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Conserved domains on  [gi|755551840|ref|XP_011243982|]
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keratin Kb40 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
61-374 4.15e-124

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 380.81  E-value: 4.15e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    61 QETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGnRSPQGLECIFETCLARLRQQLEELQRERRALDSELKT 140
Cdd:pfam00038    1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG-AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   141 YQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEEELGQLKTQADDMSVVLS 220
Cdd:pfam00038   80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   221 MDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQ 300
Cdd:pfam00038  160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551840   301 NDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECR 374
Cdd:pfam00038  240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
KLF18_N super family cl40479
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-915 2.16e-24

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: 104.00  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  706 YGGQVTMPRGE---CGGQVTVPG---REYGGQVTMPRGE---CGGQVTMPG---REYGGQVTVPRRE---CGGQVTVPG- 769
Cdd:cd21575     5 YGSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNqtlYGGQMTTSTg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  770 --REYGGQVTMPGresGGQVTvpgreYGGQVTVPRGE---CGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE- 837
Cdd:cd21575    85 nqTLYGGQMTTSG---SDQTL-----YGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDq 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  838 --YGGQVTMPRGE---CGGQVTVPRGE---CGGQVTMPGRE---YGGQVTVPGREYGGQMTMPGRE---CGGQEVIPRGE 903
Cdd:cd21575   157 tlYGGQMTTSSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSS 236

                         250
                  ....*....|..
gi 755551840  904 cggQVVMPGQEC 915
Cdd:cd21575   237 ---SLPYPGQLT 245
KLF18_N super family cl40479
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 542-735 4.75e-16

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: 79.73  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  542 GGQVTIPGRE---SGGQVTIPG---RESGGQVTMPGRE---YGGQVTIPG---RESGGQVTMPGRGS---GGQVTMPG-- 604
Cdd:cd21575     6 GSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  605 -RGSGGQVTVPGRE---YGGQVTVPGRG---SGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE---YGGQVTM 668
Cdd:cd21575    86 qTLYGGQMTTSGSDqtlYGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDqtlYGGQMTT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  669 PRGE---CGGQVTMPGRE---YGGQVTMPGRE---SGGQVTVPGREYGGQVTMPRGE---CGGQVTVPGRE---YGGQVT 733
Cdd:cd21575   166 SSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSSslpYPGQLT 245


                  ..
gi 755551840  734 MP 735
Cdd:cd21575   246 FS 247
KLF18_N super family cl40479
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 432-618 4.25e-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: 61.63  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  432 GGQVTIPGRG---SGGQVTVPRGE---CGGQVTMPG---RGSGGQVTMPGRGS---GGQVTIPG---RGSGGQVTVPGRG 496
Cdd:cd21575    20 GGQMTTPSGDqtlYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgnqTLYGGQMTTSGSD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  497 ---SGGQVTIPGRG---SGGQVTIPGRGS---GGQVTVPGRG---SGGQVTIPGRGS---GGQVTIPGRES---GGQVTI 558
Cdd:cd21575   100 qtlYGGQMTTSSGDqtlYGGQMTTSSGDQtlyGGQMTTSTGDqtlYGGQMTTSTGDQtlyGGQMTTSSGDQtlyGGQMTT 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  559 PGRES---GGQVTMPGRE---YGGQVTIPGRESGGQVTMPGRG---SGGQVTMPgrgSGGQVTVPGREY 618
Cdd:cd21575   180 STSNQtlyGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSH---QSSSLPYPGQLT 245
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
61-374 4.15e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 380.81  E-value: 4.15e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    61 QETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGnRSPQGLECIFETCLARLRQQLEELQRERRALDSELKT 140
Cdd:pfam00038    1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG-AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   141 YQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEEELGQLKTQADDMSVVLS 220
Cdd:pfam00038   80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   221 MDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQ 300
Cdd:pfam00038  160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551840   301 NDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECR 374
Cdd:pfam00038  240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-915 2.16e-24

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: 104.00  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  706 YGGQVTMPRGE---CGGQVTVPG---REYGGQVTMPRGE---CGGQVTMPG---REYGGQVTVPRRE---CGGQVTVPG- 769
Cdd:cd21575     5 YGSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNqtlYGGQMTTSTg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  770 --REYGGQVTMPGresGGQVTvpgreYGGQVTVPRGE---CGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE- 837
Cdd:cd21575    85 nqTLYGGQMTTSG---SDQTL-----YGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDq 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  838 --YGGQVTMPRGE---CGGQVTVPRGE---CGGQVTMPGRE---YGGQVTVPGREYGGQMTMPGRE---CGGQEVIPRGE 903
Cdd:cd21575   157 tlYGGQMTTSSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSS 236

                         250
                  ....*....|..
gi 755551840  904 cggQVVMPGQEC 915
Cdd:cd21575   237 ---SLPYPGQLT 245
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 542-735 4.75e-16

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: 79.73  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  542 GGQVTIPGRE---SGGQVTIPG---RESGGQVTMPGRE---YGGQVTIPG---RESGGQVTMPGRGS---GGQVTMPG-- 604
Cdd:cd21575     6 GSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  605 -RGSGGQVTVPGRE---YGGQVTVPGRG---SGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE---YGGQVTM 668
Cdd:cd21575    86 qTLYGGQMTTSGSDqtlYGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDqtlYGGQMTT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  669 PRGE---CGGQVTMPGRE---YGGQVTMPGRE---SGGQVTVPGREYGGQVTMPRGE---CGGQVTVPGRE---YGGQVT 733
Cdd:cd21575   166 SSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSSslpYPGQLT 245


                  ..
gi 755551840  734 MP 735
Cdd:cd21575   246 FS 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 114-531 1.76e-15

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 79.49  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  114 ETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQskmDLEGNLESLKEh 193
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGE- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  194 vcFLTRLYEEelgqlKTQADDMSVVLSMDnnrclDFSDIIAEVRAryeeITRTSKAEAEAVfqtkyqelqesaqlqgNSM 273
Cdd:COG3883    91 --RARALYRS-----GGSVSYLDVLLGSE-----SFSDFLDRLSA----LSKIADADADLL----------------EEL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  274 KEAQVQISQLRQAihrLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQMLRDYQELmgt 353
Cdd:COG3883   139 KADKAELEAKKAE---LEAKLAELEALKAELEAAKAELEAQ----QAEQEALLAQLSAEEAAAEAQLAELEAELAAA--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  354 klsldvEIAMYRRLLESEECRISTEHTSQVTVSITEGSIVPGRTCGGQVVVPGRIGTGQVVMPGRECGGHVVMPGRGSGG 433
Cdd:COG3883   209 ------EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  434 QVTIPGRGSGGQVTVPRGECGGQVTMPGRGSGGQVTmPGRGSGGQVTIPGRGSGGQVTVPGRGSGGQVTIPGRGSGGQVT 513
Cdd:COG3883   283 GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGG-AGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSG 361

                         410
                  ....*....|....*...
gi 755551840  514 IPGRGSGGQVTVPGRGSG 531
Cdd:COG3883   362 GGGGGVGLSVGGGYVGGA 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-349 5.90e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 76.63  E-value: 5.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    39 VLIAKNDFLIASLQRLFQVVK------TQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQgnrspqgleci 112
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKeaeeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----------- 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   113 fetclARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEvFQSKMD-LEGNLESLK 191
Cdd:TIGR02168  298 -----SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEeLEAELEELE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   192 EHVcfltRLYEEELGQLKTQADDMSVVLSMDNNRcldfsdiIAEVRARYEEItrtskaeAEAVFQTKYQELQESAQLQGN 271
Cdd:TIGR02168  372 SRL----EELEEQLETLRSKVAQLELQIASLNNE-------IERLEARLERL-------EDRRERLQQEIEELLKKLEEA 433

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551840   272 SMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQqgemAVRDAQAKLDELEAALrTAKQDMAQMLRDYQE 349
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ----ALDAAERELAQLQARL-DSLERLQENLEGFSE 506
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 432-618 4.25e-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: 61.63  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  432 GGQVTIPGRG---SGGQVTVPRGE---CGGQVTMPG---RGSGGQVTMPGRGS---GGQVTIPG---RGSGGQVTVPGRG 496
Cdd:cd21575    20 GGQMTTPSGDqtlYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgnqTLYGGQMTTSGSD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  497 ---SGGQVTIPGRG---SGGQVTIPGRGS---GGQVTVPGRG---SGGQVTIPGRGS---GGQVTIPGRES---GGQVTI 558
Cdd:cd21575   100 qtlYGGQMTTSSGDqtlYGGQMTTSSGDQtlyGGQMTTSTGDqtlYGGQMTTSTGDQtlyGGQMTTSSGDQtlyGGQMTT 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  559 PGRES---GGQVTMPGRE---YGGQVTIPGRESGGQVTMPGRG---SGGQVTMPgrgSGGQVTVPGREY 618
Cdd:cd21575   180 STSNQtlyGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSH---QSSSLPYPGQLT 245
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
120-346 4.73e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.44  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  120 LRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAY---KHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcf 196
Cdd:PRK02224  204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleEHEERREELETLEAEIEDLRETIAETEREREELAEEV-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 ltRLYEEELGQLKTQADDMSVVLSMDN-------NRCLDFSDIIAEVRARYEE----ITRTSK-----AEAEAVFQTKYQ 260
Cdd:PRK02224  282 --RDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEEcrvaAQAHNEeaeslREDADDLEERAE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  261 ELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVR---DAQAKLDELEAALRTAK 337
Cdd:PRK02224  360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTAR 439

                         250
                  ....*....|.
gi 755551840  338 QDM--AQMLRD 346
Cdd:PRK02224  440 ERVeeAEALLE 450
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 252-346 2.52e-04

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    252 EAVFQtKYQELQE-SAQLQgnsmKEAQVQISQLRQAIHRLQSQIGSLRKQNDSL-QSAIADAEQQGEMAVRDAQAKLDEL 329
Cdd:smart00935    7 QKILQ-ESPAGKAaQKQLE----KEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL 81

                            90
                    ....*....|....*..
gi 755551840    330 EAALRTAKQDMAQMLRD 346
Cdd:smart00935   82 QQDLQKRQQEELQKILD 98
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 231-297 3.73e-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: 41.65  E-value: 3.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  231 DIIAEVRARYEEITRTSKAEAEAVfqtkYQELQESAQLQGNSMKE-AQVQISQLRQ-AIHRLQSQIGSL 297
Cdd:cd06503    58 EKLAEARAEAQEIIEEARKEAEKI----KEEILAEAKEEAERILEqAKAEIEQEKEkALAELRKEVADL 122
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 627-734 1.94e-03

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 41.76  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  627 RGSGGQVTVPGR-EYGGQVTVPRGECGGQVTVPGREYGGQVTMPRGECGGQVTMPGREYGGQVTMPGRESGGQVTVPGRE 705
Cdd:PTZ00473  308 RNMGHDSRGPYNaNYGGQFNSRSGRTGSSESIRGFTYDSSTTYGGSSYGTSQTDSTSTYGSRSTFDSSTGGGSQSGGGST 387

                          90       100
                  ....*....|....*....|....*....
gi 755551840  706 YGGQVTMPRGECGGQVTVPGREYGGQVTM 734
Cdd:PTZ00473  388 YGGSSTFDGSSRGSSDSFGVSYFGPQQTV 416
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
61-374 4.15e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 380.81  E-value: 4.15e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    61 QETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGnRSPQGLECIFETCLARLRQQLEELQRERRALDSELKT 140
Cdd:pfam00038    1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG-AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   141 YQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEEELGQLKTQADDMSVVLS 220
Cdd:pfam00038   80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   221 MDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQ 300
Cdd:pfam00038  160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551840   301 NDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECR 374
Cdd:pfam00038  240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 706-915 2.16e-24

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: 104.00  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  706 YGGQVTMPRGE---CGGQVTVPG---REYGGQVTMPRGE---CGGQVTMPG---REYGGQVTVPRRE---CGGQVTVPG- 769
Cdd:cd21575     5 YGSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNqtlYGGQMTTSTg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  770 --REYGGQVTMPGresGGQVTvpgreYGGQVTVPRGE---CGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE- 837
Cdd:cd21575    85 nqTLYGGQMTTSG---SDQTL-----YGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDq 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  838 --YGGQVTMPRGE---CGGQVTVPRGE---CGGQVTMPGRE---YGGQVTVPGREYGGQMTMPGRE---CGGQEVIPRGE 903
Cdd:cd21575   157 tlYGGQMTTSSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSS 236

                         250
                  ....*....|..
gi 755551840  904 cggQVVMPGQEC 915
Cdd:cd21575   237 ---SLPYPGQLT 245
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 542-735 4.75e-16

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: 79.73  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  542 GGQVTIPGRE---SGGQVTIPG---RESGGQVTMPGRE---YGGQVTIPG---RESGGQVTMPGRGS---GGQVTMPG-- 604
Cdd:cd21575     6 GSQMTTSSGDqtlYGGQMTTPSgdqTLYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgn 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  605 -RGSGGQVTVPGRE---YGGQVTVPGRG---SGGQVTVPGRE---YGGQVTVPRGE---CGGQVTVPGRE---YGGQVTM 668
Cdd:cd21575    86 qTLYGGQMTTSGSDqtlYGGQMTTSSGDqtlYGGQMTTSSGDqtlYGGQMTTSTGDqtlYGGQMTTSTGDqtlYGGQMTT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  669 PRGE---CGGQVTMPGRE---YGGQVTMPGRE---SGGQVTVPGREYGGQVTMPRGE---CGGQVTVPGRE---YGGQVT 733
Cdd:cd21575   166 SSGDqtlYGGQMTTSTSNqtlYGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSHQSSslpYPGQLT 245


                  ..
gi 755551840  734 MP 735
Cdd:cd21575   246 FS 247
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 114-531 1.76e-15

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 79.49  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  114 ETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQskmDLEGNLESLKEh 193
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGE- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  194 vcFLTRLYEEelgqlKTQADDMSVVLSMDnnrclDFSDIIAEVRAryeeITRTSKAEAEAVfqtkyqelqesaqlqgNSM 273
Cdd:COG3883    91 --RARALYRS-----GGSVSYLDVLLGSE-----SFSDFLDRLSA----LSKIADADADLL----------------EEL 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  274 KEAQVQISQLRQAihrLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQMLRDYQELmgt 353
Cdd:COG3883   139 KADKAELEAKKAE---LEAKLAELEALKAELEAAKAELEAQ----QAEQEALLAQLSAEEAAAEAQLAELEAELAAA--- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  354 klsldvEIAMYRRLLESEECRISTEHTSQVTVSITEGSIVPGRTCGGQVVVPGRIGTGQVVMPGRECGGHVVMPGRGSGG 433
Cdd:COG3883   209 ------EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  434 QVTIPGRGSGGQVTVPRGECGGQVTMPGRGSGGQVTmPGRGSGGQVTIPGRGSGGQVTVPGRGSGGQVTIPGRGSGGQVT 513
Cdd:COG3883   283 GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGG-AGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSG 361

                         410
                  ....*....|....*...
gi 755551840  514 IPGRGSGGQVTVPGRGSG 531
Cdd:COG3883   362 GGGGGVGLSVGGGYVGGA 379
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-349 5.90e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 76.63  E-value: 5.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    39 VLIAKNDFLIASLQRLFQVVK------TQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQgnrspqgleci 112
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKeaeeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----------- 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   113 fetclARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEvFQSKMD-LEGNLESLK 191
Cdd:TIGR02168  298 -----SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEeLEAELEELE 371

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   192 EHVcfltRLYEEELGQLKTQADDMSVVLSMDNNRcldfsdiIAEVRARYEEItrtskaeAEAVFQTKYQELQESAQLQGN 271
Cdd:TIGR02168  372 SRL----EELEEQLETLRSKVAQLELQIASLNNE-------IERLEARLERL-------EDRRERLQQEIEELLKKLEEA 433

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551840   272 SMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQqgemAVRDAQAKLDELEAALrTAKQDMAQMLRDYQE 349
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ----ALDAAERELAQLQARL-DSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 117-358 6.14e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.51  E-value: 6.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEvfqskmdLEGNLESLKEhvcf 196
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-------LEQDIARLEE---- 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LTRLYEEELGQLKTQADDmsvvlsmDNNRCLDFSDIIAEVRARYEEIT--RTSKAEAEAVFQTKYQELQESAQLQGNSMK 274
Cdd:COG1196   310 RRRELEERLEELEEELAE-------LEEELEELEEELEELEEELEEAEeeLEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  275 EAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTK 354
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462


                  ....
gi 755551840  355 LSLD 358
Cdd:COG1196   463 ELLA 466
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 117-372 6.45e-14

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: 76.65  E-value: 6.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHV-- 194
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIen 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   195 --CFLTRL------YEEELGQLKTQADDMSVVLSMDNNRCL-DFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQES 265
Cdd:TIGR02169  756 vkSELKELearieeLEEDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   266 AQLQgNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQ-GEMA--VRDAQAKLDELEAALRTAKQDmAQ 342
Cdd:TIGR02169  836 QELQ-EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlGDLKkeRDELEAQLRELERKIEELEAQ-IE 913

                          250       260       270
                   ....*....|....*....|....*....|.
gi 755551840   343 MLRDYQELMGTKLS-LDVEIAMYRRLLESEE 372
Cdd:TIGR02169  914 KKRKRLSELKAKLEaLEEELSEIEDPKGEDE 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-372 8.29e-14

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 76.25  E-value: 8.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   117 LARLRQQLEELQRERRALDSELKTYQDQEDEYkskydqeaykhasvQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCF 196
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEEL--------------EEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   197 LTRLYEEELGQLKTQADDMSVVLSMDNNRCLDFSDI---IAEVRARYEEITRTSKAEAEAV--FQTKYQELQESAQLQGN 271
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKALREALdeLRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   272 SMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEmavrDAQAKLDELEAALRTAKQDMAQMLRDYQELM 351
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELEELS 900

                          250       260
                   ....*....|....*....|..
gi 755551840   352 GTKLSLDVEI-AMYRRLLESEE 372
Cdd:TIGR02168  901 EELRELESKRsELRRELEELRE 922
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-350 4.73e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.55  E-value: 4.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    64 REIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLqgnrspqglecifetcLARLRQQLEELQRERRALDSELKTYQD 143
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEE----------------LEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   144 QEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcfltRLYEEELGQLKTQADDMSVVLSMDN 223
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   224 NRcldfsdiIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQlqgnsMKEAQVQISQLRQAIHRLQSQIGSLRKQNDS 303
Cdd:TIGR02168  817 EE-------AANLRERLESLERRIAATERRLEDLEEQIEELSED-----IESLAAEIEELEELIEELESELEALLNERAS 884

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 755551840   304 LQSAIA---DAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQEL 350
Cdd:TIGR02168  885 LEEALAllrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 443-691 1.86e-12

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: 68.95  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  443 GGQVTVPRGE---CGGQVTMP--GRGSGGQVTMPGRGS----GGQVTIPgrgSGGQVTvpgrgSGGQVTIPgrgSGGQVT 513
Cdd:cd21575     6 GSQMTTSSGDqtlYGGQMTTPsgDQTLYGGQMTTSFSEqtlyGGQMTTP---SGDQTL-----YGGQMTTP---NGNQTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  514 ipgrgSGGQVTVPG---RGSGGQVTIPGRG---SGGQVTIPGRE---SGGQVTIPgreSGGQVTmpgreYGGQVTIPgre 584
Cdd:cd21575    75 -----YGGQMTTSTgnqTLYGGQMTTSGSDqtlYGGQMTTSSGDqtlYGGQMTTS---SGDQTL-----YGGQMTTS--- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  585 SGGQVTmpgrgSGGQVTMPGRGS---GGQVTVPGRE---YGGQVTVPgrgSGGQVTvpgreYGGQVTVPRGE---CGGQV 655
Cdd:cd21575   139 TGDQTL-----YGGQMTTSTGDQtlyGGQMTTSSGDqtlYGGQMTTS---TSNQTL-----YGGQMTTSSGNqtlYGGQM 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 755551840  656 TVPGREYGGQVTMPRGE---CGGQVTMPGRE---YGGQVTMP 691
Cdd:cd21575   206 TTPITLSGGQMTTSTGDqtlYGGQMTSHQSSslpYPGQLTFS 247
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
117-372 4.84e-11

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 64.93  E-value: 4.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDE--------------YKSKYDQ---EAYKHASVQND----FVVLKKDVDE 175
Cdd:COG1340    17 IEELREEIEELKEKRDELNEELKELAEKRDElnaqvkelreeaqeLREKRDElneKVKELKEERDElnekLNELREELDE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  176 VFQSKMDLEGNLESLKEhvcfLTRLYEEELGQLKTQaddmsvVLSMDNNRclDFSDIIAEVRARYEeitrtsKAEAEAVF 255
Cdd:COG1340    97 LRKELAELNKAGGSIDK----LRKEIERLEWRQQTE------VLSPEEEK--ELVEKIKELEKELE------KAKKALEK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  256 QTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRT 335
Cdd:COG1340   159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE----IVEAQEKADELHEEIIE 234

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 755551840  336 AKQDmaqmLRDYQELMGTKLSLDVEIAMYRRLLESEE 372
Cdd:COG1340   235 LQKE----LRELRKELKKLRKKQRALKREKEKEELEE 267
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 112-369 6.11e-11

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: 67.02  E-value: 6.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   112 IFETCLARLRQQLEELQRERraldSELKTYQDQEDEyksKYDQEAYKHAsvqndfvvlkKDVDEVFQSKMDLEGNLESLK 191
Cdd:TIGR02169  188 RLDLIIDEKRQQLERLRRER----EKAERYQALLKE---KREYEGYELL----------KEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   192 EHVCFLTRLYEE----------ELGQLKTQADDMSvvlsmdNNRCLDFSDIIAEVRAryeEITRTSKAEAEavfqtKYQE 261
Cdd:TIGR02169  251 EELEKLTEEISElekrleeieqLLEELNKKIKDLG------EEEQLRVKEKIGELEA---EIASLERSIAE-----KERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   262 LQESAqlqgNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMA 341
Cdd:TIGR02169  317 LEDAE----ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELK 388

                          250       260
                   ....*....|....*....|....*...
gi 755551840   342 QMLRDYQELMGTKLSLDVEIamyRRLLE 369
Cdd:TIGR02169  389 DYREKLEKLKREINELKREL---DRLQE 413
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
188-414 7.82e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 64.92  E-value: 7.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  188 ESLKEHVCFLTRLyEEELGQLKTQADDMSvvlsmdnnrcLDFSDIIAEVRARYEEITRTSKAEAEAvfQTKYQELQESAQ 267
Cdd:COG4372    31 EQLRKALFELDKL-QEELEQLREELEQAR----------EELEQLEEELEQARSELEQLEEELEEL--NEQLQAAQAELA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  268 LQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQMLRDY 347
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQEL 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551840  348 QELMGTKLSLDVEiamyrRLLESEECRISTEHTSQVTVSITEGSIVPGRTCGGQVVVPGRIGTGQVV 414
Cdd:COG4372   174 QALSEAEAEQALD-----ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-372 1.39e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  120 LRQQLEELQRERRAldseLKTYQDQEDEYKsKYDQEAYKHA--SVQNDFVVLKKDVDEvfqskmdLEGNLESLKEHVcfl 197
Cdd:COG1196   198 LERQLEPLERQAEK----AERYRELKEELK-ELEAELLLLKlrELEAELEELEAELEE-------LEAELEELEAEL--- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  198 tRLYEEELGQLKTQADDMSvvlsmdnnrcLDFSDIIAEVRARYEEITRTSKAEAEAvfQTKYQELQESAQLQGNSMKEAQ 277
Cdd:COG1196   263 -AELEAELEELRLELEELE----------LELEEAQAEEYELLAELARLEQDIARL--EERRRELEERLEELEEELAELE 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  278 VQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALR---TAKQDMAQMLRDYQELMGTK 354
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEellEALRAAAELAAQLEELEEAE 409

                         250
                  ....*....|....*...
gi 755551840  355 LSLDVEIAMYRRLLESEE 372
Cdd:COG1196   410 EALLERLERLEEELEELE 427
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
117-350 2.26e-10

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 64.65  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQdqedeykskydqeaykhasVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEhvcf 196
Cdd:COG3206   177 LEFLEEQLPELRKELEEAEAALEEFR-------------------QKNGLVDLSEEAKLLLQQLSELESQLAEARA---- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LTRLYEEELGQLKTQADDMSVVLSMDNNrcldfSDIIAEVRARYEEItRTSKAEAEAVFQTKYQELQesaQLQgNSMKEA 276
Cdd:COG3206   234 ELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL-EAELAELSARYTPNHPDVI---ALR-AQIAAL 303

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  277 QVQISQ-LRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEmAVRDAQAKLDELEAALRTAKQDMAQMLRDYQEL 350
Cdd:COG3206   304 RAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEA 377
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-333 3.55e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.31  E-value: 3.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    53 RLFQVVKTQETREIRSLNNQFASFIDKVRFLEQQ--------NKVLETKWELLQQLQGNRsPQGLECifETCLARLRQQL 124
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskelTELEAEIEELEERLEEAE-EELAEA--EAEIEELEAQI 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   125 EELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcfltRLYEEE 204
Cdd:TIGR02168  792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI----EELEEL 867

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   205 LGQLKTQADDMSVVLSMDNNRcldfsdiIAEVRARYEEITRTSKaEAEAVFQTKYQELQESAQlqgnSMKEAQVQISQLR 284
Cdd:TIGR02168  868 IEELESELEALLNERASLEEA-------LALLRSELEELSEELR-ELESKRSELRRELEELRE----KLAQLELRLEGLE 935

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 755551840   285 QAIHRLQSQIGSlrKQNDSLQSAIAdAEQQGEMAVRDAQAKLDELEAAL 333
Cdd:TIGR02168  936 VRIDNLQERLSE--EYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKI 981
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 432-618 4.25e-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: 61.63  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  432 GGQVTIPGRG---SGGQVTVPRGE---CGGQVTMPG---RGSGGQVTMPGRGS---GGQVTIPG---RGSGGQVTVPGRG 496
Cdd:cd21575    20 GGQMTTPSGDqtlYGGQMTTSFSEqtlYGGQMTTPSgdqTLYGGQMTTPNGNQtlyGGQMTTSTgnqTLYGGQMTTSGSD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  497 ---SGGQVTIPGRG---SGGQVTIPGRGS---GGQVTVPGRG---SGGQVTIPGRGS---GGQVTIPGRES---GGQVTI 558
Cdd:cd21575   100 qtlYGGQMTTSSGDqtlYGGQMTTSSGDQtlyGGQMTTSTGDqtlYGGQMTTSTGDQtlyGGQMTTSSGDQtlyGGQMTT 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  559 PGRES---GGQVTMPGRE---YGGQVTIPGRESGGQVTMPGRG---SGGQVTMPgrgSGGQVTVPGREY 618
Cdd:cd21575   180 STSNQtlyGGQMTTSSGNqtlYGGQMTTPITLSGGQMTTSTGDqtlYGGQMTSH---QSSSLPYPGQLT 245
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 120-372 2.92e-09

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 61.34  E-value: 2.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   120 LRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAykhASVQNDFVVLKKdvdevFQSkmDLEGNLESLKEHVCFLTR 199
Cdd:pfam01576  501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA---GTLEALEEGKKR-----LQR--ELEALTQQLEEKAAAYDK 570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   200 LyEEELGQLKTQADDMSVVLsmDNNRCL---------DFSDIIAE---VRARYEEitRTSKAEAEAvfqtkyqelqesaq 267
Cdd:pfam01576  571 L-EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA-------------- 631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   268 lqgnsmKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQsaiadAEQQGEMAVRDAQAK-LDELEAALRTAKQDMAQM--- 343
Cdd:pfam01576  632 ------REKETRALSLARALEEALEAKEELERTNKQLR-----AEMEDLVSSKDDVGKnVHELERSKRALEQQVEEMktq 700

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 755551840   344 ---LRDyqELMGT---KLSLDVEI----AMYRRLLESEE 372
Cdd:pfam01576  701 leeLED--ELQATedaKLRLEVNMqalkAQFERDLQARD 737
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 41-380 3.20e-09

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.80  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    41 IAKNDFLIASLQRLFQVVKTQETR---EIRSLNNQFASFIDKVRFLEQQNKVLETKwellqqlqgnrspqglECIFETCL 117
Cdd:TIGR04523  119 KNKLEVELNKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENE----------------LNLLEKEK 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   118 ARLRQQLEELQRERRALD---SELKTYQDQEDEYKSKYDQeaykhasVQNDFVVLKKDVDEVFQSKMDLEGNLESLkehv 194
Cdd:TIGR04523  183 LNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISE-------LKKQNNQLKDNIEKKQQEINEKTTEISNT---- 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   195 cfltrlyEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEItrtsKAEAEAVFQTKYQ----ELQESAQLQG 270
Cdd:TIGR04523  252 -------QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL----KSEISDLNNQKEQdwnkELKSELKNQE 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   271 NSMKEAQVQISQLRQAIHRLQSQIGSLRKQ-------NDSLQSAIADAEQQGEMAVRDAQAKLDELEaALRTAKQDMAQM 343
Cdd:TIGR04523  321 KKLEEIQNQISQNNKIISQLNEQISQLKKEltnseseNSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESK 399

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 755551840   344 LRDYQELmgTKLsLDVEIamyrRLLESEECRISTEHT 380
Cdd:TIGR04523  400 IQNQEKL--NQQ-KDEQI----KKLQQEKELLEKEIE 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
120-346 4.73e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 60.44  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  120 LRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAY---KHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcf 196
Cdd:PRK02224  204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleEHEERREELETLEAEIEDLRETIAETEREREELAEEV-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 ltRLYEEELGQLKTQADDMSVVLSMDN-------NRCLDFSDIIAEVRARYEE----ITRTSK-----AEAEAVFQTKYQ 260
Cdd:PRK02224  282 --RDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEEcrvaAQAHNEeaeslREDADDLEERAE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  261 ELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVR---DAQAKLDELEAALRTAK 337
Cdd:PRK02224  360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTAR 439

                         250
                  ....*....|.
gi 755551840  338 QDM--AQMLRD 346
Cdd:PRK02224  440 ERVeeAEALLE 450
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 78-343 5.27e-09

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 60.09  E-value: 5.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    78 DKVRFLEQQNKVLETKWELLQQLQgnRSPQGLEcifETCLARLRQ--QLEELQRERRALDSELKTYQDQEDEYKSKYDQE 155
Cdd:pfam05622  128 DKVKKLEATVETYKKKLEDLGDLR--RQVKLLE---ERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQELHGKLSEE 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   156 AYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcfltrlyeEEL--GQLK----TQADDM--SVVLSMDNnrcL 227
Cdd:pfam05622  203 SKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETN--------EELrcAQLQqaelSQADALlsPSSDPGDN---L 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   228 DFSDIIAEVRARYEEITRTSKA------EAEAVFQTKYQELQESAQLQGNSMKE----AQVQISQLRQAIHRLQSQIGSL 297
Cdd:pfam05622  272 AAEIMPAEIREKLIRLQHENKMlrlgqeGSYRERLTELQQLLEDANRRKNELETqnrlANQRILELQQQVEELQKALQEQ 351

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551840   298 RKQNDSLQSAIADAEQQGEMaVRDAQA----------------------KLDELEAALRTAKQDMAQM 343
Cdd:pfam05622  352 GSKAEDSSLLKQKLEEHLEK-LHEAQSelqkkkeqieelepkqdsnlaqKIDELQEALRKKDEDMKAM 418
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 61-341 8.44e-09

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 59.80  E-value: 8.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    61 QETREIrSLNNQFASFIDKVRFLEQQNKVLETKWELL-----------QQLQgnRSPQGLEcifeTCLARLRQQLEELQR 129
Cdd:pfam01576  634 KETRAL-SLARALEEALEAKEELERTNKQLRAEMEDLvsskddvgknvHELE--RSKRALE----QQVEEMKTQLEELED 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   130 ERRA------------------LDSELKTYQDQEDEYKSKYDQEAYKHASVQNDfvvLKKDVDEVFQSKMDLEGNLESLK 191
Cdd:pfam01576  707 ELQAtedaklrlevnmqalkaqFERDLQARDEQGEEKRRQLVKQVRELEAELED---ERKQRAQAVAAKKKLELDLKELE 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   192 EHVCFLTRLYEEELGQLKTQADDMSvvlsmDNNRCLDfsdiiaEVRARYEEITRTSKA--------EAEAV-FQ------ 256
Cdd:pfam01576  784 AQIDAANKGREEAVKQLKKLQAQMK-----DLQRELE------EARASRDEILAQSKEsekklknlEAELLqLQedlaas 852

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   257 --TKYQELQESAQLQ-----GNSMKEAQ--------VQISQLRQAIHRLQSQIGSL----RK---QNDSLQSAIA----- 309
Cdd:pfam01576  853 erARRQAQQERDELAdeiasGASGKSALqdekrrleARIAQLEEELEEEQSNTELLndrlRKstlQVEQLTTELAaerst 932

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 755551840   310 -----DAEQQGEMAVRDAQAKLDELEAALRTaKQDMA 341
Cdd:pfam01576  933 sqkseSARQQLERQNKELKAKLQEMEGTVKS-KFKSS 968
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
119-372 1.26e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 58.87  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  119 RLRQQLEELQRERRALDSELKTYQDQEDEYKSKYdqEAYKhasVQNDFVvlkkDVDEvfqskmDLEGNLESLKEhvcflt 198
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAAL--EEFR---QKNGLV----DLSE------EAKLLLQQLSE------ 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  199 rlYEEELGQLKTQaddmsvvlsmdnnrcldfsdiIAEVRARYEEITRTSKAEAEAVfqtkyQELQESAQLQG--NSMKEA 276
Cdd:COG3206   224 --LESQLAEARAE---------------------LAEAEARLAALRAQLGSGPDAL-----PELLQSPVIQQlrAQLAEL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  277 QVQISQLRQaihRLQS---QIGSLRKQNDSLQSAIADAEQQG----EMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQE 349
Cdd:COG3206   276 EAELAELSA---RYTPnhpDVIALRAQIAALRAQLQQEAQRIlaslEAELEALQAREASLQAQLAQLEARLAELPELEAE 352

                         250       260
                  ....*....|....*....|....*
gi 755551840  350 LmgTKLSLDVEIA--MYRRLLESEE 372
Cdd:COG3206   353 L--RRLEREVEVAreLYESLLQRLE 375
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
117-314 1.42e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQR-----------ERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNdfvvLKKDVDEVFQSKMDLEg 185
Cdd:COG4717    48 LERLEKEADELFKpqgrkpelnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLE- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  186 NLESLKEHVCFLTRLyEEELGQLKTQADDMSvvlsmdnNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQES 265
Cdd:COG4717   123 KLLQLLPLYQELEAL-EAELAELPERLEELE-------ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755551840  266 AQLQgNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQ 314
Cdd:COG4717   195 QDLA-EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-342 1.45e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 57.85  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  114 ETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEH 193
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  194 VCFLTRLYeeelgQLKTQADDMSVVLSMDnnrclDFSDiiAEVRARY-EEITRTSKAEAEAVfQTKYQELQESAQLQGNS 272
Cdd:COG4942   106 LAELLRAL-----YRLGRQPPLALLLSPE-----DFLD--AVRRLQYlKYLAPARREQAEEL-RADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  273 MKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQ 342
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAA 238
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-389 1.58e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   47 LIASLQRLFQVVKTQET------REIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQ-----LQGNRSPQ-------- 107
Cdd:COG4717   197 LAEELEELQQRLAELEEeleeaqEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallaLLGLGGSLlsliltia 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  108 -------GLECIFETCLARLRQQLEELQRERRALDsELKTYQDQE-DEYKSKYDQEAYKHASvqnDFVVLKKDVDEVFQS 179
Cdd:COG4717   277 gvlflvlGLLALLFLLLAREKASLGKEAEELQALP-ALEELEEEElEELLAALGLPPDLSPE---ELLELLDRIEELQEL 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  180 KMDLEGNLESLKEHVcfltrlYEEELGQLKTQADdmsvVLSMDnnrclDFSDIIAEVRaRYEEITRTsKAEAEAVFQTKY 259
Cdd:COG4717   353 LREAEELEEELQLEE------LEQEIAALLAEAG----VEDEE-----ELRAALEQAE-EYQELKEE-LEELEEQLEELL 415

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  260 QELQEsaQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQ-----AKLDELE---A 331
Cdd:COG4717   416 GELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQEleelkAELRELAeewA 493

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  332 ALRTAKQDMAQMLRDYQELMGTKLSLDVE--IAM-----YRRLLESEECRISTEHTSQVTVSITE 389
Cdd:COG4717   494 ALKLALELLEEAREEYREERLPPVLERASeyFSRltdgrYRLIRIDEDLSLKVDTEDGRTRPVEE 558
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-372 2.04e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   61 QETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQ-LQGNRSPQGLECIFETcLARLRQQLEELQRERRALDSELK 139
Cdd:COG4717    78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREeLEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLE 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  140 TYQDQEDEYKSKYDQEAYKHA-----------SVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcfltRLYEEELGQL 208
Cdd:COG4717   157 ELRELEEELEELEAELAELQEeleelleqlslATEEELQDLAEELEELQQRLAELEEELEEAQEEL----EELEEELEQL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  209 KTQADDMS------------------VVLSMDNNRCLDFSDIIAEV----------------RARYEEITRTSKAEAEAV 254
Cdd:COG4717   233 ENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAGVlflvlgllallflllaREKASLGKEAEELQALPA 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  255 FQT-KYQELQESAQLQG--------------NSMKEAQVQISQLRQAIHRLqsQIGSLRKQNDSL-QSAIADAEQQGEMA 318
Cdd:COG4717   313 LEElEEEELEELLAALGlppdlspeellellDRIEELQELLREAEELEEEL--QLEELEQEIAALlAEAGVEDEEELRAA 390

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755551840  319 VRDAQaKLDELEAALRTAKQDMAQMLRDYQELM--GTKLSLDVEIAMYRRLLESEE 372
Cdd:COG4717   391 LEQAE-EYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELE 445
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 241-331 3.79e-08

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 53.03  E-value: 3.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   241 EEITRTSKAEAEAvfQTKYQELQESAQLQGNSMKEAQV--------------QISQLRQAIHRLQSQIGSLRKQNDSLQS 306
Cdd:pfam07926    8 SEIKRLKEEAADA--EAQLQKLQEDLEKQAEIAREAQQnyerelvlhaedikALQALREELNELKAEIAELKAEAESAKA 85

                           90       100       110
                   ....*....|....*....|....*....|..
gi 755551840   307 AIADAE-------QQGEMAVRDAQAKLDELEA 331
Cdd:pfam07926   86 ELEESEesweeqkKELEKELSELEKRIEDLNE 117
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 61-353 4.03e-08

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 57.01  E-value: 4.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    61 QETREIRSLNNQFASFID-----KVRFLEQQNKVLETKWELLQqLQGNRSPQGLEC-IFETCLARLRQQLEELQR---ER 131
Cdd:pfam05622   35 QENKKLQERLDQLESGDDsgtpgGKKYLLLQKQLEQLQEENFR-LETARDDYRIKCeELEKEVLELQHRNEELTSlaeEA 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   132 RALDSE----------LKTYQDQEDEYKSKYdqEAYkhasvqNDfvvLKKdvdevfQSKMDLEGNLESLKEhvcflTRLY 201
Cdd:pfam05622  114 QALKDEmdilressdkVKKLEATVETYKKKL--EDL------GD---LRR------QVKLLEERNAEYMQR-----TLQL 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   202 EEEL-------GQL---KTQADDMSVVLSMDNNRC--LDFSDiiAEVRARYEEITRTSK---AEAEAVFQTkYQELQeSA 266
Cdd:pfam05622  172 EEELkkanalrGQLetyKRQVQELHGKLSEESKKAdkLEFEY--KKLEEKLEALQKEKErliIERDTLRET-NEELR-CA 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   267 QLQGNSMKE----------------AQVQISQLRQAIHRLQSQIGSLR-KQNDSLQSAIADAEQQGEmavrDAQAKLDEL 329
Cdd:pfam05622  248 QLQQAELSQadallspssdpgdnlaAEIMPAEIREKLIRLQHENKMLRlGQEGSYRERLTELQQLLE----DANRRKNEL 323

                          330       340
                   ....*....|....*....|....
gi 755551840   330 EAALRTAKQDMAQMLRDYQELMGT 353
Cdd:pfam05622  324 ETQNRLANQRILELQQQVEELQKA 347
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 117-372 4.77e-08

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 57.49  E-value: 4.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDvdevfqskMDLEGNLESLKEHVCf 196
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED--------LESERAARNKAEKQR- 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   197 ltRLYEEELGQLKTQADDMsvvlsmdnnrcLDFSDIIAEVRARYE-EITRTSKA-EAEAvfQTKYQELQESAQLQGNSMK 274
Cdd:pfam01576  295 --RDLGEELEALKTELEDT-----------LDTTAAQQELRSKREqEVTELKKAlEEET--RSHEAQLQEMRQKHTQALE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   275 EAQVQISQLR-------QAIHRLQSQIGSLRKQNDSLQSAIADAEQ---QGEMAVRDAQAKLDE-----LEAALRTAK-- 337
Cdd:pfam01576  360 ELTEQLEQAKrnkanleKAKQALESENAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSEserqrAELAEKLSKlq 439

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   338 ---------------------QDMAQM---LRDYQELM----------GTKL-SLDVEIAMYRRLLESEE 372
Cdd:pfam01576  440 selesvssllneaegkniklsKDVSSLesqLQDTQELLqeetrqklnlSTRLrQLEDERNSLQEQLEEEE 509
PRK09039 PRK09039
peptidoglycan -binding protein;
202-347 4.79e-08

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 56.13  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  202 EEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARyeeitrTSKAEAE-AVFQTKYQEL-QESAQLQG-----NSMK 274
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS------LSAAEAErSRLQALLAELaGAGAAAEGragelAQEL 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  275 EAQVQISQ--LRQaIHRLQSQIGSLRKQNDSLQSAIADAEQQGemavRDAQAKLDELEAALRTAKQDMAQMLRDY 347
Cdd:PRK09039  126 DSEKQVSAraLAQ-VELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVALAQRVQELNRY 195
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
 56-365 6.33e-08

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.


Pssm-ID: 462752 [Multi-domain]  Cd Length: 307  Bit Score: 55.36  E-value: 6.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    56 QVVKTQEtREIRSLNNQFASFIDKVRflEQQNKVLETKWEL---LQQLQGNRSPQGLECIFETclARLRQQLEELQRerr 132
Cdd:pfam09311   12 QAIQEQE-AETRDQVKKLQEMLRQAN--DQLEKTMKDKKELedkMNQLSEETSNQVSTLAKRN--QKSETLLDELQQ--- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   133 ALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVL----KKDVDEVFQSKMDLEGNLESLKehvcFLTRLYEEELGQL 208
Cdd:pfam09311   84 AFSQAKRNFQDQLAVLMDSREQVSDELVRLQKDNESLqgkhSLHVSLQQAEKFDMPDTVQELQ----ELVLKYREELIEV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   209 KTQADDMSVVLSMDnnrCLDFSDIIAEVRARYEEITRTSKAEAE------AVFQTKYQELQESAQLQGNSMKEAQVQISQ 282
Cdd:pfam09311  160 RTAADHMEEKLKAE---ILFLKEQIQAEQCLKENLEETLQAEIEnckeeiASISSLKVELERIKAEKEQLENGLTEKIRQ 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   283 LRQaihrLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKqdmaQMLRDYqelmgTKLSLDVEIA 362
Cdd:pfam09311  237 LED----LQTTKGSLETQLKKETNEKAAVEQL----VFEEKNKAQRLQTELDVSE----QVQRDF-----VKLSQTLQVQ 299


                   ...
gi 755551840   363 MYR 365
Cdd:pfam09311  300 LER 302
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 182-378 7.04e-08

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 54.61  E-value: 7.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   182 DLEGNLESLKEhvcflTRLYEEELGQLKTQADDmsvvlsmdnnrcldFSDIIAEVRaryEEITRTSKAEAEAVFQ--TKY 259
Cdd:pfam12795   21 DLQQALSLLDK-----IDASKQRAAAYQKALDD--------------APAELRELR---QELAALQAKAEAAPKEilASL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   260 ------QEL-QESAQLQ--GNSMKEAQVQISQLRQAIHRLQSQIGSLRKQ----NDSLQS------AIADAEQ---QGEM 317
Cdd:pfam12795   79 sleeleQRLlQTSAQLQelQNQLAQLNSQLIELQTRPERAQQQLSEARQRlqqiRNRLNGpappgePLSEAQRwalQAEL 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551840   318 AVRDAQAKLDELEAALRTAKQDMAQMLRDYQELmgtKLS-LDVEIAMY------RRLLESEECRISTE 378
Cdd:pfam12795  159 AALKAQIDMLEQELLSNNNRQDLLKARRDLLTL---RIQrLEQQLQALqellneKRLQEAEQAVAQTE 223
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 47-338 1.67e-07

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 55.61  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    47 LIASLQRLFQVVKTQETREIRSLNNQFASFIDkvrfLEQQNKVLETKW-ELLQQLQGNRSPQglecifETCLARLRQQLE 125
Cdd:pfam12128  256 AELRLSHLHFGYKSDETLIASRQEERQETSAE----LNQLLRTLDDQWkEKRDELNGELSAA------DAAVAKDRSELE 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   126 elqrerrALDSELKTYQDQEDEyksKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVcfltrlyeeel 205
Cdd:pfam12128  326 -------ALEDQHGAFLDADIE---TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI----------- 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   206 gqlktqaddmsvvlSMDNNRclDFSDIIAEVRARYEEITRtSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQIS---- 281
Cdd:pfam12128  385 --------------KEQNNR--DIAGIKDKLAKIREARDR-QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKsrlg 447

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   282 -----------------QLRQ---AIHRLQSQIGSLRKQNDSLQSAIADA----EQQGEmAVRDAQAKLDELEAALRTAK 337
Cdd:pfam12128  448 elklrlnqatatpelllQLENfdeRIERAREEQEAANAEVERLQSELRQArkrrDQASE-ALRQASRRLEERQSALDELE 526


                   .
gi 755551840   338 Q 338
Cdd:pfam12128  527 L 527
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-372 1.75e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.52  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCF 196
Cdd:COG4372    47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LtrlyEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEA 276
Cdd:COG4372   127 L----EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  277 QVQISQLRQAIhRLQSQIGSLRKQNDSLQSAIADAEQQG-EMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKL 355
Cdd:COG4372   203 AEAEKLIESLP-RELAEELLEAKDSLEAKLGLALSALLDaLELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281

                         250
                  ....*....|....*..
gi 755551840  356 SLDVEIAMYRRLLESEE 372
Cdd:COG4372   282 ALELEALEEAALELKLL 298
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
83-340 1.78e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   83 LEQQNKVLETKWELLQQLQGNRSPQGLECIfETCLARLRQQLEELQRERRALDSELKTYQDQEDEykskydqeaykhasv 162
Cdd:COG4913   257 IRELAERYAAARERLAELEYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEARLDA--------------- 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  163 qndfvvLKKDVDEVFQSKMDLEGN-LESLKEHVCFLTRLYEE---ELGQLKTQAD--DMSVVLSMDnnrclDFSDIIAEV 236
Cdd:COG4913   321 ------LREELDELEAQIRGNGGDrLEQLEREIERLERELEErerRRARLEALLAalGLPLPASAE-----EFAALRAEA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  237 RARYEEITRTSKAEAEAVFqtkyqelqesaqlqgnsmkEAQVQISQLRQAIHRLQSQIGSLRKQndslQSAIaDAEQQge 316
Cdd:COG4913   390 AALLEALEEELEALEEALA-------------------EAEAALRDLRRELRELEAEIASLERR----KSNI-PARLL-- 443

                         250       260
                  ....*....|....*....|....
gi 755551840  317 mAVRDAqakldeLEAALRTAKQDM 340
Cdd:COG4913   444 -ALRDA------LAEALGLDEAEL 460
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 59-356 2.19e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 55.11  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    59 KTQETREIRSLNNqfasfiDKVRFLEQQNKVLETKWELL----------QQLQGNRSpqglECIFetCLARLRQQLEELQ 128
Cdd:pfam05483  389 KSSELEEMTKFKN------NKEVELEELKKILAEDEKLLdekkqfekiaEELKGKEQ----ELIF--LLQAREKEIHDLE 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   129 RERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEEELGQL 208
Cdd:pfam05483  457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   209 KT-QADDMSVVLSMDNNRcldfsdiiAEVRARYEEIT-RTSKAEaEAVFQTKYQELQESAQlqgnsMKEAQVQISQLRQA 286
Cdd:pfam05483  537 ENlEEKEMNLRDELESVR--------EEFIQKGDEVKcKLDKSE-ENARSIEYEVLKKEKQ-----MKILENKCNNLKKQ 602

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755551840   287 IHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQMLRDYQ-ELMGTKLS 356
Cdd:pfam05483  603 IENKNKNIEELHQENKALKKKGSAENKQ----LNAYEIKVNKLELELASAKQKFEEIIDNYQkEIEDKKIS 669
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
233-385 2.39e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.02  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  233 IAEVRARYEEitrtskAEAE-AVFQTKYQ--ELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIA 309
Cdd:COG3206   184 LPELRKELEE------AEAAlEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551840  310 DAEQQGEmavrdaqakLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECRISTEHTSQVTV 385
Cdd:COG3206   258 ELLQSPV---------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
mukB PRK04863
chromosome partition protein MukB;
122-348 2.58e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 54.96  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  122 QQLEELQRERRALDSELKTYQDQEDEYKSKYDQ--EAY----KHA---------SVQNDFVVLKKDVDEVFQSKMDLE-- 184
Cdd:PRK04863  837 AELRQLNRRRVELERALADHESQEQQQRSQLEQakEGLsalnRLLprlnlladeTLADRVEEIREQLDEAEEAKRFVQqh 916

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  185 GNLESLKEHVCFLTRLYEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAeVRAR--YEEITRTSKAEAEAVfqTKYQEL 262
Cdd:PRK04863  917 GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ-RRAHfsYEDAAEMLAKNSDLN--EKLRQR 993

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  263 QESAQLQGNSMKEAQVQI-SQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKL----DELEAALRTAK 337
Cdd:PRK04863  994 LEQAEQERTRAREQLRQAqAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERArarrDELHARLSANR 1073

                         250
                  ....*....|.
gi 755551840  338 QDMAQMLRDYQ 348
Cdd:PRK04863 1074 SRRNQLEKQLT 1084
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-370 2.92e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYdqeaykhASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHvcf 196
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKE--- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 ltrlyEEEL-GQLKTQADDMSVVLsmdnnrcldfsdiiaevRARYeeitRTSKAEAEAVF--QTKYQELQESAQLQGNSM 273
Cdd:COG4942    92 -----IAELrAELEAQKEELAELL-----------------RALY----RLGRQPPLALLlsPEDFLDAVRRLQYLKYLA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  274 KEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQG---EMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQEL 350
Cdd:COG4942   146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                         250       260
                  ....*....|....*....|
gi 755551840  351 MGTKLSLDVEIAMYRRLLES 370
Cdd:COG4942   226 EALIARLEAEAAAAAERTPA 245
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 47-387 3.65e-07

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    47 LIASLQrlfqvvktQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGNRSPQGLECI-FETCLARLRQQLE 125
Cdd:pfam15921  501 LTASLQ--------EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIE 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   126 EL-----QRERRALDSELKTYQDQEDEYKSKYDQEAYKhasVQNDfvvlKKD--VDEVFQSKMDLEgnLESLKehvcfLT 198
Cdd:pfam15921  573 NMtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFK---ILKD----KKDakIRELEARVSDLE--LEKVK-----LV 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   199 RLYEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEvrarYEEITRTskaeaeavFQTKYQELQESAQLQGNSMKEAQV 278
Cdd:pfam15921  639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED----YEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQS 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   279 QISQLRQAIHRL--------------QSQIGSLRKQNDSLQSAIADAEQQGEMA------VRDAQAKLDELEAALRTAKQ 338
Cdd:pfam15921  707 ELEQTRNTLKSMegsdghamkvamgmQKQITAKRGQIDALQSKIQFLEEAMTNAnkekhfLKEEKNKLSQELSTVATEKN 786

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755551840   339 DMA---QMLRDYQELMGTKLSlDVEIAMYRRLLESEECRISTEHTSQVTVSI 387
Cdd:pfam15921  787 KMAgelEVLRSQERRLKEKVA-NMEVALDKASLQFAECQDIIQRQEQESVRL 837
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 37-346 3.72e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 54.41  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    37 RVVLIAKNDFLIASLQRLFQ--VVKTQETREIRSLNNQFASFIDKvrfLEQQ----NKVLETKWELLQQLQGNRSPqgLE 110
Cdd:pfam01576  235 RAQLAKKEEELQAALARLEEetAQKNNALKKIRELEAQISELQED---LESEraarNKAEKQRRDLGEELEALKTE--LE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   111 CIFETCLAR--LRQQLE-ELQRERRALDSELKTYQDQEDEYKSKYDQ-------------------EAYKHAsVQNDFVV 168
Cdd:pfam01576  310 DTLDTTAAQqeLRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQaleelteqleqakrnkanlEKAKQA-LESENAE 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   169 LKKDVDEVFQSKMD-------LEGNLESLKEHVCFLTRLYEE---ELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRA 238
Cdd:pfam01576  389 LQAELRTLQQAKQDsehkrkkLEGQLQELQARLSESERQRAElaeKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   239 RYEEITRTSKAEAEAVFQ--TKYQELQESAqlqgNSMKEAQVQISQLRQAIHR----LQSQIGSLRKQNDSLQSAIADAE 312
Cdd:pfam01576  469 QLQDTQELLQEETRQKLNlsTRLRQLEDER----NSLQEQLEEEEEAKRNVERqlstLQAQLSDMKKKLEEDAGTLEALE 544

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 755551840   313 QQGEMAVRDAQAK---LDELEAA---LRTAKQDMAQMLRD 346
Cdd:pfam01576  545 EGKKRLQRELEALtqqLEEKAAAydkLEKTKNRLQQELDD 584
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 230-372 5.07e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  230 SDIIAEVRARYEEITRtskaEAEAvfQTKYQELQE-----SAQLQGNSMKEAQ--------------------------- 277
Cdd:COG1196   192 EDILGELERQLEPLER----QAEK--AERYRELKEelkelEAELLLLKLRELEaeleeleaeleeleaeleeleaelael 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  278 -VQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAV---RDAQAKLDELEAALRTAKQDMAQMLRDYQELMGT 353
Cdd:COG1196   266 eAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEE 345

                         170
                  ....*....|....*....
gi 755551840  354 KLSLDVEIAMYRRLLESEE 372
Cdd:COG1196   346 LEEAEEELEEAEAELAEAE 364
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
64-358 5.29e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.61  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   64 REIRSLNNQFASFIDKVRFLEQQNKvletkwELLQQLQGNRSpqglecifetclAR--LRQQLEELQRERRALDSELKTY 141
Cdd:COG1340    29 EKRDELNEELKELAEKRDELNAQVK------ELREEAQELRE------------KRdeLNEKVKELKEERDELNEKLNEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  142 QDQEDEYKSKYDQEAYKHASVQNdfvvLKKDVDEV---FQ-SKMDLEgnleslKEhvcflTRLYEEeLGQLKTQADDMSV 217
Cdd:COG1340    91 REELDELRKELAELNKAGGSIDK----LRKEIERLewrQQtEVLSPE------EE-----KELVEK-IKELEKELEKAKK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  218 VLsmdnnrclDFSDIIAEVRARYEEItrtsKAEAEAVFQtKYQELQESAQLQGNSM---------------------KEA 276
Cdd:COG1340   155 AL--------EKNEKLKELRAELKEL----RKEAEEIHK-KIKELAEEAQELHEEMielykeadelrkeadelhkeiVEA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  277 QVQISQLRQAIHRLQSQIGSLRKQNDSLQsaiadaEQQGEMAVRDAQAKLDELeaalrtAKQDMAQMLRdyqelmGTKLS 356
Cdd:COG1340   222 QEKADELHEEIIELQKELRELRKELKKLR------KKQRALKREKEKEELEEK------AEEIFEKLKK------GEKLT 283


                  ..
gi 755551840  357 LD 358
Cdd:COG1340   284 TE 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
117-370 7.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKydQEAYKhasvqndfvvlkkDVDEVFQSKMDLEGnleslkehvcf 196
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQER--REALQ-------------RLAEYSWDEIDVAS----------- 665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 ltrlYEEELGQLKTQADdmsvvlsmdnnRCLDFSDIIAEVRARYEEitrtskAEAEavfqtkYQEL-QESAQLQGNsMKE 275
Cdd:COG4913   666 ----AEREIAELEAELE-----------RLDASSDDLAALEEQLEE------LEAE------LEELeEELDELKGE-IGR 717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  276 AQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMA-------VRDAQAKLDELEAALRTAKQDMAQMLRDYQ 348
Cdd:COG4913   718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGdaverelRENLEERIDALRARLNRAEEELERAMRAFN 797

                         250       260
                  ....*....|....*....|....*.
gi 755551840  349 EL-MGTKLSLDVEIA---MYRRLLES 370
Cdd:COG4913   798 REwPAETADLDADLEslpEYLALLDR 823
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 52-347 7.38e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 53.51  E-value: 7.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    52 QRLFQVVKtqETRE-IRSLNNQFASFIDKVRFLEQQNKVLETKWELL------QQLQGNRSPQGLECIFE------TCLA 118
Cdd:TIGR00606  684 QRVFQTEA--ELQEfISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgRQSIIDLKEKEIPELRNklqkvnRDIQ 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   119 RLRQQLEELQRERRALDSELKT-------------YQDQEDEYKSKYDQEAYKHASVQNDfvvlkKDVDEVFQSKMDLEG 185
Cdd:TIGR00606  762 RLKNDIEEQETLLGTIMPEEESakvcltdvtimerFQMELKDVERKIAQQAAKLQGSDLD-----RTVQQVNQEKQEKQH 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   186 NLESLKEHVCFLTRLYEEE----------LGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEItRTSKAEAEAVF 255
Cdd:TIGR00606  837 ELDTVVSKIELNRKLIQDQqeqiqhlkskTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI-KDAKEQDSPLE 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   256 QTKYQELQESAQL---QGNSMKEAQVQISQLRQaihRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAA 332
Cdd:TIGR00606  916 TFLEKDQQEKEELissKETSNKKAQDKVNDIKE---KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH 992

                          330
                   ....*....|....*
gi 755551840   333 LRTAKQDMAQMLRDY 347
Cdd:TIGR00606  993 QEKINEDMRLMRQDI 1007
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-372 7.51e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 7.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCF 196
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LTRLY---EEELGQLKTQADdmsvvlsmdnnrcldfsDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSM 273
Cdd:COG4372   141 LQSEIaerEEELKELEEQLE-----------------SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  274 KEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADA---EQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQEL 350
Cdd:COG4372   204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAlelEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283

                         250       260
                  ....*....|....*....|..
gi 755551840  351 MGTKLSLDVEIAMYRRLLESEE 372
Cdd:COG4372   284 ELEALEEAALELKLLALLLNLA 305
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 56-382 8.63e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 52.82  E-value: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    56 QVVKTQETREIRSL----NNQFASFIDKVRFLEQQNKVLETKWellqqlqgnrspQGLEcifetclaRLRQQLEELQRER 131
Cdd:pfam05557  106 ISCLKNELSELRRQiqraELELQSTNSELEELQERLDLLKAKA------------SEAE--------QLRQNLEKQQSSL 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   132 raLDSELKTyqdQEDEYkskydqeaykHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLyEEELGQLKTQ 211
Cdd:pfam05557  166 --AEAEQRI---KELEF----------EIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN-IENKLLLKEE 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   212 ADDMSVVLSmdnnrcldfsdiiaevraRYEeitrtsKAEAEAV--------FQTKYQELQESAQLQGNSMK---EAQVQI 280
Cdd:pfam05557  230 VEDLKRKLE------------------REE------KYREEAAtlelekekLEQELQSWVKLAQDTGLNLRspeDLSRRI 285

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   281 SQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKqdmAQMLRdyqeLMGTKLSLDVE 360
Cdd:pfam05557  286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQE----LAQYLKKIEDLNKKLKRHK---ALVRR----LQRRVLLLTKE 354

                          330       340
                   ....*....|....*....|..
gi 755551840   361 IAMYRRLLESEECRISTEHTSQ 382
Cdd:pfam05557  355 RDGYRAILESYDKELTMSNYSP 376
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 231-379 9.21e-07

type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274165 [Multi-domain]  Cd Length: 166  Bit Score: 49.99  E-value: 9.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   231 DIIAEVRARYEEITRTSKAEAEAVFQTKYQE-LQESAQLQGNSMKEAQVQISQL-RQAIHRLQSQIgslrkqNDSLQSaI 308
Cdd:TIGR02499   17 AILAAARQRAEAILADAEEEAEASRQLGYEQgLEQFWQEAAAQLAEWQQEAEQLeASLEERLAELV------LQALEQ-I 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551840   309 ADAEQQGEMAVRDAQ----AKLDELEAALRTAKQD---MAQMLRDYQELMGTKLSLDVEIAmyrrlleSEECRISTEH 379
Cdd:TIGR02499   90 LGEYDEPERLVRLLRqllrAVANQGRLTLRVHPEQldeVREALAERLALEPWELEPDASLA-------PGACVLETES 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-369 1.08e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   235 EVRARYEEITRTS--------KAEAEAVFQT--KYQELQESAQLQgnsMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSL 304
Cdd:TIGR02168  217 ELKAELRELELALlvlrleelREELEELQEElkEAEEELEELTAE---LQELEEKLEELRLEVSELEEEIEELQKELYAL 293

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551840   305 QSAIADAEQQGEMAV---RDAQAKLDELEAALRTAKQ-------DMAQMLRDYQELMGTKLSLDVEIAMYRRLLE 369
Cdd:TIGR02168  294 ANEISRLEQQKQILRerlANLERQLEELEAQLEELESkldelaeELAELEEKLEELKEELESLEAELEELEAELE 368
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
76-301 1.10e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   76 FIDKVRFLEQQNKVLETKWELLQQLQGNrspqglecifetcLARLRQQLEELQRERRALDSELKTYQDQEDEYKskydqe 155
Cdd:COG4717    69 NLKELKELEEELKEAEEKEEEYAELQEE-------------LEELEEELEELEAELEELREELEKLEKLLQLLP------ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  156 aykhasvqndfvvLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLyEEELGQLKTQADDmsvvlsmdnnrcldfsdiIAE 235
Cdd:COG4717   130 -------------LYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAELAE------------------LQE 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551840  236 VRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQN 301
Cdd:COG4717   178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 117-354 1.20e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.69  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQeaykhasvqndfvvLKKDVDEvfqskmdLEGNLESLKEHvcf 196
Cdd:COG1579    19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------------LEKEIKR-------LELEIEEVEAR--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LTRlYEEELGQLKtqaddmsvvlsmdNNRcldfsdiiaEVRARYEEITrtskaeaeavFQTKYQELQESAQLqgnsmkEA 276
Cdd:COG1579    75 IKK-YEEQLGNVR-------------NNK---------EYEALQKEIE----------SLKRRISDLEDEIL------EL 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  277 QVQISQLRQAIHRLQSQIgslrkqnDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDM-AQMLRDYQELMGTK 354
Cdd:COG1579   116 MERIEELEEELAELEAEL-------AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRK 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-368 1.68e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  265 SAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEAALRTAKQDMAQML 344
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELE 89

                          90       100
                  ....*....|....*....|....
gi 755551840  345 RDYQELmgtKLSLDVEIAMYRRLL 368
Cdd:COG4942    90 KEIAEL---RAELEAQKEELAELL 110
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
 38-330 1.73e-06

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 51.23  E-value: 1.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    38 VVLIAKNDFLIASLQRLFQVVKtqetREIRSLNNQFASFIDKVRFLEQQNKVLETKWE--------------LLQQLQGN 103
Cdd:pfam04108   27 VVLLAKIAFLRRGLSVQLANLE----KVREGLEKVLNELKKDFKQLLKDLDAALERLEetldklrntpvepaLPPGEEKQ 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   104 R------SPQGLECIFEtclaRLRQQLEELQRERRALDSELKTYqdqEDEYKSKydQEAYKHASVQNDFVVLKKDV-DEV 176
Cdd:pfam04108  103 KtlldfiDEDSVEILRD----ALKELIDELQAAQESLDSDLKRF---DDDLRDL--QKELESLSSPSESISLIPTLlKEL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   177 FQSKMDLEGNLESLKEH---VCFLTRLYEEELgqlktqaDDMSVVLSMDNnrcLDFSDIIAEVRARYEEITRTSKaeaea 253
Cdd:pfam04108  174 ESLEEEMASLLESLTNHydqCVTAVKLTEGGR-------AEMLEVLENDA---RELDDVVPELQDRLDEMENNYE----- 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551840   254 vfqtKYQELQESAqlqgNSMKEAQVQISQLrqaIHRLQSQIgslrkqnDSLQSAIADAEQQGEMAVRDAQAKLDELE 330
Cdd:pfam04108  239 ----RLQKLLEQK----NSLIDELLSALQL---IAEIQSRL-------PEYLAALKEFEERWEEEKETIEDYLSELE 297
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 63-351 1.78e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.82  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    63 TREIRSLNNQFASFIDKVRFLEQQNKVLetkwellqqlqgnrSPQGLEciFETCLARLRQ-------QLEELQRERRALD 135
Cdd:pfam07888  114 SEEKDALLAQRAAHEARIRELEEDIKTL--------------TQRVLE--RETELERMKErakkagaQRKEEEAERKQLQ 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   136 SELKTYQDQE-------DEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLE---SLKEHVCFLTRLYE--- 202
Cdd:pfam07888  178 AKLQQTEEELrslskefQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEelrSLQERLNASERKVEglg 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   203 EELGQLKTQADDmsvvlsmdnnrcldfsdIIAEV-RARYEEITRTSK-AEAE-AVFQTKYQELQESAQLQGNSMKEaQVQ 279
Cdd:pfam07888  258 EELSSMAAQRDR-----------------TQAELhQARLQAAQLTLQlADASlALREGRARWAQERETLQQSAEAD-KDR 319

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551840   280 ISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELM 351
Cdd:pfam07888  320 IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
232-383 2.09e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  232 IIAEVRARYEEITRTSKAEAEaVFQTKYQELQE---SAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAI 308
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPE-LNLKELKELEEelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  309 ADAEQQGEMavRDAQAKLDELEAALRTAKQDMAQmlrdYQELMGTKLSLDVEIAMYRRLLESEECRISTEHTSQV 383
Cdd:COG4717   126 QLLPLYQEL--EALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-372 2.81e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQeaykhasvqndfvvLKKDVDEvfqskmdLEGNLESLKEHVcf 196
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ--------------LEEELEE-------LNEQLQAAQAEL-- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 ltRLYEEELGQLKTQADdmsvvlsmdnnrcldfsdiiaEVRARYEEItrtsKAEAEAVfQTKYQELQESAQLQGNSMKEA 276
Cdd:COG4372    97 --AQAQEELESLQEEAE---------------------ELQEELEEL----QKERQDL-EQQRKQLEAQIAELQSEIAER 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  277 QVQISQLRQAIHRLQSQIGSLRKQNDSLqsAIADAEQQGEMAVRDAQakldelEAALRTAKQDMAQMLRDYQELMGTKLS 356
Cdd:COG4372   149 EEELKELEEQLESLQEELAALEQELQAL--SEAEAEQALDELLKEAN------RNAEKEEELAEAEKLIESLPRELAEEL 220

                         250
                  ....*....|....*.
gi 755551840  357 LDVEIAMYRRLLESEE 372
Cdd:COG4372   221 LEAKDSLEAKLGLALS 236
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
118-370 3.42e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  118 ARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYD---------QEAYKHASVQNDFV-----VLKKDVDEVFQSKMDL 183
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEeleeeieelRERFGDAPVDLGNAedfleELREERDELREREAEL 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  184 EGNLESLKEHVCFLTRLYEE----ELGQlktQADDMSVVLSMDNNR------CLDFSDIIAEVRARYEEITRTSKA-EAE 252
Cdd:PRK02224  432 EATLRTARERVEEAEALLEAgkcpECGQ---PVEGSPHVETIEEDRerveelEAELEDLEEEVEEVEERLERAEDLvEAE 508

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  253 AVFQTKYQELQESAQLqgnsmkeaqvqISQLRQAIHRLQSQIGSLRKQNDSLQsaiADAEQQGEmavrDAQAKLDELEAA 332
Cdd:PRK02224  509 DRIERLEERREDLEEL-----------IAERRETIEEKRERAEELRERAAELE---AEAEEKRE----AAAEAEEEAEEA 570

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 755551840  333 LRTAK---QDMAQmLRDYQELMGTKLSLDVEIAMYRRLLES 370
Cdd:PRK02224  571 REEVAelnSKLAE-LKERIESLERIRTLLAAIADAEDEIER 610
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 201-372 4.61e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 50.51  E-value: 4.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   201 YEEELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQV-- 278
Cdd:pfam05557   25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAre 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   279 -------QISQLRQAIHRLQSQIGS-------LRKQNDSLQSAIADAEQ--------QGEMAvrDAQAKLDELE------ 330
Cdd:pfam05557  105 visclknELSELRRQIQRAELELQStnseleeLQERLDLLKAKASEAEQlrqnlekqQSSLA--EAEQRIKELEfeiqsq 182

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840   331 ----AALRTAKQDMAQM---------LRD----YQELMGTKLSLDVEIAMYRRLLESEE 372
Cdd:pfam05557  183 eqdsEIVKNSKSELARIpelekelerLREhnkhLNENIENKLLLKEEVEDLKRKLEREE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-305 7.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   31 LGWSTcrvvlIAKNDFLIASLQRLFQVVKTQETR------EIRSLNNQFASFIDKVRFLEQQNKVLETKWELL---QQLQ 101
Cdd:COG4913   604 LGFDN-----RAKLAALEAELAELEEELAEAEERlealeaELDALQERREALQRLAEYSWDEIDVASAEREIAeleAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  102 GNRSPQGLecifetcLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQ--EAYKHASVQNDFVVLKKDVDEVFqs 179
Cdd:COG4913   679 RLDASSDD-------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeEELDELQDRLEAAEDLARLELRA-- 749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  180 kmDLEGNLESL--KEHVCFLTRLYEEELGQLKTQAddmsvvlsmdnNRCLD-FSDIIAEVRARYEEITRTSKAEAEAV-- 254
Cdd:COG4913   750 --LLEERFAAAlgDAVERELRENLEERIDALRARL-----------NRAEEeLERAMRAFNREWPAETADLDADLESLpe 816

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755551840  255 FQTKYQELQES---------AQLQGNSMKEAQVQI-SQLRQAIHRLQSQIGSLrkqNDSLQ 305
Cdd:COG4913   817 YLALLDRLEEDglpeyeerfKELLNENSIEFVADLlSKLRRAIREIKERIDPL---NDSLK 874
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 120-351 1.80e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   120 LRQQLEELQRERRALDSELKTYQDQEDEykskyDQEAYKHASVQNDFVV--LKKDVDEvfqskmdLEGNLESLKEHVcfl 197
Cdd:pfam07888   32 LQNRLEECLQERAELLQAQEAANRQREK-----EKERYKRDREQWERQRreLESRVAE-------LKEELRQSREKH--- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   198 trlyeEELGQLKTQADDMSVVLSMDNNRCLDFSdiiAEVRARYEEITRTSKAEAEAVF--QTKYQELQESAQLQGNSMKE 275
Cdd:pfam07888   97 -----EELEEKYKELSASSEELSEEKDALLAQR---AAHEARIRELEEDIKTLTQRVLerETELERMKERAKKAGAQRKE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   276 AQVQISQLRQaihRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRdAQAKLDELEAALRTAKQDMAQM------LRDYQE 349
Cdd:pfam07888  169 EEAERKQLQA---KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENealleeLRSLQE 244


                   ..
gi 755551840   350 LM 351
Cdd:pfam07888  245 RL 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-366 1.94e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  171 KDVDEVFQSKM----DLEGNLESLKEHVCFLTRLYE-------------------EELGQLKTQADDMSVVLSM----DN 223
Cdd:COG4913   207 GDLDDFVREYMleepDTFEAADALVEHFDDLERAHEaledareqiellepirelaERYAAARERLAELEYLRAAlrlwFA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  224 NRCLD-FSDIIAEVRARY----EEITRTSKAEAEAvfQTKYQELQES-AQLQGNSMKEAQVQISQLRQAIHRLQSQIGSL 297
Cdd:COG4913   287 QRRLElLEAELEELRAELarleAELERLEARLDAL--REELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARL 364

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  298 RKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRR 366
Cdd:COG4913   365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
46 PHA02562
endonuclease subunit; Provisional
 78-364 2.58e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 48.09  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   78 DKVRFLEQQNKVLETKWELLQQlqgnrspqglecifetclaRLRQQlEELQRERRALDSElktyqdQEDEYKSKYDQEAY 157
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQ-------------------QIKTY-NKNIEEQRKKNGE------NIARKQNKYDELVE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  158 KHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKehvcfltrlyeEELGQLKTQADDMSVVLSM--DNNRCLDFSDIIAE 235
Cdd:PHA02562  228 EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLN-----------TAAAKIKSKIEQFQKVIKMyeKGGVCPTCTQQISE 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  236 VRARYEEITrTSKAEAeavfQTKYQELQESAQlqgnSMKEAQVQISQLRQAIHRLQSQIgslRKQNDSLQSAIADAeqqg 315
Cdd:PHA02562  297 GPDRITKIK-DKLKEL----QHSLEKLDTAID----ELEEIMDEFNEQSKKLLELKNKI---STNKQSLITLVDKA---- 360

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755551840  316 emavRDAQAKLDELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMY 364
Cdd:PHA02562  361 ----KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
117-323 3.21e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRA---------LDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGN- 186
Cdd:COG3206   184 LPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSp 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  187 -LESLKEhvcfltrlyeeELGQLKTQADDMSVVLSMDNNRcldfsdiIAEVRARYEEITRTSKAEAEAVF---QTKYQEL 262
Cdd:COG3206   264 vIQQLRA-----------QLAELEAELAELSARYTPNHPD-------VIALRAQIAALRAQLQQEAQRILaslEAELEAL 325

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551840  263 QES-AQLQG--NSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVRDAQ 323
Cdd:COG3206   326 QAReASLQAqlAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 117-346 3.67e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.52  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQrerrALDSELKT-YQDQEDEYKSKYDQeaykhaSVQNDFVVLKKDVDEVFQskmDLEGNLESLKEHvc 195
Cdd:PRK04778  207 LAALEQIMEEIP----ELLKELQTeLPDQLQELKAGYRE------LVEEGYHLDHLDIEKEIQ---DLKEQIDENLAL-- 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  196 fLTRLY----EEELGQLKTQADDMSvvlsmdnnrcldfsDII-AEVRARY---EEITRTSKAEAEAvfQTKYQELQ-ESA 266
Cdd:PRK04778  272 -LEELDldeaEEKNEEIQERIDQLY--------------DILeREVKARKyveKNSDTLPDFLEHA--KEQNKELKeEID 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  267 QLQGN---SMKEAQVQisqlrqaiHRLQSQIGSLRKQNDSLQSAIADaeqqGEMAVRDAQAKLDELEAALRTAK------ 337
Cdd:PRK04778  335 RVKQSytlNESELESV--------RQLEKQLESLEKQYDEITERIAE----QEIAYSELQEELEEILKQLEEIEkeqekl 402


                  ....*....
gi 755551840  338 QDMAQMLRD 346
Cdd:PRK04778  403 SEMLQGLRK 411
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 63-382 3.82e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 47.73  E-value: 3.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    63 TREIRSLNNQFASFIDKVRFLEQQ----NKVLETKWELLQQLQGNrspqglecIFETC--------LARLRQQLEELQRE 130
Cdd:TIGR00606  583 SKEINQTRDRLAKLNKELASLEQNknhiNNELESKEEQLSSYEDK--------LFDVCgsqdeesdLERLKEEIEKSSKQ 654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   131 RRALDSELKTYqdqeDEYKSKYDQEAYKHASV-QNDFVVlKKDVDEV---FQSKMDL-EGNLESLKEHVCFLTRLYEEEL 205
Cdd:TIGR00606  655 RAMLAGATAVY----SQFITQLTDENQSCCPVcQRVFQT-EAELQEFisdLQSKLRLaPDKLKSTESELKKKEKRRDEML 729

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   206 GQLKTQADDMSVV---LSMDNNRCLDFSDIIAEVRARYEEI-----TRTSKAEAEAVFQTK---YQELQEsaQLQGNSMK 274
Cdd:TIGR00606  730 GLAPGRQSIIDLKekeIPELRNKLQKVNRDIQRLKNDIEEQetllgTIMPEEESAKVCLTDvtiMERFQM--ELKDVERK 807

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   275 EAQV-----------QISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemaVRDAQAKLDELEA---ALRTAKQDM 340
Cdd:TIGR00606  808 IAQQaaklqgsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ----IQHLKSKTNELKSeklQIGTNLQRR 883

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755551840   341 AQMLRDYQELMGTKLSLDVEIAMYR-----------RLLESEECRISTEHTSQ 382
Cdd:TIGR00606  884 QQFEEQLVELSTEVQSLIREIKDAKeqdspletfleKDQQEKEELISSKETSN 936
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 242-348 3.99e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  242 EITRTSKAEAEAVfQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemavrd 321
Cdd:COG4942    20 DAAAEAEAELEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE------- 91

                          90       100
                  ....*....|....*....|....*..
gi 755551840  322 aqakLDELEAALRTAKQDMAQMLRDYQ 348
Cdd:COG4942    92 ----IAELRAELEAQKEELAELLRALY 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-372 4.81e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  249 AEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQND--SLQSAIADAEQQGEmAVRDAQAKL 326
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELE-RLDASSDDL 687

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755551840  327 DELEAALRTAKQDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEE 372
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 63-285 5.33e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    63 TREIRSLNNQFASFIDKVRFLEQQ---------------NKVLETKWEL---LQQLQGNRSPQGLECI-FETCLARLRQQ 123
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKEREledaeerlakleaeiDKLLAEIEELereIEEERKRRDKLTEEYAeLKEELEDLRAE 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   124 LEELQRERRALDSELKTYQDQEDEYKSKYDQeaykhasvqndfvvLKKDVDEVFQSKMDLEGNLESLKEHvcfLTRLyEE 203
Cdd:TIGR02169  373 LEEVDKEFAETRDELKDYREKLEKLKREINE--------------LKRELDRLQEELQRLSEELADLNAA---IAGI-EA 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   204 ELGQLKTQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEITRTskaeaeavfQTKYQELQESAQLQgNSMKEAQVQISQL 283
Cdd:TIGR02169  435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE---------YDRVEKELSKLQRE-LAEAEAQARASEE 504


                   ..
gi 755551840   284 RQ 285
Cdd:TIGR02169  505 RV 506
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
233-343 5.94e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 46.58  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  233 IAEVRARYEEITRTSKAEAE--------AVFQTKYQELQESAQLQGNSMKE---AQVQISQLRQAIHRLQSQIGSLRKQN 301
Cdd:COG1566    92 LAAAEAQLARLEAELGAEAEiaaaeaqlAAAQAQLDLAQRELERYQALYKKgavSQQELDEARAALDAAQAQLEAAQAQL 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755551840  302 DSLQSAIADAEQqgemaVRDAQAKLDELEAALRTAKQDMAQM 343
Cdd:COG1566   172 AQAQAGLREEEE-----LAAAQAQVAQAEAALAQAELNLART 208
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
257-362 6.44e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 45.20  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  257 TKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSL--QSAIADAEQQ-----GEMAVRDAQAKLDEL 329
Cdd:COG1842    91 ERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKvnealSGIDSDDATSALERM 170

                          90       100       110
                  ....*....|....*....|....*....|....
gi 755551840  330 EaalrtAKQD-MAQMLRDYQELMGTKlSLDVEIA 362
Cdd:COG1842   171 E-----EKIEeMEARAEAAAELAAGD-SLDDELA 198
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 275-349 7.38e-05

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 46.26  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   275 EAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQ-----------GEMAVRDAQAKLDELEAALRTAKQDMAQM 343
Cdd:TIGR04320  265 TAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKElanaqaqalqtAQNNLATAQAALANAEARLAKAKEALANL 344


                   ....*.
gi 755551840   344 LRDYQE 349
Cdd:TIGR04320  345 NADLAK 350
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 121-337 8.40e-05

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.39  E-value: 8.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   121 RQQLEELQRERRALDSELKT----YQDQEDEYKSKYD--QEAYKHASVQNdFVVLKKDVDEVFQskmDLEGNLESLKEHv 194
Cdd:pfam06160  178 REVLEKLEEETDALEELMEDipplYEELKTELPDQLEelKEGYREMEEEG-YALEHLNVDKEIQ---QLEEQLEENLAL- 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   195 cfltrlyeeeLGQLKTqaDDMSVVLSMDNNRCLDFSDII-AEVRARYE-----EITRTSKAEAEAVFQ---TKYQELQES 265
Cdd:pfam06160  253 ----------LENLEL--DEAEEALEEIEERIDQLYDLLeKEVDAKKYveknlPEIEDYLEHAEEQNKelkEELERVQQS 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   266 AQLQGNsmkEAQVQisqlrqaiHRLQSQIGSLRKQNDSLQSAIAD----------------------AEQQGEMA----- 318
Cdd:pfam06160  321 YTLNEN---ELERV--------RGLEKQLEELEKRYDEIVERLEEkevayselqeeleeileqleeiEEEQEEFKeslqs 389

                          250       260
                   ....*....|....*....|...
gi 755551840   319 ----VRDAQAKLDELEAALRTAK 337
Cdd:pfam06160  390 lrkdELEAREKLDEFKLELREIK 412
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 122-348 9.55e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.48  E-value: 9.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  122 QQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQ--NDFVVLKKDvDEVFQSKMDLEGNLESLKEHVCFLtR 199
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNklLPQANLLAD-ETLADRLEELREELDAAQEAQAFI-Q 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  200 LYEEELGQLKTQADdmsvVLSMDNnrcLDFsdiiAEVRARYEEIT---RTSKAEAEA---VFQTK----YQElqESAQLQ 269
Cdd:COG3096   914 QHGKALAQLEPLVA----VLQSDP---EQF----EQLQADYLQAKeqqRRLKQQIFAlseVVQRRphfsYED--AVGLLG 980

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  270 GNS---------MKEAQVQISQLRQAIHRLQSQ-------IGSLRKQNDSLQSAIADAEQQ-GEMAVRD-------AQAK 325
Cdd:COG3096   981 ENSdlneklrarLEQAEEARREAREQLRQAQAQysqynqvLASLKSSRDAKQQTLQELEQElEELGVQAdaeaeerARIR 1060

                         250       260
                  ....*....|....*....|...
gi 755551840  326 LDELEAALRTAKQDMAQMLRDYQ 348
Cdd:COG3096  1061 RDELHEELSQNRSRRSQLEKQLT 1083
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 238-349 9.71e-05

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


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 43.54  E-value: 9.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   238 ARYEEITRTSKAEAEAVFQTKYQELQESAQLQGNSMKE----------------AQVQISQ-LRQAIHRLQSQIGSLRKQ 300
Cdd:pfam07321    2 RRLLRVKHLREDRAEKAVKRQEQALAAARAAHQQAQASlqdyrawrpqeeqrlyAEIQGKLvLLKELEKVKQQVALLREN 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 755551840   301 NDSLQSAIADAEQQGEMAVRDAQAKLDELEAAlRTAKQDMAQMLRDYQE 349
Cdd:pfam07321   82 EADLEKQVAEARQQLEAEREALRQARQALAEA-RRAVEKFAELVRLVQA 129
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 48-342 1.16e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    48 IASLQRLFQVVKTQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQgnrspqglecifetclarlrQQLEEL 127
Cdd:TIGR04523  241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK--------------------SEISDL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   128 QRERRA-----LDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDvdevfqsKMDLEGNLESLKEHVcfltrlyE 202
Cdd:TIGR04523  301 NNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE-------LTNSESENSEKQREL-------E 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   203 EELGQLKTqaddmsvvlsmdnnrcldfsdIIAEVRARYEEIT--RTSKAEAEavfqTKYQELQESAQLQGNSMKEAQV-- 278
Cdd:TIGR04523  367 EKQNEIEK---------------------LKKENQSYKQEIKnlESQINDLE----SKIQNQEKLNQQKDEQIKKLQQek 421

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   279 -----QISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQqgemaVRDAQ-AKLDELEAALRTAKQDMAQ 342
Cdd:TIGR04523  422 ellekEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----TRESLeTQLKVLSRSINKIKQNLEQ 486
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 59-209 1.54e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    59 KTQETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQqLQGNRSPQGLEcIFETCLARLRQQLEELQRERRALDSEL 138
Cdd:TIGR04523  435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS-RSINKIKQNLE-QKQKELKSKEKELKKLNEEKKELEEKV 512

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755551840   139 KTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDevfqsKMDLEGNLESLKEHVcfltRLYEEELGQLK 209
Cdd:TIGR04523  513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-----KDDFELKKENLEKEI----DEKNKEIEELK 574
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 112-216 1.99e-04

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 42.24  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   112 IFETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQEAYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLK 191
Cdd:pfam07926    5 SLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEAESAK 84

                           90       100       110
                   ....*....|....*....|....*....|..
gi 755551840   192 EH-----VCFLTR--LYEEELGQLKTQADDMS 216
Cdd:pfam07926   85 AEleeseESWEEQkkELEKELSELEKRIEDLN 116
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
272-350 2.29e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.66  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  272 SMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMAVR---------------DAQAKLDELEAALRTA 336
Cdd:COG1842    31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEkgredlarealerkaELEAQAEALEAQLAQL 110

                          90
                  ....*....|....
gi 755551840  337 KQDMAQMLRDYQEL 350
Cdd:COG1842   111 EEQVEKLKEALRQL 124
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 252-346 2.52e-04

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 42.19  E-value: 2.52e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    252 EAVFQtKYQELQE-SAQLQgnsmKEAQVQISQLRQAIHRLQSQIGSLRKQNDSL-QSAIADAEQQGEMAVRDAQAKLDEL 329
Cdd:smart00935    7 QKILQ-ESPAGKAaQKQLE----KEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQKL 81

                            90
                    ....*....|....*..
gi 755551840    330 EAALRTAKQDMAQMLRD 346
Cdd:smart00935   82 QQDLQKRQQEELQKILD 98
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 113-368 3.12e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  113 FETCLARLRQQLEELQRERRALDSELktyqDQEDEYKSKYDQeAYKhasvqndfvVLKKDVDEV-----FQSKMDLegnL 187
Cdd:COG3096   439 AEDYLAAFRAKEQQATEEVLELEQKL----SVADAARRQFEK-AYE---------LVCKIAGEVersqaWQTAREL---L 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  188 ESLKEHVCFLTRLyeeelGQLKTQADDMSVVLSMDNN--RCL-DFSDIIAEVRARYEEITRTsKAEAEAvfqtKYQELQE 264
Cdd:COG3096   502 RRYRSQQALAQRL-----QQLRAQLAELEQRLRQQQNaeRLLeEFCQRIGQQLDAAEELEEL-LAELEA----QLEELEE 571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  265 SAqlqgnsmKEAQVQISQLRQAIHRLQSQIGSLRKQND---SLQSAIAD-AEQQGEmAVRDAQAKLDELEAALRTAKQdm 340
Cdd:COG3096   572 QA-------AEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERlREQSGE-ALADSQEVTAAMQQLLERERE-- 641

                         250       260
                  ....*....|....*....|....*...
gi 755551840  341 AQMLRDyqELMGTKLSLDVEIamyRRLL 368
Cdd:COG3096   642 ATVERD--ELAARKQALESQI---ERLS 664
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 240-362 3.72e-04

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 44.08  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   240 YEEITRTSKAEAEavfqtkyQELQESAQL---------QGNSMKEAQVQ---------ISQLRQAIHRLQSQ-------I 294
Cdd:pfam03148  202 WEKFTQDNIERAE-------KERAASAQLrelidsileQTANDLRAQADavnfalrkrIEETEDAKNKLEWQlkktlqeI 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   295 GSLRKQNDSLQSAIADAEQQgeMAV-----------------RD-AQAKL-DELEaALRTAKQDMAQMLRD----YQELM 351
Cdd:pfam03148  275 AELEKNIEALEKAIRDKEAP--LKLaqtrlenrtyrpnvelcRDeAQYGLvDEVK-ELEETIEALKQKLAEaeasLQALE 351

                          170
                   ....*....|.
gi 755551840   352 GTKLSLDVEIA 362
Cdd:pfam03148  352 RTRLRLEEDIA 362
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 231-297 3.73e-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: 41.65  E-value: 3.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551840  231 DIIAEVRARYEEITRTSKAEAEAVfqtkYQELQESAQLQGNSMKE-AQVQISQLRQ-AIHRLQSQIGSL 297
Cdd:cd06503    58 EKLAEARAEAQEIIEEARKEAEKI----KEEILAEAKEEAERILEqAKAEIEQEKEkALAELRKEVADL 122
WXG100_ESAT6 TIGR03930
WXG100 family type VII secretion target; Members of this protein family include secretion ...
 255-342 4.00e-04

WXG100 family type VII secretion target; Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.


Pssm-ID: 274862 [Multi-domain]  Cd Length: 90  Bit Score: 40.28  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   255 FQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQ-IGslrkqndslQSAIADAEQQGEM--AVRDAQAKLDELEA 331
Cdd:TIGR03930    2 IKVDPEELRQAAARFGKTAQELQQLLQRLRSEIDALQGTwEG---------AAADAFQAEFQQWdpAAERLINALQEISE 72

                           90
                   ....*....|.
gi 755551840   332 ALRTAKQDMAQ 342
Cdd:TIGR03930   73 ALRQAADKFEQ 83
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
263-362 4.65e-04

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 43.87  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  263 QESAQLQGNSMKEAQVQI-SQLRQA---IHRLQSQIGSLRKQNDSLQSAIADAEQQGE------MAVRDAQAKLDELEAA 332
Cdd:COG1538    57 KAQAEAAEADLRAARLDLaAEVAQAyfdLLAAQEQLALAEENLALAEELLELARARYEaglasrLDVLQAEAQLAQARAQ 136

                          90       100       110
                  ....*....|....*....|....*....|
gi 755551840  333 LRTAKQDMAQMLRDYQELMGTKLSLDVEIA 362
Cdd:COG1538   137 LAQAEAQLAQARNALALLLGLPPPAPLDLP 166
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 44-223 5.00e-04

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 42.81  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    44 NDFLIASLQRlfqvvktqETREIRSLNNQFASFIDKVRFLEQQNKVLETKWELLQQLQGnrspqglecifetclaRLRQQ 123
Cdd:pfam17078   54 NDNLSSMLNR--------KERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASET----------------TLEAE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   124 LEELQRERRALdselktyQDQEDEYKSKYDQEAykhASVQNDFVVLKKDVDEVFQSKM--------DLEGNLESLKEHVC 195
Cdd:pfam17078  110 LERLQIQYDAL-------VDSQNEYKDHYQQEI---NTLQESLEDLKLENEKQLENYQqrissndkDIDTKLDSYNNKFK 179

                          170       180
                   ....*....|....*....|....*...
gi 755551840   196 FLTRLYEEELGQLKTQADDMSVVLSMDN 223
Cdd:pfam17078  180 NLDNIYVNKNNKLLTKLDSLAQLLDLPS 207
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 59-365 5.27e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.27  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    59 KTQETR-EIRSLNNQFASFIDKVRFLEQQNKVLETKW--------ELLQQLQGNRSPQGLEciFETCLARLRQQLEELQR 129
Cdd:TIGR00606  256 EIEHNLsKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTVRE--KERELVDCQRELEKLNK 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   130 ERRALDSELKTYQDQEDEYKSKYDQeaYKHASVQNDFVVLKKDVdevfQSKMD-LEGNLESLKEHVCFLTRLYEEELGQL 208
Cdd:TIGR00606  334 ERRLLNQEKTELLVEQGRLQLQADR--HQEHIRARDSLIQSLAT----RLELDgFERGPFSERQIKNFHTLVIERQEDEA 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   209 KTQADDMSVVLSMDNNRcldfSDIIAEVRARYEEITRTskAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIH 288
Cdd:TIGR00606  408 KTAAQLCADLQSKERLK----QEQADEIRDEKKGLGRT--IELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   289 RLQSQIgSLRKQNDSLQSAIADaeqqgEMAVRDAQAKLDEleaALRTAKQDMAQMLRD----YQELMGTKLSLDVEIAMY 364
Cdd:TIGR00606  482 KAEREL-SKAEKNSLTETLKKE-----VKSLQNEKADLDR---KLRKLDQEMEQLNHHtttrTQMEMLTKDKMDKDEQIR 552


                   .
gi 755551840   365 R 365
Cdd:TIGR00606  553 K 553
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 238-331 5.80e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 40.65  E-value: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   238 ARYEEITR--TSKAEAEAVFQT---KYQELQESAQLQGNSMKEAQVQISQLRQAIHR-------LQSQIGSLRKQNDSLQ 305
Cdd:pfam18595   12 AELERKARelQAKIDALQVVEKdlrSCIKLLEEIEAELAKLEEAKKKLKELRDALEEkeielreLERREERLQRQLENAQ 91

                           90       100
                   ....*....|....*....|....*.
gi 755551840   306 SAIADAEQQGEMAVRDAQAKLDELEA 331
Cdd:pfam18595   92 EKLERLREQAEEKREAAQARLEELRE 117
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
117-367 6.58e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELqRERRALDSELKTyqDQEDEYKSKYDQEAYKHASVQNdfvvLKKDVDEVFQSKMDLEGNLESLKEHVCF 196
Cdd:PRK02224  504 LVEAEDRIERL-EERREDLEELIA--ERRETIEEKRERAEELRERAAE----LEAEAEEKREAAAEAEEEAEEAREEVAE 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  197 LtrlyEEELGQLKTQADDMsvvlsmdnNRCLDFSDIIAEVRARYEEIT--RTSKAEAEAVFQTKYQELQE-----SAQLQ 269
Cdd:PRK02224  577 L----NSKLAELKERIESL--------ERIRTLLAAIADAEDEIERLRekREALAELNDERRERLAEKRErkrelEAEFD 644

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  270 GNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEqqgemavrdaqAKLDELEaALRTAKQDMAQMLRDYQE 349
Cdd:PRK02224  645 EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE-----------NELEELE-ELRERREALENRVEALEA 712

                         250
                  ....*....|....*...
gi 755551840  350 LMGTKLSLDveiAMYRRL 367
Cdd:PRK02224  713 LYDEAEELE---SMYGDL 727
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 272-372 8.17e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 8.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  272 SMKEAQVQISQLrQAIHrlqSQIGSLRKQNDSLQSAIADAEQQ---GEMAVRDAQAKLDELEAALRTAKQDMAQM---LR 345
Cdd:COG1579     1 AMPEDLRALLDL-QELD---SELDRLEHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEEVearIK 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 755551840  346 DYQELMGTKLS------LDVEIAMYRRLLESEE 372
Cdd:COG1579    77 KYEEQLGNVRNnkeyeaLQKEIESLKRRISDLE 109
OEP pfam02321
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ...
 258-352 8.81e-04

Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.


Pssm-ID: 396757 [Multi-domain]  Cd Length: 181  Bit Score: 41.35  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   258 KYQELQESAQLQgNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQ------GEMAVRDAQAKLDELEA 331
Cdd:pfam02321   82 KAQVEAAEAQLE-QARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARyeagliSLLDVLQAEVELLEARL 160

                           90       100
                   ....*....|....*....|.
gi 755551840   332 ALRTAKQDMAQMLRDYQELMG 352
Cdd:pfam02321  161 ELLNAEADLELALAQLEQLLG 181
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 124-271 9.60e-04

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 41.22  E-value: 9.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   124 LEELQRERRALDS---EL----KTYQDQEDEYKSKYDQeaykhasVQNDFvvlkkdVDEVFQSKMdlegnlesLKEHVCF 196
Cdd:pfam15272   10 LDKLDKNNRALHLlnkDVrerdEHYQLQETSYKKKYLQ-------TRNEL------INELKQSKK--------LYDNYYK 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   197 LTRLYeEELGQLKTQADDMS----------VVLSMDNNR-CLDFSDIIAEVRARYEEITRTSKAEAEAvFQTKYQELQES 265
Cdd:pfam15272   69 LYSKY-QQLKKISNESLDLQstitnlesqlVDQAIDKDReIHNLNEKILSLELRNQELETKREIDKMK-YESRIDELERQ 146


                   ....*.
gi 755551840   266 AQLQGN 271
Cdd:pfam15272  147 LKEQEY 152
EAD9 pfam19962
Effector-associated domain 9; Effector-associated domains (EADs) are predicted to function as ...
 79-139 9.85e-04

Effector-associated domain 9; Effector-associated domains (EADs) are predicted to function as adaptor domains mediating protein-protein interactions. The EADs show a characteriztic architectural pattern. One copy is always fused, typically to the N- or C-terminus, of a core component of a biological conflict system; examples include VMAP, iSTAND, or GAP1. Further copies of the same EAD are fused to either effector or signal-transducing domains, or additional EADs. EAD pairs are frequently observed together on the genome in conserved gene neighborhoods, but can also be severed from such neighborhoods and located in distant regions, indicating EAD-EAD protein domain coupling attenuates collinear transcription requirements.


Pssm-ID: 437794 [Multi-domain]  Cd Length: 62  Bit Score: 38.35  E-value: 9.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551840    79 KVRFLEQQNKVLETKWELL-QQLQGNRSPQGLEcifetclaRLRQQLEELQRERRALDSELK 139
Cdd:pfam19962    7 KRKFLEKRLAALEEEYEAVnNQLNYTLDAVDRN--------RLQRQLERLEQEMEKVESELN 60
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 242-350 1.05e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   242 EITRTSKAEAEAVFQTKYQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQgemavRD 321
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKE-----IL 75

                           90       100
                   ....*....|....*....|....*....
gi 755551840   322 AQAKLDELEAALRTAKQDMAQMLRDYQEL 350
Cdd:pfam12795   76 ASLSLEELEQRLLQTSAQLQELQNQLAQL 104
PRK01294 PRK01294
lipase secretion chaperone;
196-348 1.10e-03

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 42.36  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  196 FLTRLYEEELGQLKTQaddmsvvlsmdnnrcldfsdIIAEVRARYEEITRtskAEAEAVFQTKYQELQESAQLQGNSMKE 275
Cdd:PRK01294   95 FLSALGELDLAAIDAL--------------------VEREIAAQLPEPAD---SQALDLWLRYKAYLSALAQLEDDGPGK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  276 AQVQ-ISQLRQAIHRLQSQIGSL-----------RKQNDSL-------QSAIADAEQQGEMAVRDAQAKLDELEAALRTA 336
Cdd:PRK01294  152 LDLQaLQQLLDARLALRARFFSDweiqaffgeenQYQRYALerlriaqDPSLSDAQKAARLAALEAQLPEDLRAALQESQ 231

                         170
                  ....*....|...
gi 755551840  337 KQ-DMAQMLRDYQ 348
Cdd:PRK01294  232 RQqALLQQLAQLQ 244
PRK01156 PRK01156
chromosome segregation protein; Provisional
 117-370 1.23e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKS----KYDQEAYKHASVQNDfvvLKKDVDEVFQSKmDLEGNLESLKE 192
Cdd:PRK01156  478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKN 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  193 hvcfltRLYEEELGQLKTQADD----MSVVLSMDnnrcldfsdiIAEVRARYEEIT--------RTSKAEAEAVFQTKY- 259
Cdd:PRK01156  554 ------RYKSLKLEDLDSKRTSwlnaLAVISLID----------IETNRSRSNEIKkqlndlesRLQEIEIGFPDDKSYi 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  260 ----QELQESAQLQGNSMKEAQ---VQISQLRQAIHRLQSQIGSLRKQNDSLQ------SAIADAEQQGEMAVRDAQAKL 326
Cdd:PRK01156  618 dksiREIENEANNLNNKYNEIQenkILIEKLRGKIDNYKKQIAEIDSIIPDLKeitsriNDIEDNLKKSRKALDDAKANR 697

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 755551840  327 DELEAALRTAKQD---MAQMLRDYQELMGTKLSLDVEIAMYRRLLES 370
Cdd:PRK01156  698 ARLESTIEILRTRineLSDRINDINETLESMKKIKKAIGDLKRLREA 744
PRK06937 PRK06937
HrpE/YscL family type III secretion apparatus protein;
226-371 1.43e-03

HrpE/YscL family type III secretion apparatus protein;


Pssm-ID: 180763 [Multi-domain]  Cd Length: 204  Bit Score: 41.19  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  226 CLDFSDIIAEVRARYEEItrtsKAEAEAVFQTK----YQE-LQESAQLQGNSMKEAQVQISQLRQAIHRLQSQI--GSLR 298
Cdd:PRK06937   29 LLSAEELVEAARQRAEEI----EAEAQEVYEQQkqlgYQAgLDEARTEQAELILETVLQCQEFYRGVEQQMSEVvlEAVR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  299 KQNDSL----------QSAIADAEQQGEMAVRDAQAKldelEAALRtakQDMAQMLRDYQELMGTKLSLDVEIAMYRRLL 368
Cdd:PRK06937  105 KILNDYddvertlqvvREALALVSNQKQVVVRVNPDQ----AAAVR---EQIAKVLKDFPEVGYLEVVADARLDQGGCIL 177


                  ...
gi 755551840  369 ESE 371
Cdd:PRK06937  178 ETE 180
mukB PRK04863
chromosome partition protein MukB;
118-350 1.63e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  118 ARlRQQLEELQRERralDSELKTYqDQEDEYKSKYdQEAYKHASvqnDFVVLKKDVdeVFQSkmDLEGNLESLK----EH 193
Cdd:PRK04863  783 AR-EKRIEQLRAER---EELAERY-ATLSFDVQKL-QRLHQAFS---RFIGSHLAV--AFEA--DPEAELRQLNrrrvEL 849

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  194 VCFLTRLYEEELgQLKTQADDMSVVLSMdNNRCLDFSDIIA------EVRARYEEITRTSKAEAeavFQTKYQELQESAQ 267
Cdd:PRK04863  850 ERALADHESQEQ-QQRSQLEQAKEGLSA-LNRLLPRLNLLAdetladRVEEIREQLDEAEEAKR---FVQQHGNALAQLE 924

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  268 LQGNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIAD------AEQQGEMA------------VRDAQAKLDEL 329
Cdd:PRK04863  925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRrahfsyEDAAEMLAknsdlneklrqrLEQAEQERTRA 1004

                         250       260
                  ....*....|....*....|.
gi 755551840  330 EAALRTAKQDMAQMLRDYQEL 350
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASL 1025
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 627-734 1.94e-03

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 41.76  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  627 RGSGGQVTVPGR-EYGGQVTVPRGECGGQVTVPGREYGGQVTMPRGECGGQVTMPGREYGGQVTMPGRESGGQVTVPGRE 705
Cdd:PTZ00473  308 RNMGHDSRGPYNaNYGGQFNSRSGRTGSSESIRGFTYDSSTTYGGSSYGTSQTDSTSTYGSRSTFDSSTGGGSQSGGGST 387

                          90       100
                  ....*....|....*....|....*....
gi 755551840  706 YGGQVTMPRGECGGQVTVPGREYGGQVTM 734
Cdd:PTZ00473  388 YGGSSTFDGSSRGSSDSFGVSYFGPQQTV 416
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 228-326 2.00e-03

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: 39.77  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  228 DFSDIIAEVRARYEEITRTSKAEAEAVfqtkYQELQESAQLQGNSMKE-AQVQISQLR-QAIHRLQSQIGSLrkqndslq 305
Cdd:COG0711    56 EYEEKLAEARAEAAEIIAEARKEAEAI----AEEAKAEAEAEAERIIAqAEAEIEQERaKALAELRAEVADL-------- 123

                          90       100
                  ....*....|....*....|..
gi 755551840  306 sAIADAEQQ-GEMAVRDAQAKL 326
Cdd:COG0711   124 -AVAIAEKIlGKELDAAAQAAL 144
LXG pfam04740
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ...
 229-352 2.05e-03

LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of polymorphic toxin proteins in bacteria. It is predicted to use Type VII secretion pathway to mediate export of bacterial toxins.


Pssm-ID: 428100 [Multi-domain]  Cd Length: 202  Bit Score: 40.69  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   229 FSDIIAEVRARYEEItrtsKAEAEAvfqtkyQELQESA---------QLQgNSMKEAQVQISQLRQAIHRLQ---SQIGS 296
Cdd:pfam04740   66 LQDFIDEYIEFLEQI----KAALES------FEPSSNAfidesflehELE-NGLKKAKEKTEELTDEINSILasvSDIVS 134

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755551840   297 LRKQNDS-LQSAIADAEQQgemaVRDAQAKLDELEA----ALRTAKQDMAQMLRDYQELMG 352
Cdd:pfam04740  135 LPKLSDSeVQDSLQKAKKK----VKDTIEKLYDFDQeqtsELSELEADLQALKTYVSELEE 191
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 230-340 2.23e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 40.31  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  230 SDIIAEVRARYEEITRTSKAEAEAVFQTKYQELQESAQlqgNSMKEAQVQISQLRQAI---HRLQSQIGSLRKQNDSLQS 306
Cdd:COG1390     9 EEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKE---EILEKAEREAEREKRRIissAELEARKELLEAKEELIEE 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 755551840  307 AIADAEQQGEmAVRDAQAKLDELEAALRTAKQDM 340
Cdd:COG1390    86 VFEEALEKLK-NLPKDPEYKELLKKLLKEAAEEL 118
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 182-375 2.29e-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: 41.98  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   182 DLEGNLESLKEhvcfltrlyeeELGQLKTQADDMSVVLSmdnnrclDFSDIIAEVRARYEEITR---TSKAEAEAVfQTK 258
Cdd:TIGR02169  685 GLKRELSSLQS-----------ELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQeeeKLKERLEEL-EED 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   259 YQELQESAQLQGNSMKEAQVQISQLRQAIHRLQSQIGSL-RKQNDSLQSAIADAEQQGEMAVRDAQAKLDELEAALRTAK 337
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 755551840   338 QDMAQMLRDYQELMGTKLSLDVEIAMYRRLLESEECRI 375
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 53-264 2.81e-03

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


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 2.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840     53 RLFQVVKTQETREIRSLNNQFASFIDKVRfleqqnkvLETK--W-ELLQQLQgnrspQGLECIFETCLARLRQQLEELQR 129
Cdd:smart00787   99 PLFKEYFSASPDVKLLMDKQFQLVKTFAR--------LEAKkmWyEWRMKLL-----EGLKEGLDENLEGLKEDYKLLMK 165

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    130 ERRALDSELKTYQDQEDEYKSKYDQEAyKHASVQNDfvvlkKDVDEVFQSKMDLEgnlESLKEHVCFLTrlyeeELGQLK 209
Cdd:smart00787  166 ELELLNSIKPKLRDRKDALEEELRQLK-QLEDELED-----CDPTELDRAKEKLK---KLLQEIMIKVK-----KLEELE 231

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 755551840    210 TQADDMSVVLSMDNNRCLDFSDIIAEVRARYEEITRTSKAEAEAVfQTKYQELQE 264
Cdd:smart00787  232 EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKL-KEQLKLLQS 285
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
201-343 3.14e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.16  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  201 YEEELGQLKTQADDMsvvlsMDNnrcldFSDIIAEVRARYEEITRTSkaeaeavfqtkyQELQESAQLQGNSMKEAQVQI 280
Cdd:COG0840   233 SKDEIGQLADAFNRM-----IEN-----LRELVGQVRESAEQVASAS------------EELAASAEELAAGAEEQAASL 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551840  281 SQLRQAIHRLQSQIGSLRKQ----NDSLQSAIADAeQQGEMAVRDAQAKLDELEAALRTAKQDMAQM 343
Cdd:COG0840   291 EETAAAMEELSATVQEVAENaqqaAELAEEASELA-EEGGEVVEEAVEGIEEIRESVEETAETIEEL 356
COG5022 COG5022
Myosin heavy chain [General function prediction only];
42-302 3.27e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   42 AKNDFLIASLQRLFQVVKTQetREIrslnNQFASFIDKVRFLEQQNKVL-----ETKWELLQQLQ------GNRSPQG-- 108
Cdd:COG5022   742 AKLDNIATRIQRAIRGRYLR--RRY----LQALKRIKKIQVIQHGFRLRrlvdyELKWRLFIKLQpllsllGSRKEYRsy 815

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  109 LECIFE-TCLARLRQQLEELQRERRALDSEL------KTYQDQED----EYKSKYDQEAYKHASVQNDFVVLKKDVDEVF 177
Cdd:COG5022   816 LACIIKlQKTIKREKKLRETEEVEFSLKAEVliqkfgRSLKAKKRfsllKKETIYLQSAQRVELAERQLQELKIDVKSIS 895

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  178 QSKM------------------DLEGNLESLKEHVCFLTRLYEEelGQLKTQADDMSVVLSMDNN----------RCLDF 229
Cdd:COG5022   896 SLKLvnleleseiielkkslssDLIENLEFKTELIARLKKLLNN--IDLEEGPSIEYVKLPELNKlhevesklkeTSEEY 973

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  230 SDI-------IAEVRARYEEITRTSKAEAEavFQTKYQELQESAQlqgnSMKEAQVQISQLRQAIHRLQSQIGSLRKQND 302
Cdd:COG5022   974 EDLlkkstilVREGNKANSELKNFKKELAE--LSKQYGALQESTK----QLKELPVEVAELQSASKIISSESTELSILKP 1047
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 202-350 3.98e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  202 EEELGQLKTQADDMSV---VLSMDNNRC----LDFSDIIAEVRARYEEitrTSKAEAEAVFQTKYQELQ-ESAQLQGNsM 273
Cdd:COG3096   784 EKRLEELRAERDELAEqyaKASFDVQKLqrlhQAFSQFVGGHLAVAFA---PDPEAELAALRQRRSELErELAQHRAQ-E 859

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  274 KEAQVQISQLRQAI---HRLQSQIG------------SLRKQNDSLQSAIADAEQQGEmavrdAQAKLDELEAALRTAKQ 338
Cdd:COG3096   860 QQLRQQLDQLKEQLqllNKLLPQANlladetladrleELREELDAAQEAQAFIQQHGK-----ALAQLEPLVAVLQSDPE 934

                         170
                  ....*....|..
gi 755551840  339 DMAQMLRDYQEL 350
Cdd:COG3096   935 QFEQLQADYLQA 946
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
117-356 4.68e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  117 LARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQeaYKHAsvqndfvvlkkdVDEVfqSKMDL-EGNLESL-KEHv 194
Cdd:COG0497   153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDL--LRFQ------------LEEL--EAAALqPGEEEELeEER- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  195 cflTRLyeEELGQLKTQADDMSVVLSMDNNRCLdfsDIIAEVRARYEEITRtskaeaeavFQTKYQELQE---SAQLQgn 271
Cdd:COG0497   216 ---RRL--SNAEKLREALQEALEALSGGEGGAL---DLLGQALRALERLAE---------YDPSLAELAErleSALIE-- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  272 sMKEAQVQISQLRQAI----HRLQ------SQIGSL-RKQNDSLQSAIADAEQqgemavrdAQAKLDELEAA---LRTAK 337
Cdd:COG0497   277 -LEEAASELRRYLDSLefdpERLEeveerlALLRRLaRKYGVTVEELLAYAEE--------LRAELAELENSderLEELE 347

                         250
                  ....*....|....*....
gi 755551840  338 QDMAQMLRDYQELmGTKLS 356
Cdd:COG0497   348 AELAEAEAELLEA-AEKLS 365
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 76-203 4.87e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840    76 FIDKVRFLEQQNKVLETKWELLQQLqgnrspqglECIFETCLARLRQQLEELQRERRALDSELKTYQDQEDEYKSKYDQE 155
Cdd:pfam13863    1 LLEKKREMFLVQLALDAKREEIERL---------EELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 755551840   156 AYKHASVQNDFVVLKKDVDEVFQSKMDLEGNLESLKEHVCFLTRLYEE 203
Cdd:pfam13863   72 TKLKKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLEKVVPK 119
PTZ00491 PTZ00491
major vault protein; Provisional
 242-371 5.84e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.77  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  242 EITrTSKAEAEAVFQTKYQELQESAQLQGNSMKEaQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADA-----EQQGE 316
Cdd:PTZ00491  658 EIT-TKSQEAAARHQAELLEQEARGRLERQKMHD-KAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAearliEAEAE 735

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  317 MAVRDAQAKLDELEAALRTAKQDMAQMLrdyqELMGTKLSLDVEIAMYRRLLESE 371
Cdd:PTZ00491  736 VEQAELRAKALRIEAEAELEKLRKRQEL----ELEYEQAQNELEIAKAKELADIE 786
WXG100 pfam06013
Proteins of 100 residues with WXG; ESAT-6 is a small protein appears to be of fundamental ...
 255-342 5.86e-03

Proteins of 100 residues with WXG; ESAT-6 is a small protein appears to be of fundamental importance in virulence and protective immunity in Mycobacterium tuberculosis. homologs have been detected in other Gram-positive bacterial species. It may represent a novel secretion system potentially driven by the pfam01580 domains in the YukA-like proteins.


Pssm-ID: 428722  Cd Length: 85  Bit Score: 36.86  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   255 FQTKYQELQESAqlqgnsmKEAQVQISQLRQAIHRLQSQIGSLRkqnDSLQSAIADA--EQQGEM--AVRDAQAKLDELE 330
Cdd:pfam06013    2 IKVDPEELRQAA-------ARFQKSAEEIEDELQRLKSTVAALG---GGWSGAAADAfqAEFDEWkpAAQKLVDALEEIS 71

                           90
                   ....*....|..
gi 755551840   331 AALRTAKQDMAQ 342
Cdd:pfam06013   72 EALKQAANAYED 83
PRK11281 PRK11281
mechanosensitive channel MscK;
160-369 6.07e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  160 ASVQNDFVVLKKDVDEVFQSKM---DLEGNLESLKEhvcflTRLYEEELGQLKTQADDMSvvlsmdnnrcldfsdiiAEV 236
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLvqqDLEQTLALLDK-----IDRQKEETEQLKQQLAQAP-----------------AKL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  237 RARYEEITRTSKAEAEAVFQTkYQELqESAQLQgNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQge 316
Cdd:PRK11281   97 RQAQAELEALKDDNDEETRET-LSTL-SLRQLE-SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQR-- 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755551840  317 mavrdaqakLDELEAALRTAKQDMAQMLRDYQELMGTKLS-LDVEIAMYRRLLE 369
Cdd:PRK11281  172 ---------LQQIRNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLE 216
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 48-129 6.20e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.17  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840   48 IASLQRLFQVvKTQETREIRSlnnqfaSFIDK----VRFLEQ-QNKVLE---TKWELLQQLQGNRSPQG--LECIFETC- 116
Cdd:cd16855    70 KEQLEQLLNA-KAQELLQLRM------ELADKfkktIQLLSKlQSRVLDeelIQWKRQQQLAGNGAPFEsnLDTIQEWCe 142

                          90
                  ....*....|....*...
gi 755551840  117 -LARL----RQQLEELQR 129
Cdd:cd16855   143 sLAEIiwqnRQQIKRAER 160
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 279-338 6.44e-03

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 37.91  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  279 QISQLRQAIHRLQSQIGSLRKQNDSLQSA----------------------IADAEQQGEMAVRDAQAKLDELEAALRTA 336
Cdd:COG3599    42 ENKELKEKLEELEEELEEYRELEETLQKTlvvaqetaeevkenaekeaeliIKEAELEAEKIIEEAQEKARKIVREIEEL 121


                  ..
gi 755551840  337 KQ 338
Cdd:COG3599   122 KR 123
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
233-351 6.49e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  233 IAEVRARYEEITRTSKAEAEAvfqtKYQELQESAQLQGNSM-----KEAQVQISQLRqAIHRLQSQIGSLRKQNDS-LQS 306
Cdd:COG2268   246 LAKKKAEERREAETARAEAEA----AYEIAEANAEREVQRQleiaeREREIELQEKE-AEREEAELEADVRKPAEAeKQA 320

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755551840  307 AIADAEQQGEMAVRDAQAK---LDELEAALRTAKQD-----MAQMLRDYQELM 351
Cdd:COG2268   321 AEAEAEAEAEAIRAKGLAEaegKRALAEAWNKLGDAaillmLIEKLPEIAEAA 373
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
271-378 7.19e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  271 NSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIAD--------AEQQGEMA--VRDAQAKLDELEAALRTAKQDM 340
Cdd:COG1340    15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKElreeaqelREKRDELNekVKELKEERDELNEKLNELREEL 94

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755551840  341 AQMLRDYQELMGTKLSLDvEIamyRRLLESEECRISTE 378
Cdd:COG1340    95 DELRKELAELNKAGGSID-KL---RKEIERLEWRQQTE 128
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 273-345 7.45e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 37.18  E-value: 7.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551840   273 MKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEmavrdaqaKLDELEAALRTAKQDMAQMLR 345
Cdd:pfam02403   38 RRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELKD--------ELKALEAELKELEAELDKLLL 102
EsxA COG4842
Secreted virulence factor YukE/EsxA, WXG100 family [Defense mechanisms];
255-352 9.20e-03

Secreted virulence factor YukE/EsxA, WXG100 family [Defense mechanisms];


Pssm-ID: 443870  Cd Length: 93  Bit Score: 36.51  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  255 FQTKYQELQESAQlqgnsmkeaqvqisQLRQAIHRLQSQIGSLRKQNDSLQS----AIADA--EQQGEM--AVRDAQAKL 326
Cdd:COG4842     1 IRVDPEALRAAAG--------------RFGAAAGELQALLDDLRSQLAALQSswegDAATAfqAAQAQWdqAATKLNQAL 66

                          90       100
                  ....*....|....*....|....*.
gi 755551840  327 DELEAALRTAKQDMAQMLRDYQELMG 352
Cdd:COG4842    67 EDIAQALRQAADAYEEAEQANAALFG 92
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 171-351 9.35e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  171 KDVDEVFQSKmdLEGNLESLKEHvcFLTRLYEEELGQLKTQADDMSVVLsMDNNRCLDFS---------DIIAEVRARYE 241
Cdd:cd16269    85 KDEDQKFQKK--LMEQLEEKKEE--FCKQNEEASSKRCQALLQELSAPL-EEKISQGSYSvpggyqlylEDREKLVEKYR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551840  242 EITRtSKAEAEAVFQTKYQELQESAQ--LQ-GNSMKEAQVQISQLRQAIHRLQSQIGSLRKQNDSLQSAIADAEQQGEMA 318
Cdd:cd16269   160 QVPR-KGVKAEEVLQEFLQSKEAEAEaiLQaDQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEH 238

                         170       180       190
                  ....*....|....*....|....*....|....
gi 755551840  319 VRDAQAKLD-ELEAALRTAKQDMAQMLRDYQELM 351
Cdd:cd16269   239 LRQLKEKMEeERENLLKEQERALESKLKEQEALL 272
mukB PRK04863
chromosome partition protein MukB;
119-166 9.73e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 9.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755551840  119 RLRQQLEELQRERRALDSELKTYQDQEDEY-------KSKYDQEAYKHASVQNDF 166
Cdd:PRK04863  989 KLRQRLEQAEQERTRAREQLRQAQAQLAQYnqvlaslKSSYDAKRQMLQELKQEL 1043
 
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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