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Conserved domains on  [gi|124512056|ref|XP_001349161|]
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DNA mismatch repair protein PMS1, putative [Plasmodium falciparum 3D7]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mutl super family cl36694
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-317 2.89e-81

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00585:

Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 269.51  E-value: 2.89e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056     1 MKIKNIGEESIHNICSSQVIFTLSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKI 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056    81 KDFNDIHsSLNTLGFRGEALNSLCMLSNVNITTKNEENDH-AYLLKFDklGRLYHE-EPIARLRGTTVSCENIFHNIPIR 158
Cdd:TIGR00585   81 QSFEDLE-RIETLGFRGEALASISSVSRLTITTKTSAADGlAYQALLE--GGMIESiKPAPRPVGTTVEVRDLFYNLPVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   159 KKdFIKNIKTQVSDLLLLMQQYAIIYHNIKFVIYNIvtskgcTKNMNLLITNGTDSIKKNFY-SIYGKRNIGNLIEFN-I 236
Cdd:TIGR00585  158 RK-FLKSPKKEFRKILDVLQRYALIHPDISFSLTHD------GKKVLQLSTKPNQSTKENRIrSVFGTAVLRKLIPLDeW 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   237 DGNEWNIRGYISDSNSGRRDKDL-QFYYINSRPIHiLKNVNKLINTIYREFNSRL-YPIIICNILSDTKNIDINVTPDKR 314
Cdd:TIGR00585  231 EDLDLQLEGFISQPNVTRSRRSGwQFLFINGRPVE-LKLLLKAIREVYHEYLPKGqYPVFVLNLEIDPELVDVNVHPDKK 309


                   ...
gi 124512056   315 EVF 317
Cdd:TIGR00585  310 EVR 312
MutL super family cl33837
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1065-1268 4.03e-17

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0323:

Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 86.25  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1065 LFIIDQHAADEKSNFEKYNKIF---TMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVqileepihkrrktnnnni 1141
Cdd:COG0323   347 LVLIDQHAAHERILYERLKKALaegGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI------------------ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1142 nEPIDDEEemlmelnVYLLSLPVFNGKILEVVDFMSLLHHLTEHpvasynESEVSVKTTIDlnnktdtwfnynfprpqkv 1221
Cdd:COG0323   409 -EPFGPNT-------VAVRAVPALLGEGDAEELLRDLLDELAEE------GSSESLEELRE------------------- 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124512056 1222 wRILASKACRNAIMVGKALNIYEMIKIKKKLSFLKNPWNCPHGRPTI 1268
Cdd:COG0323   456 -ELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTW 501
KLF18_N super family cl40479
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-852 5.12e-10

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


The actual alignment was detected with superfamily member cd21575:

Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 62.01  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  706 NIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNND 785
Cdd:cd21575    45 TLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTS 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124512056  786 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPYLnGQ 852
Cdd:cd21575   125 SGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLYGGQMTTSSGDQTLYGGQMTTSTSNQTLYG-GQ 190
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-317 2.89e-81

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 269.51  E-value: 2.89e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056     1 MKIKNIGEESIHNICSSQVIFTLSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKI 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056    81 KDFNDIHsSLNTLGFRGEALNSLCMLSNVNITTKNEENDH-AYLLKFDklGRLYHE-EPIARLRGTTVSCENIFHNIPIR 158
Cdd:TIGR00585   81 QSFEDLE-RIETLGFRGEALASISSVSRLTITTKTSAADGlAYQALLE--GGMIESiKPAPRPVGTTVEVRDLFYNLPVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   159 KKdFIKNIKTQVSDLLLLMQQYAIIYHNIKFVIYNIvtskgcTKNMNLLITNGTDSIKKNFY-SIYGKRNIGNLIEFN-I 236
Cdd:TIGR00585  158 RK-FLKSPKKEFRKILDVLQRYALIHPDISFSLTHD------GKKVLQLSTKPNQSTKENRIrSVFGTAVLRKLIPLDeW 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   237 DGNEWNIRGYISDSNSGRRDKDL-QFYYINSRPIHiLKNVNKLINTIYREFNSRL-YPIIICNILSDTKNIDINVTPDKR 314
Cdd:TIGR00585  231 EDLDLQLEGFISQPNVTRSRRSGwQFLFINGRPVE-LKLLLKAIREVYHEYLPKGqYPVFVLNLEIDPELVDVNVHPDKK 309


                   ...
gi 124512056   315 EVF 317
Cdd:TIGR00585  310 EVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 10-193 1.84e-77

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 253.51  E-value: 1.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   10 SIHNICSSQVIFTLSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKIKDFNDIHsS 89
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLF-S 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   90 LNTLGFRGEALNSLCMLSNVNITTKNEENDHAYLLKFDKLGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKTQ 169
Cdd:cd16926    80 ITTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTE 158

                         170       180
                  ....*....|....*....|....
gi 124512056  170 VSDLLLLMQQYAIIYHNIKFVIYN 193
Cdd:cd16926   159 LSKILDLVQRLALAHPDVSFSLTH 182
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
24-323 4.99e-65

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 229.93  E-value: 4.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   24 SSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKK----INFEnicaRHATSKIKDFNDIHsSLNTLGFRGEA 99
Cdd:COG0323    25 ASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPedlpLAFE----RHATSKIRSAEDLF-RIRTLGFRGEA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  100 LNSLCMLSNVNITTKNEENDHAYLLKFDKlGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKT---QVSDlllL 176
Cdd:COG0323   100 LASIASVSRLTLTTRTAGAELGTRIEVEG-GKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDATelaHITD---V 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  177 MQQYAIIYHNIKFVIYNivtskgctKNMNLLITNGTDSIKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRD 256
Cdd:COG0323   175 VRRLALAHPDIAFTLIH--------NGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSRSN 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512056  257 KDLQFYYINSRPIHilknvNKLINTIYRE-FNSRL----YPIIICNILSDTKNIDINVTPDKREVFFTFEQE 323
Cdd:COG0323   247 RDYQYFFVNGRPVR-----DKLLSHAVREaYRDLLpkgrYPVAVLFLELDPELVDVNVHPTKTEVRFRDERE 313
mutL PRK00095
DNA mismatch repair endonuclease MutL;
23-326 9.06e-55

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 202.75  E-value: 9.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   23 LSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKIKDFNDIHsSLNTLGFRGEALNS 102
Cdd:PRK00095   23 PASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIASLDDLE-AIRTLGFRGEALPS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  103 LCMLSNVNITTKNEENDHAYLLKFDKlGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKTQVSDLLLLMQQYAI 182
Cdd:PRK00095  102 IASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGTTIEVRDLFFNTPARRK-FLKSEKTELGHIDDVVNRLAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  183 IYHNIKFViyniVTSKGctKNMnlLITNGTDSIKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFY 262
Cdd:PRK00095  180 AHPDVAFT----LTHNG--KLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYL 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512056  263 YINSRPIHilknvNKLIN-TI---YREFNSR-LYPIIICNILSDTKNIDINVTPDKREVFFTFEQEMCE 326
Cdd:PRK00095  252 FVNGRYVR-----DKLLNhAIrqaYHDLLPRgRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHD 315
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 220-335 1.44e-26

DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain of the mutL/hexB/PMS1 family. This domain has a ribosomal S5 domain 2-like fold.


Pssm-ID: 426060 [Multi-domain]  Cd Length: 117  Bit Score: 105.66  E-value: 1.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   220 YSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFYYINSRPIHiLKNVNKLINTIYREF-NSRLYPIIICNI 298
Cdd:pfam01119    1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVR-DKLLSHAIREAYRDLlPKGRYPVAVLFL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 124512056   299 LSDTKNIDINVTPDKREVFFTFEQEMCEHMKTALVKL 335
Cdd:pfam01119   80 EIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREA 116
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1065-1268 4.03e-17

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 86.25  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1065 LFIIDQHAADEKSNFEKYNKIF---TMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVqileepihkrrktnnnni 1141
Cdd:COG0323   347 LVLIDQHAAHERILYERLKKALaegGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI------------------ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1142 nEPIDDEEemlmelnVYLLSLPVFNGKILEVVDFMSLLHHLTEHpvasynESEVSVKTTIDlnnktdtwfnynfprpqkv 1221
Cdd:COG0323   409 -EPFGPNT-------VAVRAVPALLGEGDAEELLRDLLDELAEE------GSSESLEELRE------------------- 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124512056 1222 wRILASKACRNAIMVGKALNIYEMIKIKKKLSFLKNPWNCPHGRPTI 1268
Cdd:COG0323   456 -ELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTW 501
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1065-1239 4.18e-17

MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.


Pssm-ID: 214857 [Multi-domain]  Cd Length: 140  Bit Score: 79.32  E-value: 4.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   1065 LFIIDQHAADEKSNFEKY-NKIFTMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVQILEepihkrrktnnnnine 1143
Cdd:smart00853   18 LYLLDQHAAHERILYEQLlKQAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIFG---------------- 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   1144 piddeeemlmELNVYLLSLPVFNGKILEVVDFMSLLHHLTEHPVASynesevsvkttidlnnktdtwfnynfpRPQKVWR 1223
Cdd:smart00853   82 ----------PQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENA---------------------------RPSRLEA 124

                           170
                    ....*....|....*.
gi 124512056   1224 ILASKACRNAIMVGKA 1239
Cdd:smart00853  125 LLASLACRSAIRAGDA 140
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1065-1268 5.26e-12

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 70.25  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1065 LFIIDQHAADEKSNFEKY-NKI--FTMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVQILEEpihkrrktnnnni 1141
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQLkDKLaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGP------------- 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1142 nepiddeeemlmelNVYLL-SLPVFNGKILEVVDFMSLLHHLTEHPVAsynesevsvkttidlnnktdtwfnynfpRPQK 1220
Cdd:PRK00095  517 --------------NSFAVrEVPALLGQQELEELIRDLLDELAEEGDS----------------------------DTLK 554

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124512056 1221 VWRILASKACRNAIMVGKALNIYEMIKIKKKLSFLKNPWNCPHGRPTI 1268
Cdd:PRK00095  555 ERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTY 602
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1065-1240 3.11e-11

MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.


Pssm-ID: 430147  Cd Length: 145  Bit Score: 62.62  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  1065 LFIIDQHAADEKSNFEKYNKIF---TMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVqileepihkrrktnnnni 1141
Cdd:pfam08676   20 LYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL------------------ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  1142 nEPIDDEEEMLMELNVYllsLPVFNGKILevvdFMSLLHHLTEHPVASynesevsvkttidlnnktdtwfnynfpRPQKV 1221
Cdd:pfam08676   82 -EEFGPNSVIVRSVPAL---LRQQNLQEL----IRELLDELAEKGGSS---------------------------LEESL 126

                          170
                   ....*....|....*....
gi 124512056  1222 WRILASKACRNAIMVGKAL 1240
Cdd:pfam08676  127 EELLATMACHSAVRAGRRL 145
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-852 5.12e-10

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 62.01  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  706 NIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNND 785
Cdd:cd21575    45 TLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTS 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124512056  786 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPYLnGQ 852
Cdd:cd21575   125 SGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLYGGQMTTSSGDQTLYGGQMTTSTSNQTLYG-GQ 190
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 23-63 2.14e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 39.17  E-value: 2.14e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 124512056     23 LSSVVKELVENSIDA--DASEIKIKLVESGIKL-IEVNDNGVGI 63
Cdd:smart00387    6 LRQVLSNLLDNAIKYtpEGGRITVTLERDGDHVeITVEDNGPGI 49
PRK08581 PRK08581
amidase domain-containing protein;
670-863 2.50e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.08  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  670 LNSDDTKNNIYEYKLNNDDTKNNIyEYKLNNDDTKNNIYEYKLNNDDSNNTIYEYKlnNDDSNNTIYEYKLNNDDSNNTI 749
Cdd:PRK08581   31 QKDSTAKTTSHDSKKSNDDETSKD-TSSKDTDKADNNNTSNQDNNDKKFSTIDSST--SDSNNIIDFIYKNLPQTNINQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  750 YEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTiyeyklNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDS 829
Cdd:PRK08581  108 LTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTND------SNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNN 181

                         170       180       190
                  ....*....|....*....|....*....|....
gi 124512056  830 NNTIYEYKLNSDDSNNTPYLNGQEKNEETEEGND 863
Cdd:PRK08581  182 TKPSTSNKQPNSPKPTQPNQSNSQPASDDTANQK 215
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-317 2.89e-81

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 269.51  E-value: 2.89e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056     1 MKIKNIGEESIHNICSSQVIFTLSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKI 80
Cdd:TIGR00585    1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056    81 KDFNDIHsSLNTLGFRGEALNSLCMLSNVNITTKNEENDH-AYLLKFDklGRLYHE-EPIARLRGTTVSCENIFHNIPIR 158
Cdd:TIGR00585   81 QSFEDLE-RIETLGFRGEALASISSVSRLTITTKTSAADGlAYQALLE--GGMIESiKPAPRPVGTTVEVRDLFYNLPVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   159 KKdFIKNIKTQVSDLLLLMQQYAIIYHNIKFVIYNIvtskgcTKNMNLLITNGTDSIKKNFY-SIYGKRNIGNLIEFN-I 236
Cdd:TIGR00585  158 RK-FLKSPKKEFRKILDVLQRYALIHPDISFSLTHD------GKKVLQLSTKPNQSTKENRIrSVFGTAVLRKLIPLDeW 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   237 DGNEWNIRGYISDSNSGRRDKDL-QFYYINSRPIHiLKNVNKLINTIYREFNSRL-YPIIICNILSDTKNIDINVTPDKR 314
Cdd:TIGR00585  231 EDLDLQLEGFISQPNVTRSRRSGwQFLFINGRPVE-LKLLLKAIREVYHEYLPKGqYPVFVLNLEIDPELVDVNVHPDKK 309


                   ...
gi 124512056   315 EVF 317
Cdd:TIGR00585  310 EVR 312
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 10-193 1.84e-77

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 253.51  E-value: 1.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   10 SIHNICSSQVIFTLSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKIKDFNDIHsS 89
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLF-S 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   90 LNTLGFRGEALNSLCMLSNVNITTKNEENDHAYLLKFDKLGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKTQ 169
Cdd:cd16926    80 ITTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVGTTVTVRDLFYNTPARRK-FLKSPKTE 158

                         170       180
                  ....*....|....*....|....
gi 124512056  170 VSDLLLLMQQYAIIYHNIKFVIYN 193
Cdd:cd16926   159 LSKILDLVQRLALAHPDVSFSLTH 182
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
24-323 4.99e-65

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 229.93  E-value: 4.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   24 SSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKK----INFEnicaRHATSKIKDFNDIHsSLNTLGFRGEA 99
Cdd:COG0323    25 ASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPedlpLAFE----RHATSKIRSAEDLF-RIRTLGFRGEA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  100 LNSLCMLSNVNITTKNEENDHAYLLKFDKlGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKT---QVSDlllL 176
Cdd:COG0323   100 LASIASVSRLTLTTRTAGAELGTRIEVEG-GKVVEVEPAAAPKGTTVEVRDLFFNTPARRK-FLKSDATelaHITD---V 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  177 MQQYAIIYHNIKFVIYNivtskgctKNMNLLITNGTDSIKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRD 256
Cdd:COG0323   175 VRRLALAHPDIAFTLIH--------NGREVFQLPGAGDLLQRIAAIYGREFAENLLPVEAEREGLRLSGYIGKPEFSRSN 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512056  257 KDLQFYYINSRPIHilknvNKLINTIYRE-FNSRL----YPIIICNILSDTKNIDINVTPDKREVFFTFEQE 323
Cdd:COG0323   247 RDYQYFFVNGRPVR-----DKLLSHAVREaYRDLLpkgrYPVAVLFLELDPELVDVNVHPTKTEVRFRDERE 313
mutL PRK00095
DNA mismatch repair endonuclease MutL;
23-326 9.06e-55

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 202.75  E-value: 9.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   23 LSSVVKELVENSIDADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSKIKDFNDIHsSLNTLGFRGEALNS 102
Cdd:PRK00095   23 PASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATSKIASLDDLE-AIRTLGFRGEALPS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  103 LCMLSNVNITTKNEENDHAYLLKFDKlGRLYHEEPIARLRGTTVSCENIFHNIPIRKKdFIKNIKTQVSDLLLLMQQYAI 182
Cdd:PRK00095  102 IASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGTTIEVRDLFFNTPARRK-FLKSEKTELGHIDDVVNRLAL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  183 IYHNIKFViyniVTSKGctKNMnlLITNGTDSIKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFY 262
Cdd:PRK00095  180 AHPDVAFT----LTHNG--KLV--LQTRGAGQLLQRLAAILGREFAENALPIDAEHGDLRLSGYVGLPTLSRANRDYQYL 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512056  263 YINSRPIHilknvNKLIN-TI---YREFNSR-LYPIIICNILSDTKNIDINVTPDKREVFFTFEQEMCE 326
Cdd:PRK00095  252 FVNGRYVR-----DKLLNhAIrqaYHDLLPRgRYPAFVLFLELDPHQVDVNVHPAKHEVRFRDERLVHD 315
MutL_Trans_hPMS_2_like cd03484
MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 214-336 3.35e-39

MutL_Trans_hPMS2_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM2 (hPSM2). hPSM2 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to yeast PMS1. The yeast MLH1-PMS1 and the human MLH1-PMS2 heterodimers play a role in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Cells lacking hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome.


Pssm-ID: 239566 [Multi-domain]  Cd Length: 142  Bit Score: 142.41  E-value: 3.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  214 SIKKNFYSIYGKRNIGNLIEFNID-----------------GNEWNIRGYIS--DSNSGRRDKDLQFYYINSRPIHiLKN 274
Cdd:cd03484     1 DIKDNIINVFGGKVIKGLIPINLEldvnptkeeldsdedlaDSEVKITGYISkpSHGCGRSSSDRQFFYINGRPVD-LKK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512056  275 VNKLINTIYREFNSRLYPIIICNILSDTKNIDINVTPDKREVFFTFEQEMCEHMKTALVKLF 336
Cdd:cd03484    80 VAKLINEVYKSFNSRQYPFFILNISLPTSLYDVNVTPDKRTVLLHDEDRLIDTLKTSLSELF 141
MutL_Trans cd00782
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 215-336 3.36e-32

MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. Included in this group are proteins similar to human MLH1, hPMS2, hPMS1, hMLH3 and E. coli MutL, MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hPMS2 causes predisposition to HPNCC and Turcot syndrome. Mutation in hMLH1 accounts for a large fraction of HNPCC families. There is no convincing evidence to support hPMS1 having a role in HNPCC predisposition. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH.


Pssm-ID: 238405 [Multi-domain]  Cd Length: 122  Bit Score: 121.88  E-value: 3.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  215 IKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFYYINSRPIHiLKNVNKLINTIYREFNS-RLYPI 293
Cdd:cd00782     1 LKDRIAQVYGKEVAKNLIEVELESGDFRISGYISKPDFGRSSKDRQFLFVNGRPVR-DKLLSKAINEAYRSYLPkGRYPV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 124512056  294 IICNILSDTKNIDINVTPDKREVFFTFEQEMCEHMKTALVKLF 336
Cdd:cd00782    80 FVLNLELPPELVDVNVHPTKREVRFSDEEEVLELIREALRSAL 122
DNA_mis_repair pfam01119
DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain ...
 220-335 1.44e-26

DNA mismatch repair protein, C-terminal domain; This family represents the C-terminal domain of the mutL/hexB/PMS1 family. This domain has a ribosomal S5 domain 2-like fold.


Pssm-ID: 426060 [Multi-domain]  Cd Length: 117  Bit Score: 105.66  E-value: 1.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   220 YSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFYYINSRPIHiLKNVNKLINTIYREF-NSRLYPIIICNI 298
Cdd:pfam01119    1 AAIYGKEFAENLLPIEKEDDGLRLSGYISKPTLSRSNRDYQYLFVNGRPVR-DKLLSHAIREAYRDLlPKGRYPVAVLFL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 124512056   299 LSDTKNIDINVTPDKREVFFTFEQEMCEHMKTALVKL 335
Cdd:pfam01119   80 EIDPELVDVNVHPTKREVRFRDEREVYDFIKEALREA 116
TopoII_MutL_Trans cd00329
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ...
 215-317 5.27e-20

MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.


Pssm-ID: 238202 [Multi-domain]  Cd Length: 107  Bit Score: 86.55  E-value: 5.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  215 IKKNFYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFYYINSRPIHILKNVNKLINTIYREF----NSRL 290
Cdd:cd00329     1 LKDRLAEILGDKVADKLIYVEGESDGFRVEGAISYPDSGRSSKDRQFSFVNGRPVREGGTHVKAVREAYTRAlngdDVRR 80

                          90       100
                  ....*....|....*....|....*..
gi 124512056  291 YPIIICNILSDTKNIDINVTPDKREVF 317
Cdd:cd00329    81 YPVAVLSLKIPPSLVDVNVHPTKEEVR 107
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
1065-1268 4.03e-17

DNA mismatch repair ATPase MutL [Replication, recombination and repair];


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 86.25  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1065 LFIIDQHAADEKSNFEKYNKIF---TMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVqileepihkrrktnnnni 1141
Cdd:COG0323   347 LVLIDQHAAHERILYERLKKALaegGVASQPLLIPETLELSPAEAALLEEHLEELARLGFEI------------------ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1142 nEPIDDEEemlmelnVYLLSLPVFNGKILEVVDFMSLLHHLTEHpvasynESEVSVKTTIDlnnktdtwfnynfprpqkv 1221
Cdd:COG0323   409 -EPFGPNT-------VAVRAVPALLGEGDAEELLRDLLDELAEE------GSSESLEELRE------------------- 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 124512056 1222 wRILASKACRNAIMVGKALNIYEMIKIKKKLSFLKNPWNCPHGRPTI 1268
Cdd:COG0323   456 -ELLATMACHGAIKAGRRLSLEEMNALLRDLEATENPYTCPHGRPTW 501
MutL_C smart00853
MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair ...
 1065-1239 4.18e-17

MutL C terminal dimerisation domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognises mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerisation.


Pssm-ID: 214857 [Multi-domain]  Cd Length: 140  Bit Score: 79.32  E-value: 4.18e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   1065 LFIIDQHAADEKSNFEKY-NKIFTMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVQILEepihkrrktnnnnine 1143
Cdd:smart00853   18 LYLLDQHAAHERILYEQLlKQAGGLESQPLLIPVRLELSPQEAALLEEHLELLRQLGFELEIFG---------------- 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056   1144 piddeeemlmELNVYLLSLPVFNGKILEVVDFMSLLHHLTEHPVASynesevsvkttidlnnktdtwfnynfpRPQKVWR 1223
Cdd:smart00853   82 ----------PQSLILRSVPALLRQQNLQKLIPELLDLLSDEEENA---------------------------RPSRLEA 124

                           170
                    ....*....|....*.
gi 124512056   1224 ILASKACRNAIMVGKA 1239
Cdd:smart00853  125 LLASLACRSAIRAGDA 140
mutL PRK00095
DNA mismatch repair endonuclease MutL;
1065-1268 5.26e-12

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 70.25  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1065 LFIIDQHAADEKSNFEKY-NKI--FTMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVQILEEpihkrrktnnnni 1141
Cdd:PRK00095  450 LYLVDQHAAHERLLYEQLkDKLaeVGLASQPLLIPLVLELSEDEADRLEEHKELLARLGLELEPFGP------------- 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056 1142 nepiddeeemlmelNVYLL-SLPVFNGKILEVVDFMSLLHHLTEHPVAsynesevsvkttidlnnktdtwfnynfpRPQK 1220
Cdd:PRK00095  517 --------------NSFAVrEVPALLGQQELEELIRDLLDELAEEGDS----------------------------DTLK 554

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 124512056 1221 VWRILASKACRNAIMVGKALNIYEMIKIKKKLSFLKNPWNCPHGRPTI 1268
Cdd:PRK00095  555 ERELLATMACHGAIRAGRRLTLEEMNALLRQLEATENPGTCPHGRPTY 602
MutL_Trans_hPMS_1_like cd03485
MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 214-336 1.97e-11

MutL_Trans_hPMS1_like: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to human PSM1 (hPSM1) and yeast MLH2. hPSM1 and yMLH2 are members of the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. PMS1 forms a heterodimer with MLH1. The MLH1-PMS1 complex functions in meiosis. Loss of yMLH2 results in a small but significant decrease in spore viability and a significant increase in gene conversion frequencies. A role for hMLH1-hPMS1 in DNA mismatch repair has not been established. Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families, however there is no convincing evidence to support hPMS1 having a role in HNPCC predisposition.


Pssm-ID: 239567 [Multi-domain]  Cd Length: 132  Bit Score: 62.67  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  214 SIKKNFYSIYGKRNIGNLIEFNIDGN--EWNIRGYI----SDSNSGRRDKdlQFYYINSRPIHILKNVNKLIN----TIY 283
Cdd:cd03485     1 DHKEALARVLGTAVAANMVPVQSTDEdpQISLEGFLpkpgSDVSKTKSDG--KFISVNSRPVSLGKDIGKLLRqyysSAY 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124512056  284 REFNSRLYPIIICNILSDTKNIDINVTPDKREVFFTFEQEMCEHMKTALVKLF 336
Cdd:cd03485    79 RKSSLRRYPVFFLNILCPPGLVDVNIEPDKDDVLLQNKEAVLQAVENLLESLY 131
MutL_C pfam08676
MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair ...
 1065-1240 3.11e-11

MutL C terminal dimerization domain; MutL and MutS are key components of the DNA repair machinery that corrects replication errors. MutS recognizes mispaired or unpaired bases in a DNA duplex and in the presence of ATP, recruits MutL to form a DNA signaling complex for repair. The N terminal region of MutL contains the ATPase domain and the C terminal is involved in dimerization.


Pssm-ID: 430147  Cd Length: 145  Bit Score: 62.62  E-value: 3.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  1065 LFIIDQHAADEKSNFEKYNKIF---TMKSQKLISKIHVQVSPAQVHIIQKYMSIFLQNGFEVqileepihkrrktnnnni 1141
Cdd:pfam08676   20 LYLIDQHAAHERILYEKLKRALaegGLAAQPLLIPLVLELSPEEAALLEEHKEELAQLGFEL------------------ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  1142 nEPIDDEEEMLMELNVYllsLPVFNGKILevvdFMSLLHHLTEHPVASynesevsvkttidlnnktdtwfnynfpRPQKV 1221
Cdd:pfam08676   82 -EEFGPNSVIVRSVPAL---LRQQNLQEL----IRELLDELAEKGGSS---------------------------LEESL 126

                          170
                   ....*....|....*....
gi 124512056  1222 WRILASKACRNAIMVGKAL 1240
Cdd:pfam08676  127 EELLATMACHSAVRAGRRL 145
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-852 5.12e-10

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 62.01  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  706 NIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNND 785
Cdd:cd21575    45 TLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTS 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124512056  786 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPYLnGQ 852
Cdd:cd21575   125 SGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLYGGQMTTSSGDQTLYGGQMTTSTSNQTLYG-GQ 190
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 692-861 1.51e-09

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 60.47  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  692 NIYEYKLNNDDTKNNIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNND 771
Cdd:cd21575    45 TLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  772 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTpYLNG 851
Cdd:cd21575   125 SGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLYGGQMTTSSGDQTLYGGQMTTSTSNQTLYGGQMTTSSGNQT-LYGG 203

                         170
                  ....*....|
gi 124512056  852 QEKNEETEEG 861
Cdd:cd21575   204 QMTTPITLSG 213
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 716-848 1.20e-08

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 57.77  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  716 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYK 795
Cdd:cd21575    41 FSEQTLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQ 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124512056  796 LNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPY 848
Cdd:cd21575   121 MTTSSGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLYGGQMTTSSGDQTLY 173
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-848 3.90e-07

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 53.15  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  706 NIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNND 785
Cdd:cd21575    17 TLYGGQMTTPSGDQTLYGGQMTTSFSEQTLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTSTGNQTLYGGQMTTS 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124512056  786 DSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPY 848
Cdd:cd21575    97 GSDQTLYGGQMTTSSGDQTLYGGQMTTSSGDQTLYGGQMTTSTGDQTLYGGQMTTSTGDQTLY 159
MutL_Trans_MLH1 cd03483
MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 214-326 1.48e-06

MutL_Trans_MLH1: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH1 (MutL homologue 1). This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with PMS2, PMS1 and MLH3. These three complexes have distinct functions in meiosis. hMLH1-hPMS2 also participates in the repair of all DNA mismatch repair (MMR) substrates. Roles for hMLH1-hPMS1 or hMLH1-hMLH3 in MMR have not been established. Cells lacking hMLH1 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 causes predisposition to HNPCC, Muir-Torre syndrome and Turcot syndrome (HNPCC variant). Mutation in hMLH1 accounts for a large fraction of HNPCC families.


Pssm-ID: 239565 [Multi-domain]  Cd Length: 127  Bit Score: 48.77  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  214 SIKKNFYSIYGKRNIGNLIEFNIDGNE----WNIRGYISDSNSGRRdKDLQFYYINSRPIHiLKNVNKLINTIYREF-NS 288
Cdd:cd03483     1 STKDNIRSVYGAAVANELIEVEISDDDddlgFKVKGLISNANYSKK-KIIFILFINNRLVE-CSALRRAIENVYANYlPK 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124512056  289 RLYPIIICNILSDTKNIDINVTPDKREVFFTFEQEMCE 326
Cdd:cd03483    79 GAHPFVYLSLEIPPENVDVNVHPTKREVHFLNEEEIIE 116
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 23-117 1.54e-06

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 48.87  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056    23 LSSVVKELVENSIDADASEIKIKLV--ESGIKLIEVNDNGVGIKKINFENICARHATSKikdfnDIHSSLNTLGFRG--E 98
Cdd:pfam13589    1 LEGALAELIDNSIDADATNIKIEVNknRGGGTEIVIEDDGHGMSPEELINALRLATSAK-----EAKRGSTDLGRYGigL 75

                           90
                   ....*....|....*....
gi 124512056    99 ALNSLCMLSNVNITTKNEE 117
Cdd:pfam13589   76 KLASLSLGAKLTVTSKKEG 94
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 718-850 1.89e-06

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 51.23  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  718 NNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLN 797
Cdd:cd21575     1 DQTLYGSQMTTSSGDQTLYGGQMTTPSGDQTLYGGQMTTSFSEQTLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124512056  798 NDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNSDDSNNTPYLN 850
Cdd:cd21575    81 TSTGNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTSSGDQTLYGG 133
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 707-834 5.94e-06

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 49.69  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  707 IYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDD 786
Cdd:cd21575     4 LYGSQMTTSSGDQTLYGGQMTTPSGDQTLYGGQMTTSFSEQTLYGGQMTTPSGDQTLYGGQMTTPNGNQTLYGGQMTTST 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 124512056  787 SNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTIY 834
Cdd:cd21575    84 GNQTLYGGQMTTSGSDQTLYGGQMTTSSGDQTLYGGQMTTSSGDQTLY 131
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 23-79 1.12e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 45.82  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512056    23 LSSVVKELVENSID--ADASEIKIKLVESGIKLIEVNDNGVGIKKINFENICARHATSK 79
Cdd:pfam02518    6 LRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
MutL_Trans_MutL cd03482
MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 219-318 2.71e-04

MutL_Trans_MutL: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to Escherichia coli MutL. EcMutL belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from the ATP-binding site to the DNA breakage/reunion regions of the enzymes. It has been suggested that during initiation of DNA mismatch repair in E. coli, the mismatch recognition protein MutS recruits MutL in the presence of ATP. The MutS(ATP)-MutL ternary complex formed, then recruits the latent endonuclease MutH. Prokaryotic MutS and MutL are homodimers.


Pssm-ID: 239564 [Multi-domain]  Cd Length: 123  Bit Score: 42.19  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  219 FYSIYGKRNIGNLIEFNIDGNEWNIRGYISDSNSGRRDKDLQFYYINSRpihILKnvNKLIN----TIYREFNSR-LYPI 293
Cdd:cd03482     5 LADILGEDFAEQALAIDEEAGGLRLSGWIALPTFARSQADIQYFYVNGR---MVR--DKLIShavrQAYSDVLHGgRHPA 79

                          90       100
                  ....*....|....*....|....*
gi 124512056  294 IICNILSDTKNIDINVTPDKREVFF 318
Cdd:cd03482    80 YVLYLELDPAQVDVNVHPAKHEVRF 104
MutL_Trans_MLH3 cd03486
MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in ...
 219-284 5.18e-04

MutL_Trans_MLH3: transducer domain, having a ribosomal S5 domain 2-like fold, found in proteins similar to yeast and human MLH3 (MutL homologue 3). MLH3 belongs to the DNA mismatch repair (MutL/MLH1/PMS2) family. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. MLH1 forms heterodimers with MLH3. The MLH1-MLH3 complex plays a role in meiosis. A role for hMLH1-hMLH3 in DNA mismatch repair (MMR) has not been established. It has been suggested that hMLH3 may be a low risk gene for colorectal cancer; however there is little evidence to support it having a role in classical HNPCC.


Pssm-ID: 239568 [Multi-domain]  Cd Length: 141  Bit Score: 41.53  E-value: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124512056  219 FYSIYGKRNIGNLIEFNIDGNEWNIRGYISdsNSGRRDKDLQFYYINSRPIHILKnVNKLINTIYR 284
Cdd:cd03486     6 FKQIYGLVLAQKLKEVSAKFQEYEVSGYIS--SEGHYSKSFQFIYVNGRLYLKTR-FHKLINKLFR 68
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 23-63 2.14e-03

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 39.17  E-value: 2.14e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 124512056     23 LSSVVKELVENSIDA--DASEIKIKLVESGIKL-IEVNDNGVGI 63
Cdd:smart00387    6 LRQVLSNLLDNAIKYtpEGGRITVTLERDGDHVeITVEDNGPGI 49
PRK08581 PRK08581
amidase domain-containing protein;
670-863 2.50e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.08  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  670 LNSDDTKNNIYEYKLNNDDTKNNIyEYKLNNDDTKNNIYEYKLNNDDSNNTIYEYKlnNDDSNNTIYEYKLNNDDSNNTI 749
Cdd:PRK08581   31 QKDSTAKTTSHDSKKSNDDETSKD-TSSKDTDKADNNNTSNQDNNDKKFSTIDSST--SDSNNIIDFIYKNLPQTNINQL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512056  750 YEYKLNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDSNNTiyeyklNNDDSNNTIYEYKLNNDDSNNTIYEYKLNNDDS 829
Cdd:PRK08581  108 LTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTND------SNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNN 181

                         170       180       190
                  ....*....|....*....|....*....|....
gi 124512056  830 NNTIYEYKLNSDDSNNTPYLNGQEKNEETEEGND 863
Cdd:PRK08581  182 TKPSTSNKQPNSPKPTQPNQSNSQPASDDTANQK 215
 
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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