLFLAENLAFLPYQTQDEPLFVIH 1158

                         1290      1300      1310      1320      1330      1340      1350
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799133487 1994 QIDQNIAQTGQSLLvqyklqlrmqesededivfldenmmsrlsqlgqietfHQLFLDSQVPSLLLYVRTFLMQLYG 2069
Cdd:cd23958   1159 TIDRILSVTGSSLL-------------------------------------QAIAKASQALLLLLLLKQHLKRLYG 1197
Nipped-B_C pfam12830
Sister chromatid cohesion C-terminus; This domain lies towards the C-terminus of nipped-B or ...
 1798-1997 2.32e-57

Sister chromatid cohesion C-terminus; This domain lies towards the C-terminus of nipped-B or sister chromatid cohesion proteins.


Pssm-ID: 463722  Cd Length: 180  Bit Score: 196.60  E-value: 2.32e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1798 GSSVIQKYWKAVLESYVDADIQLRRAAVQVVWLTLNQGLVTPGASIPTLIAMTTDPVDVIRNRIDILLKEIDSKYSGMVQ 1877
Cdd:pfam12830    1 CSALVQRYLKHILEICLSSDDQVRLLALEVLALILRQGLVHPKECIPTLIALETSPNPYIRKLAFELHKELHEKHESLLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1878 SKAMQGVRLSYKLHLKLrmlqqekfVRGFRFcdfhlntlpnalpektHDGMAVLSGLYQSLRTNRQQRRSFLQSMVKLF- 1956
Cdd:pfam12830   81 SRYMEGIRLAFEYQRRV--------LSGATL----------------EPPTSFLSLLYSLLRSNKKSRKKFLKSLVKLFf 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1799133487 1957 --SEEFSHDKPQLMEYIFIADNLAMFPYQMIDEPLYVMRQIDQ 1997
Cdd:pfam12830  137 dlDLSSESSPSDLDFLRFLAENLAFLPYQTQDEVLFLIHHIDR 179
Cohesin_HEAT pfam12765
HEAT repeat associated with sister chromatid cohesion; This HEAT repeat is found most ...
 1304-1345 2.90e-10

HEAT repeat associated with sister chromatid cohesion; This HEAT repeat is found most frequently in sister chromatid cohesion proteins such as Nipped-B. HEAT repeats are found tandemly repeated in many proteins, and they appear to serve as flexible scaffolding on which other components can assemble.


Pssm-ID: 403845 [Multi-domain]  Cd Length: 42  Bit Score: 57.08  E-value: 2.90e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1799133487 1304 KCLSSIIEADSSVLILEDVQQAVHTRMVDSHAQVRESAVELI 1345
Cdd:pfam12765    1 KALSSLVEKDPSILDSPDVKEAISRRLTDSSPSVRDAALELL 42
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 219-302 1.05e-07

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 53.51  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  219 EELKRL-----RIAEEKRLLEEQQRlREQMERERLaeikRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAEVE 293
Cdd:pfam05672   10 EEAARIlaekrRQAREQREREEQER-LEKEEEERL----RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEE 84


                   ....*....
gi 1799133487  294 RQRSELEER 302
Cdd:pfam05672   85 AEEREQREQ 93
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 185-302 2.03e-07

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: 56.29  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  185 QKLYEEQcRQIEKERKEQEERKRKQELEEQRKRneELKRL---RIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLE 261
Cdd:pfam17380  404 VKILEEE-RQRKIQQQKVEMEQIRAEQEEARQR--EVRRLeeeRAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1799133487  262 DERRIAADIEAQKQAMLQKMQAEQNKHIAEVERQR----SELEER 302
Cdd:pfam17380  481 KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRklleKEMEER 525
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 212-302 6.62e-07

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: 54.74  E-value: 6.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEdERRIAADIEAQKQAMLQKMQAEQNKHIAE 291
Cdd:pfam17380  453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIYE 531

                           90
                   ....*....|.
gi 1799133487  292 VERQRSELEER 302
Cdd:pfam17380  532 EERRREAEEER 542
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 211-308 6.70e-07

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 50.95  E-value: 6.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQR---KRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRiaadiEAQK---QAMLQKMQ-A 283
Cdd:pfam15236   55 LEHQNaikKQLEEKERQKKLEEERRRQEEQEEEERLRREREEEQKQFEEERRKQKEKE-----EAMTrktQALLQAMQkA 129

                           90       100
                   ....*....|....*....|....*
gi 1799133487  284 EQNKHIAEVERQRSELEERFARVSQ 308
Cdd:pfam15236  130 QELAQRLKQEQRIRELAEKGHDTSQ 154
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 206-308 7.59e-07

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 50.81  E-value: 7.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  206 KRKQELEEQRKRNEELKRlRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRiaadiEAQKQAMLQKMQAE- 284
Cdd:pfam05672   33 ERLEKEEEERLRKEELRR-RAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQR-----EQEEQERLQKQKEEa 106

                           90       100
                   ....*....|....*....|....
gi 1799133487  285 QNKHIAEVERQRSELEERFARVSQ 308
Cdd:pfam05672  107 EAKAREEAERQRQEREKIMQQEEQ 130
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-300 1.54e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEElkrlRIAEEKR--LLEEQQRLREQmERERLAE---IKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQN 286
Cdd:PRK09510    78 EEQRKKKEQ----QQAEELQqkQAAEQERLKQL-EKERLAAqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE 152

                           90
                   ....*....|....
gi 1799133487  287 KHIAEVERQRSELE 300
Cdd:PRK09510   153 AKRAAAAAKKAAAE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-308 2.88e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIA 290
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                           90
                   ....*....|....*...
gi 1799133487  291 EVERQRSELEERFARVSQ 308
Cdd:COG1196    380 ELEELAEELLEALRAAAE 397
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 211-308 2.97e-06

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 48.38  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEEL-KRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAAdieaqKQAMLQKMQAEQNKHI 289
Cdd:pfam20492   29 LEESEETAEELeEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAE-----AQEEIARLEEEVERKE 103

                           90
                   ....*....|....*....
gi 1799133487  290 AEVERQRSELEErfARVSQ 308
Cdd:pfam20492  104 EEARRLQEELEE--AREEE 120
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 212-308 1.35e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 47.35  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQ---------QRLREQMERERLAEIKRLEEAARLEDERRiaADIEAQKQAMLQKMQ 282
Cdd:pfam15346   10 EETARRVEEAVAKRVEEELEKRKDEieaeverrvEEARKIMEKQVLEELEREREAELEEERRK--EEEERKKREELERIL 87

                           90       100
                   ....*....|....*....|....*.
gi 1799133487  283 AEQNKHIAEVerQRSELEERFARVSQ 308
Cdd:pfam15346   88 EENNRKIEEA--QRKEAEERLAMLEE 111
PRK12704 PRK12704
phosphodiesterase; Provisional
 211-308 1.48e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.16  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKrllEEQQRLREQMERE---RLAEIKRLEEaaRLED-----ERRIAA------DIEAQKQA 276
Cdd:PRK12704    44 LEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKElreRRNELQKLEK--RLLQkeenlDRKLELlekreeELEKKEKE 118

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1799133487  277 MLQKMQAEQNKHiAEVERQRSELEERFARVSQ 308
Cdd:PRK12704   119 LEQKQQELEKKE-EELEELIEEQLQELERISG 149
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-301 1.50e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLE-EQQRLREQMERERLAEIKRLEEAARLEDER-RIAADIEAQKQAMLQKMQAEQNKHI 289
Cdd:PRK09510    91 ELQQKQAAEQERLKQLEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAAAEAKKK 170

                           90
                   ....*....|..
gi 1799133487  290 AEVERQRSELEE 301
Cdd:PRK09510   171 AEAEAAKKAAAE 182
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 185-302 1.60e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.96  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  185 QKLYEEQCRQIEKERKEQEERKRKQELEEQRKRNEElkRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDER 264
Cdd:pfam05672   26 QREREEQERLEKEEEERLRKEELRRRAEEERARREE--EARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQK 103

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1799133487  265 RIAadiEAQKQAMLQKMQAEQNKHIAEVERQRSELEER 302
Cdd:pfam05672  104 EEA---EAKAREEAERQRQEREKIMQQEEQERLERKKR 138
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-305 1.86e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRL---REQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNK 287
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                           90
                   ....*....|....*...
gi 1799133487  288 HIAEVERQRSELEERFAR 305
Cdd:COG1196    401 QLEELEEAEEALLERLER 418
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 213-304 2.08e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 49.56  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELkRLRiaeEKRLLEEQQRlREQMERERLAEIKRLEEAARLEDE--RRIAADIEAQKQamlqkmQAEQNKHIA 290
Cdd:pfam15709  381 EQQRRFEEI-RLR---KQRLEEERQR-QEEEERKQRLQLQAAQERARQQQEefRRKLQELQRKKQ------QEEAERAEA 449

                           90
                   ....*....|....
gi 1799133487  291 EVERQRsELEERFA 304
Cdd:pfam15709  450 EKQRQK-ELEMQLA 462
PTZ00121 PTZ00121
MAEBL; Provisional
 212-308 2.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKR-----LRIAEEKRLLEEQQRLR-EQMERERLAEIKRLEEAARLEDERRIAADI------EAQKQAMLQ 279
Cdd:PTZ00121  1629 EEEKKKVEQLKKkeaeeKKKAEELKKAEEENKIKaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeaeEAKKAEELK 1708

                           90       100
                   ....*....|....*....|....*....
gi 1799133487  280 KMQAEQNKHIAEVerqRSELEERFARVSQ 308
Cdd:PTZ00121  1709 KKEAEEKKKAEEL---KKAEEENKIKAEE 1734
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 214-299 4.99e-05

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 46.10  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  214 QRKRNEELKRLRIAEEK------RLLEEQQRLRE-QMERER-LAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQ 285
Cdd:PRK07352    49 EERREAILQALKEAEERlrqaaqALAEAQQKLAQaQQEAERiRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQ 128

                           90
                   ....*....|....
gi 1799133487  286 NKHIAEVERQRSEL 299
Cdd:PRK07352   129 ERVIAQLRREAAEL 142
PRK01294 PRK01294
lipase secretion chaperone;
212-304 7.09e-05

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 47.36  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKR--LEEAARLEDERRIAADIEAQK---QAMLQKMQ---- 282
Cdd:PRK01294   183 EENQYQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRaaLQESQRQQALLQQLAQLQASGaspQELRLMRAqlvg 262

                           90       100
                   ....*....|....*....|..
gi 1799133487  283 AEQNKHIAEVERQRSELEERFA 304
Cdd:PRK01294   263 PEAAQRLEQLDQQRAAWQQRYD 284
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 212-300 7.58e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERlaeiKRLEEAAR-LEDERRIAADIEAQKQAMLQKMQAEQN-KHI 289
Cdd:TIGR02794  107 AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER----KAKEEAAKqAEEEAKAKAAAEAKKKAEEAKKKAEAEaKAK 182

                           90
                   ....*....|.
gi 1799133487  290 AEVERQRSELE 300
Cdd:TIGR02794  183 AEAEAKAKAEE 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-302 8.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 8.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIA 290
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                           90
                   ....*....|..
gi 1799133487  291 EVERQRSELEER 302
Cdd:COG1196    440 EEEALEEAAEEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
211-305 1.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMER-----ERLAEIKRLEEAARLeDERRIAADIEAQKQAMLQKMQAEQ 285
Cdd:COG4913    697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdrlEAAEDLARLELRALL-EERFAAALGDAVERELRENLEERI 775

                           90       100
                   ....*....|....*....|
gi 1799133487  286 NKHIAEVERQRSELEERFAR 305
Cdd:COG4913    776 DALRARLNRAEEELERAMRA 795
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 218-300 1.41e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.38  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  218 NEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAEVERQRS 297
Cdd:TIGR02794   49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128


                   ...
gi 1799133487  298 ELE 300
Cdd:TIGR02794  129 AAE 131
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 212-287 1.50e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 1.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEA---ARLEDERRIAADIEAQKQAMLQKMQAEQNK 287
Cdd:pfam15709  441 QEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAeekARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
PTZ00121 PTZ00121
MAEBL; Provisional
 213-304 1.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKRLRIAEEKRLLEEQQR----LREQMERERLAE--IKRLEEAARLEDERRIAADIEAQKQAMLQKMQaEQN 286
Cdd:PTZ00121  1650 EELKKAEEENKIKAAEEAKKAEEDKKkaeeAKKAEEDEKKAAeaLKKEAEEAKKAEELKKKEAEEKKKAEELKKAE-EEN 1728

                           90
                   ....*....|....*...
gi 1799133487  287 KHIAEVERQRSELEERFA 304
Cdd:PTZ00121  1729 KIKAEEAKKEAEEDKKKA 1746
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-305 2.31e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLRE-QMERERL-AEIKRLEEAARLEDERRIAADIE----AQKQAMLQKMQAE 284
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRElEERLEELeEELAELEEELEELEEELEELEEEleeaEEELEEAEAELAE 362

                           90       100
                   ....*....|....*....|.
gi 1799133487  285 QNKHIAEVERQRSELEERFAR 305
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEE 383
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 211-284 2.99e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 43.24  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLE---EQQRLREQMERERLAEIKRLEEAARLEDERRIA---ADIEAQKQAMLQKMQAE 284
Cdd:COG0711     40 LAEAERAKEEAEAALAEYEEKLAEaraEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAqaeAEIEQERAKALAELRAE 119
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-305 3.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERL-------------AEIKRLEEAARLEDERRIAADIEAQKqam 277
Cdd:COG1196    244 LEAELEELEAELEELEAELAELEAELEELRLELEELELeleeaqaeeyellAELARLEQDIARLEERRRELEERLEE--- 320

                           90       100
                   ....*....|....*....|....*...
gi 1799133487  278 LQKMQAEQNKHIAEVERQRSELEERFAR 305
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELEE 348
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
212-302 3.18e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEE--KRLLEEQQRLREQMErERLAEIKRLEEaaRLEDERRiAADIEAQKQAMLQKMQAEqnkhI 289
Cdd:COG2433    403 HEERELTEEEEEIRRLEEqvERLEAEVEELEAELE-EKDERIERLER--ELSEARS-EERREIRKDREISRLDRE----I 474

                           90
                   ....*....|...
gi 1799133487  290 AEVERQRSELEER 302
Cdd:COG2433    475 ERLERELEEERER 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-304 3.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEEL-KRLRIAEEKRL-LEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIE----AQKQAMLQKMQAE 284
Cdd:COG1196    276 LEELELELEEAqAEEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEleelEEELEEAEEELEE 355

                           90       100
                   ....*....|....*....|
gi 1799133487  285 QNKHIAEVERQRSELEERFA 304
Cdd:COG1196    356 AEAELAEAEEALLEAEAELA 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-308 3.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRiAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERR-IAADIEAQKQAM--LQKMQAEQNKH 288
Cdd:COG1196    274 LELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAeLEEELEELEEELeeLEEELEEAEEE 352

                           90       100
                   ....*....|....*....|
gi 1799133487  289 IAEVERQRSELEERFARVSQ 308
Cdd:COG1196    353 LEEAEAELAEAEEALLEAEA 372
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 211-284 4.32e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLE---EQQRLREQMERERLAEIKRLEEAARLEDERRIA---ADIEAQKQAMLQKMQAE 284
Cdd:cd06503     39 LEEAEKAKEEAEELLAEYEEKLAEaraEAQEIIEEARKEAEKIKEEILAEAKEEAERILEqakAEIEQEKEKALAELRKE 118
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
225-301 4.58e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.25  E-value: 4.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1799133487  225 RIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNkhiAEVERQRSELEE 301
Cdd:COG2268    193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEER---REAETARAEAEA 266
PTZ00121 PTZ00121
MAEBL; Provisional
 213-302 5.00e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKR---LRIAEEKRLLEEQQRLRE-QMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKh 288
Cdd:PTZ00121  1543 EEKKKADELKKaeeLKKAEEKKKAEEAKKAEEdKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK- 1621

                           90
                   ....*....|....
gi 1799133487  289 iaeVERQRSELEER 302
Cdd:PTZ00121  1622 ---AEELKKAEEEK 1632
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 209-302 5.40e-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: 44.52  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  209 QELEEQRKRNEELKRLRIAeekRLLEEQQRLREQM-ERERLAEIKRLEEAARLEDERRIAAdiEAQKQAMLQKMQAEQNK 287
Cdd:pfam13868  169 EEREAEREEIEEEKEREIA---RLRAQQEKAQDEKaERDELRAKLYQEEQERKERQKEREE--AEKKARQRQELQQAREE 243

                           90
                   ....*....|....*
gi 1799133487  288 HIAEVERQRSELEER 302
Cdd:pfam13868  244 QIELKERRLAEEAER 258
PTZ00121 PTZ00121
MAEBL; Provisional
 190-302 6.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  190 EQCRQI----EKERKEQEERKRKQELEEQRKRNEELKRlriAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERR 265
Cdd:PTZ00121  1584 EEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1799133487  266 IAADIEAQKqAMLQKMQAEQNKHIAEVERQRSELEER 302
Cdd:PTZ00121  1661 IKAAEEAKK-AEEDKKKAEEAKKAEEDEKKAAEALKK 1696
Radial_spoke_3 pfam06098
Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) ...
 228-283 6.78e-04

Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) sequences. Eukaryotic cilia and flagella present in diverse types of cells perform motile, sensory, and developmental functions in organizms from protists to humans. They are centred by precisely organized, microtubule-based structures, the axonemes. The axoneme consists of two central singlet microtubules, called the central pair, and nine outer doublet microtubules. These structures are well-conserved during evolution. The outer doublet microtubules, each composed of A and B sub-fibres, are connected to each other by nexin links, while the central pair is held at the centre of the axoneme by radial spokes. The radial spokes are T-shaped structures extending from the A-tubule of each outer doublet microtubule to the centre of the axoneme. Radial spoke protein 3 (RSP3), is present at the proximal end of the spoke stalk and helps in anchoring the radial spoke to the outer doublet. It is thought that radial spokes regulate the activity of inner arm dynein through protein phosphorylation and dephosphorylation.


Pssm-ID: 461827  Cd Length: 286  Bit Score: 43.78  E-value: 6.78e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1799133487  228 EEKRLLEEQQRLREQMERERLAEIKRLEEAAR---LEDERRIAADIEAQKQ--AMLQKMQA 283
Cdd:pfam06098  153 EELANLREQQRAFEELRNAELAEVQRLEEQERrlrEEKERRIAQQREALKKekETAEKIAA 213
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-305 7.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMER-ERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHI 289
Cdd:COG1196    381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                           90
                   ....*....|....*.
gi 1799133487  290 AEVERQRSELEERFAR 305
Cdd:COG1196    461 LLELLAELLEEAALLE 476
PTZ00121 PTZ00121
MAEBL; Provisional
 211-305 8.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKR---------LRIAEEKRLLEEQQRLREQMERE---RLAEIKRLEEAARLEDERRIAA---DIEAQKQ 275
Cdd:PTZ00121  1111 AEEARKAEEAKKKaedarkaeeARKAEDARKAEEARKAEDAKRVEiarKAEDARKAEEARKAEDAKKAEAarkAEEVRKA 1190

                           90       100       110
                   ....*....|....*....|....*....|
gi 1799133487  276 AMLQKmqAEQNKHIAEVERQRSELEERFAR 305
Cdd:PTZ00121  1191 EELRK--AEDARKAEAARKAEEERKAEEAR 1218
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
211-308 8.52e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLriAEEKRLLEEQQRLREQMERERLAEI--KRLEEAARLEDERRIA---ADIEAQKQAmLQKMQaEQ 285
Cdd:PRK02224   539 AEELRERAAELEAE--AEEKREAAAEAEEEAEEAREEVAELnsKLAELKERIESLERIRtllAAIADAEDE-IERLR-EK 614

                           90       100
                   ....*....|....*....|....
gi 1799133487  286 NKHIAEVERQRSE-LEERFARVSQ 308
Cdd:PRK02224   615 REALAELNDERRErLAEKRERKRE 638
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-293 9.43e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 9.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDE----------RRIAADIEAQKQAMLQKM 281
Cdd:PRK09510    99 EQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEaeakraaaaaKKAAAEAKKKAEAEAAKK 178

                           90
                   ....*....|..
gi 1799133487  282 QAEQNKHIAEVE 293
Cdd:PRK09510   179 AAAEAKKKAEAE 190
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 213-302 1.08e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKRLRIAEEKRLL-----------EEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQK- 280
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLlqqsqeqwqaeKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERa 114

                           90       100
                   ....*....|....*....|....*...
gi 1799133487  281 -MQAEQNKH-----IAEVERQRSELEER 302
Cdd:pfam15558  115 rQEAEQRKQcqeqrLKEKEEELQALREQ 142
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 211-302 1.17e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.79  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEelkRLRIAEEKRlleeQQRLREQMERER-----------LAEIKR---LEEAARLEDERRIAADIE---AQ 273
Cdd:pfam15709  391 LRKQRLEEE---RQRQEEEER----KQRLQLQAAQERarqqqeefrrkLQELQRkkqQEEAERAEAEKQRQKELEmqlAE 463

                           90       100
                   ....*....|....*....|....*....
gi 1799133487  274 KQAMLQKMQAEQNkhiAEVERQRSELEER 302
Cdd:pfam15709  464 EQKRLMEMAEEER---LEYQRQKQEAEEK 489
PTZ00121 PTZ00121
MAEBL; Provisional
 213-301 1.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKRL---RIAEEKRLLEEQQR---LREQMERERLAEIKRLEEAARLEDERRI--------AADIEAQKQAML 278
Cdd:PTZ00121  1155 EIARKAEDARKAeeaRKAEDAKKAEAARKaeeVRKAEELRKAEDARKAEAARKAEEERKAeearkaedAKKAEAVKKAEE 1234

                           90       100
                   ....*....|....*....|...
gi 1799133487  279 QKMQAEQNKHiAEVERQRSELEE 301
Cdd:PTZ00121  1235 AKKDAEEAKK-AEEERNNEEIRK 1256
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 235-302 1.50e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 40.11  E-value: 1.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799133487  235 EQQRLREQMeRERLAEIKRLEEAARLEDERRI------AADIEAQKQAMLQKMQAEQNKHI-AEVERQRSELEER 302
Cdd:pfam16999    2 VSSRLLSEL-AEREAALDQQIEAARKEAEREVeaaeaeAARILREAEAKAKALQAEYRQELaAETARIREEARAR 75
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 212-301 1.70e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEE-LKRLRIAEEKRlleEQQRLREQMERERLAEIKRLEEAARLEDERRIAADiEAQKQAMLQKMQAEQ-NKHI 289
Cdd:TIGR02794   60 KPAAKKEQErQKKLEQQAEEA---EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAE-EKQKQAEEAKAKQAAeAKAK 135

                           90
                   ....*....|..
gi 1799133487  290 AEVERQRSELEE 301
Cdd:TIGR02794  136 AEAEAERKAKEE 147
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
212-302 1.73e-03

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: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRneELKRLRIAEEKRLLEE-QQRLREQMERER--------LAEIKRLEEAARLEDERRIAADIEAQkQAMLQKMQ 282
Cdd:COG2268    227 ELEQER--EIETARIAEAEAELAKkKAEERREAETARaeaeaayeIAEANAEREVQRQLEIAEREREIELQ-EKEAEREE 303

                           90       100
                   ....*....|....*....|...
gi 1799133487  283 AEQNKHI---AEVERQRSELEER 302
Cdd:COG2268    304 AELEADVrkpAEAEKQAAEAEAE 326
PDS5 pfam20168
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
 1296-1618 1.89e-03

Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.


Pssm-ID: 466319 [Multi-domain]  Cd Length: 1051  Bit Score: 43.35  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1296 VALRSKALKCLSSIIEADSSvlILEDVQQAVHTRMVDSHAQVRESAVELIGRFVLYDEEYV--RKYYSQIAERILDTGVA 1373
Cdd:pfam20168  298 VAVRIAWVEAAKQILLNHPD--LRSEILEALKDRLLDPDEKVRLAAVKAIGDLDYETLLHVvsEKLLKTLAERLRDKKPS 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1374 VRKRVIRIMREI----CEKFPT--------FEMIPD-MLarMIRRVTDEEgVKKLVFETFTT--LWFQPVD----TRIYT 1434
Cdd:pfam20168  376 VRKEALKTLAKLynvaYGEIEEgdeeaiekFGWIPNkIL--HLYYINDPE-IRALVERVLFEylLPALLDDeervKRLLT 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1435 -----NAVATKVTTMCSVAQHCIKDAMSDYLEqliLHIVKNGQEgSGMSVAVKQIIDSLVDHILNL--EQHKSSENV--- 1504
Cdd:pfam20168  453 llshlDEKAKKAFNAILKRQSRLQKALRKFLD---LCEKYNGVI-DDEEEEIKKKLEKIIQWLSASfpDPSKAEEDLqkf 528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1505 ---------------------------SEVELMRRKEQEEKymAYLSTLAVF-SKIRPLLL-TSHVEVLLPYLTFSGAKT 1555
Cdd:pfam20168  529 aklndkrlykllrtcidpdsdyktiekARKELLKRLGDSKS--SLLETLKLLlYRSSPLIVnKSSIPALLKLLRSSESGN 606

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799133487 1556 NAENQVTKEMIGMLERVIPLvpfpsniVLDSIDENLCKVIMFNGMALVVSAVSCVASIYKKFK 1618
Cdd:pfam20168  607 SELANESSELLKQISKVFPA-------VFKGHVKELVKLLKDEDPDVVEDALQALAKVGKKFP 662
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 212-302 2.22e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRiAEEKRLLEEQQRLREQMERERLAE---IKRLEEAARLEDERRIAADIEAQKQAMLQKMQA-EQNK 287
Cdd:pfam13868   62 EKEEERKEERKRYR-QELEEQIEEREQKRQEEYEEKLQEreqMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQA 140

                           90
                   ....*....|....*
gi 1799133487  288 HIAEVERQRSELEER 302
Cdd:pfam13868  141 EWKELEKEEEREEDE 155
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 1296-1385 2.53e-03

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 42.90  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487 1296 VALRSKALKCLSSIIEADSSvlILEDVQQAVHTRMVDSHAQVRESAVELIGRFVLYD-EEYV-RKYYSQIAERILDTGVA 1373
Cdd:cd19953    301 PEVRLAWVESAKHILLNHPD--LAEDILEALKKRLLDPDEKVRLAAVKAICDLAYEDlLHKVpEELLSTLAERLRDKKAS 378

                           90
                   ....*....|..
gi 1799133487 1374 VRKRVIRIMREI 1385
Cdd:cd19953    379 VRKEALQGLARL 390
PTZ00121 PTZ00121
MAEBL; Provisional
 189-308 2.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  189 EEQCRQ-------------IEKERKEQEERKRKQELEEQRKRNEelkrLRIAEEKRLLEEqqrLREQMERERLAEIKRLE 255
Cdd:PTZ00121  1239 AEEAKKaeeernneeirkfEEARMAHFARRQAAIKAEEARKADE----LKKAEEKKKADE---AKKAEEKKKADEAKKKA 1311

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1799133487  256 EAARLEDERRIAADiEAQKQAMLQKMQAEQNKHIAEVERQRSELEERFARVSQ 308
Cdd:PTZ00121  1312 EEAKKADEAKKKAE-EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
212-308 2.65e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAE 291
Cdd:COG3064     73 AEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKA 152

                           90
                   ....*....|....*..
gi 1799133487  292 VERQRSELEERFARVSQ 308
Cdd:COG3064    153 EAEAARAAAAAAAAAAA 169
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 211-301 3.09e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMER------ERLAEIKrlEEAARLEDERRIAADIEAQKQAMLQKMQAE 284
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeEEQLRVK--EKIGELEAEIASLERSIAEKERELEDAEER 323

                           90
                   ....*....|....*..
gi 1799133487  285 QNKHIAEVERQRSELEE 301
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEE 340
PTZ00121 PTZ00121
MAEBL; Provisional
 212-302 4.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLriAEEKRLLEEQQRLREQmERERLAEIKRLEEAARLEDERRIAAD-----IEAQKQAMlQKMQAEQN 286
Cdd:PTZ00121  1374 EEAKKKADAAKKK--AEEKKKADEAKKKAEE-DKKKADELKKAAAAKKKADEAKKKAEekkkaDEAKKKAE-EAKKADEA 1449

                           90
                   ....*....|....*.
gi 1799133487  287 KHIAEVERQRSELEER 302
Cdd:PTZ00121  1450 KKKAEEAKKAEEAKKK 1465
PTZ00121 PTZ00121
MAEBL; Provisional
 213-302 4.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKRlriAEEKRLLEEqqrLREQMERERLAEIKRLEEAARLEDERRIA---ADI--EAQKQAMLQKMQAEQNK 287
Cdd:PTZ00121  1531 EEAKKADEAKK---AEEKKKADE---LKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkAEEakKAEEARIEEVMKLYEEE 1604

                           90
                   ....*....|....*
gi 1799133487  288 HIAEVERQRSELEER 302
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAK 1619
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
211-300 4.16e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.17  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKRLLEEQQRLrEQMERER---LAEIKRLEEAARLEDERRIAAdiEAQKQAMLQKMQAEqnk 287
Cdd:COG2268    255 REAETARAEAEAAYEIAEANAEREVQRQL-EIAEREReieLQEKEAEREEAELEADVRKPA--EAEKQAAEAEAEAE--- 328

                           90
                   ....*....|...
gi 1799133487  288 hiAEVERQRSELE 300
Cdd:COG2268    329 --AEAIRAKGLAE 339
RNase_Y_N pfam12072
RNase Y N-terminal region;
211-301 4.29e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEELKRLRIAEEKrllEEQQRLREQMERE---RLAEIKRLEEaaRL-EDERRIAADIEA--QKQAMLQKMQAE 284
Cdd:pfam12072   40 IEEAKKEAETKKKEALLEAK---EEIHKLRAEAERElkeRRNELQRQER--RLlQKEETLDRKDESleKKEESLEKKEKE 114

                           90
                   ....*....|....*..
gi 1799133487  285 QNKHIAEVERQRSELEE 301
Cdd:pfam12072  115 LEAQQQQLEEKEEELEE 131
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 211-313 4.31e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 40.69  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEEL---KRLRIAEEKRLLEEQQRLREQMERERLAEIKRLEEAARLEDERriaadieaQKQAMLQKMQAEQ-- 285
Cdd:pfam06391   70 IEQYEKENKDLilkNKMKLSQEEEELEELLELEKREKEERRKEEKQEEEEEKEKKEK--------AKQELIDELMTSNkd 141

                           90       100
                   ....*....|....*....|....*....
gi 1799133487  286 -NKHIAEVERQRSELEERFARVSQPMTLV 313
Cdd:pfam06391  142 aEEIIAQHKKTAKKRKSERRRKLEELNRV 170
PTZ00121 PTZ00121
MAEBL; Provisional
 212-298 4.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKR---------LRIAEEKRLLEEQQRLRE--------QMERERLAEIKRLEEAARLEDERR--------I 266
Cdd:PTZ00121  1506 AEAKKKADEAKKaeeakkadeAKKAEEAKKADEAKKAEEkkkadelkKAEELKKAEEKKKAEEAKKAEEDKnmalrkaeE 1585

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1799133487  267 AADIEAQKQAMLQKMQAEQNKHIAEVERQRSE 298
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 212-280 5.89e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 39.65  E-value: 5.89e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLrIAEEKRLLEEQQRLREQMERERLAEIKR-LEEAARLEDERRiaADIEAQKQAMLQK 280
Cdd:pfam15346   74 EEERKKREELERI-LEENNRKIEEAQRKEAEERLAMLEEQRRmKEERQRREKEEE--EREKREQQKILNK 140
PTZ00121 PTZ00121
MAEBL; Provisional
 213-308 6.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  213 EQRKRNEELKR--LRIAEEKRLLEEqQRLREQM-----ERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQ 285
Cdd:PTZ00121  1567 EEAKKAEEDKNmaLRKAEEAKKAEE-ARIEEVMklyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645

                           90       100
                   ....*....|....*....|...
gi 1799133487  286 NKHIAEVERQRSELEERFARVSQ 308
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAAEEAK 1668
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
212-304 6.65e-03

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 39.99  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQ-----QRLREQM---ERERLAEIKRLEEAARLEDE-RRIAADIEAQKQAMLQKMQ 282
Cdd:pfam03280   55 EEEAYDRYALERLAIAQDSALSAEEkqqrlAALRAQLpedLRAAREAQQRLQELAARTAQlQKAGASPQQLRQARAQLVG 134

                           90       100
                   ....*....|....*....|..
gi 1799133487  283 AEQNKHIAEVERQRSELEERFA 304
Cdd:pfam03280  135 PEAAQRLAALDQQRAAWQQRLD 156
DUF5384 pfam17358
Family of unknown function (DUF5384); This is a family of unknown function found in ...
 212-306 7.51e-03

Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.


Pssm-ID: 407453 [Multi-domain]  Cd Length: 145  Bit Score: 39.20  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKRLRIAEEKRLLEEQQRlreQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQAEQNKHIaE 291
Cdd:pfam17358    1 EQQGKEDRVAAERQAAYEREWEEEQAR---AEAAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRAL-E 76

                           90
                   ....*....|....*
gi 1799133487  292 VERQRSELEERFARV 306
Cdd:pfam17358   77 IEERKLALAAQKARA 91
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 211-316 7.76e-03

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 41.28  E-value: 7.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRK-----RNEELKRL---RIAEEKRLLEEQQR----LREQMERERLAEIKRLEEAA--RLEDErriaadIEAQKQA 276
Cdd:pfam09731  318 LEKQKEeldklAEELSARLeevRAADEAQLRLEFERereeIRESYEEKLRTELERQAEAHeeHLKDV------LVEQEIE 391

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1799133487  277 MLQKMQAEQNKHIAEvER--QRSELEERFARVSQPMTLVGTH 316
Cdd:pfam09731  392 LQREFLQDIKEKVEE-ERagRLLKLNELLANLKGLEKATSSH 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-300 7.82e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  167 QIQSAASSIFDSSVISSHQKLYEEQCRQIEKERKEQEERKRKQELEEQRKRNEELKRLRIAEEKRLLEEQQRLREQMERE 246
Cdd:COG1196    654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1799133487  247 RLAEIKRLEEAARLEDERRIAADIEAQKqamlqkmQAEQNKHIAEVERQRSELE 300
Cdd:COG1196    734 REELLEELLEEEELLEEEALEELPEPPD-------LEELERELERLEREIEALG 780
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
211-305 7.84e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.18  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  211 LEEQRKRNEEL-KRLRIAEEKRLL--EEQQRLREQMERERLAEIKRLEEAarlEDErriAADIEAQKQAMLQKMQAEQNK 287
Cdd:COG3064      4 ALEEKAAEAAAqERLEQAEAEKRAaaEAEQKAKEEAEEERLAELEAKRQA---EEE---AREAKAEAEQRAAELAAEAAK 77

                           90
                   ....*....|....*...
gi 1799133487  288 HIAEVERQRSELEERFAR 305
Cdd:COG3064     78 KLAEAEKAAAEAEKKAAA 95
PTZ00121 PTZ00121
MAEBL; Provisional
 209-308 8.86e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  209 QELEEQRKRNEELKR----LRIAEEKRLLEEQQRLREQMERERLAEIKRLEE------AARLEDERRIAADIEAQKQAML 278
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVI 1781

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1799133487  279 QK-MQAEQNKHIAEVERQRSELEERFARVSQ 308
Cdd:PTZ00121  1782 EEeLDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 212-300 9.18e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.60  E-value: 9.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEElKRLRIAEEKRLLEEQ--QRLREQMERERLAEIKRLEEAARLEDERRIAADIEAQKQAMLQKMQ--AEQNK 287
Cdd:TIGR02794   87 EQARQKELE-QRAAAEKAAKQAEQAakQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAkaAAEAK 165

                           90
                   ....*....|...
gi 1799133487  288 HIAEVERQRSELE 300
Cdd:TIGR02794  166 KKAEEAKKKAEAE 178
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 225-309 9.58e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  225 RIAE-EKRLLEEQQRLREQMERERL---AEIKRLEEA-ARLEDERRIAADIEAQKQAMLQKMQAEQNKHIAEVERQRSEL 299
Cdd:COG3883    126 KIADaDADLLEELKADKAELEAKKAeleAKLAELEALkAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205

                           90
                   ....*....|
gi 1799133487  300 EERFARVSQP 309
Cdd:COG3883    206 AAAEAAAAAA 215
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 212-302 9.98e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 41.26  E-value: 9.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133487  212 EEQRKRNEELKR----LRIAEEKRLLEEQQRLREQMERERLAEIKRLE-EAARLEDERRIAADIEAQKQAMLQKMQAEQn 286
Cdd:PTZ00266   436 ERARIEKENAHRkaleMKILEKKRIERLEREERERLERERMERIERERlERERLERERLERDRLERDRLDRLERERVDR- 514

                           90
                   ....*....|....*.
gi 1799133487  287 khiaeVERQRSELEER 302
Cdd:PTZ00266   515 -----LERDRLEKARR 525
 
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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