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Conserved domains on  [gi|42566188|ref|NP_567176|]
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XH/XS domain-containing protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 503-633 9.93e-70

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


:

Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 222.08  E-value: 9.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   503 KRMGELDEKPFLDVCKLRYSANEARVEAATLCSTWKENLKNPSWQPFKREGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 582
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42566188   583 AVKAALVEMNEYNASGRYPTSELWNFKEGRKATLKEVITFISTDIKNLKRK 633
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 119-223 6.11e-38

RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important.


:

Pssm-ID: 409710  Cd Length: 107  Bit Score: 135.95  E-value: 6.11e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 119 YVWPWMGIVVNPLKETDD--KELLLDSVYWLQTLSKFKPVEVNAFWVEQDSIVGVIAKFDSDWSGFAAATELEKEFETQG 196
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDnrKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEVDG 80

                        90       100
                ....*....|....*....|....*..
gi 42566188 197 SCKKEWTERSGDSESKAYGWCARADDF 223
Cdd:cd12266  81 HGKKDWRNKKGGRKSKLYGWLARADDY 107
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 42-84 1.25e-19

XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in proteins that also contain an XS domain.


:

Pssm-ID: 251981  Cd Length: 43  Bit Score: 82.18  E-value: 1.25e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42566188    42 CPFCVGKKKQDYKYKELHAHATGVSKGSATRSALQKSNHLALA 84
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-486 1.86e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    251 QDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMS--LRHIQRILYDKEKLRNEL 328
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    329 DRKMRDLESRAKQLEKHEALTELER----QKLDEDKRKSDAMNKSLQlasrEQKKADESVLRLVEEHQRQKEDALNKILL 404
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLeeleSKLDELAEELAELEEKLE----ELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    405 LEKQLDTKQT----LEMEIQELKGKLQVMK---------------HLGDDDDEAVQTKMKEMNDELDDKKAELEDLESMN 465
Cdd:TIGR02168  377 LEEQLETLRSkvaqLELQIASLNNEIERLEarlerledrrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          250       260
                   ....*....|....*....|.
gi 42566188    466 SVLMTKERQSNDEIQAARQKM 486
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQAL 477
 
Name Accession Description Interval E-value
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 503-633 9.93e-70

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 222.08  E-value: 9.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   503 KRMGELDEKPFLDVCKLRYSANEARVEAATLCSTWKENLKNPSWQPFKREGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 582
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42566188   583 AVKAALVEMNEYNASGRYPTSELWNFKEGRKATLKEVITFISTDIKNLKRK 633
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 119-223 6.11e-38

RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important.


Pssm-ID: 409710  Cd Length: 107  Bit Score: 135.95  E-value: 6.11e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 119 YVWPWMGIVVNPLKETDD--KELLLDSVYWLQTLSKFKPVEVNAFWVEQDSIVGVIAKFDSDWSGFAAATELEKEFETQG 196
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDnrKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEVDG 80

                        90       100
                ....*....|....*....|....*..
gi 42566188 197 SCKKEWTERSGDSESKAYGWCARADDF 223
Cdd:cd12266  81 HGKKDWRNKKGGRKSKLYGWLARADDY 107
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 118-225 4.31e-37

XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins including gene X and SGS3. SGS3 is thought to be involved in post-transcriptional gene silencing (PTGS). This domain contains a conserved aspartate residue that may be functionally important. The XS domain has recently been predicted to possess an RRM-like RNA-binding domain by fold recognition.


Pssm-ID: 460933  Cd Length: 113  Bit Score: 133.84  E-value: 4.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   118 VYVWPWMGIVVNPLKETD-DKELLLDSVYWLQT-LSKFKPVEVNAFWVEQDSIVGVIAKFDSDWSGFAAATELEKEFETQ 195
Cdd:pfam03468   3 LFVWPWMGIVVNIPTEQDeDGRWVGMSGEELKDkLSRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKHFEAQ 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 42566188   196 GSCKKEWTE-RSGDSESKAYGWCARADDFQS 225
Cdd:pfam03468  83 GHGKKDWGGkRNRGSGSKLYGWVARADDYNS 113
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 42-84 1.25e-19

XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in proteins that also contain an XS domain.


Pssm-ID: 251981  Cd Length: 43  Bit Score: 82.18  E-value: 1.25e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42566188    42 CPFCVGKKKQDYKYKELHAHATGVSKGSATRSALQKSNHLALA 84
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-486 1.86e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    251 QDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMS--LRHIQRILYDKEKLRNEL 328
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    329 DRKMRDLESRAKQLEKHEALTELER----QKLDEDKRKSDAMNKSLQlasrEQKKADESVLRLVEEHQRQKEDALNKILL 404
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLeeleSKLDELAEELAELEEKLE----ELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    405 LEKQLDTKQT----LEMEIQELKGKLQVMK---------------HLGDDDDEAVQTKMKEMNDELDDKKAELEDLESMN 465
Cdd:TIGR02168  377 LEEQLETLRSkvaqLELQIASLNNEIERLEarlerledrrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          250       260
                   ....*....|....*....|.
gi 42566188    466 SVLMTKERQSNDEIQAARQKM 486
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQAL 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-484 2.07e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 296 HQAFAEETKKMQ-QMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLAS 374
Cdd:COG1196 215 YRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 375 REQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDEAVQTKMKEMNDELDDK 454
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190
                ....*....|....*....|....*....|
gi 42566188 455 KAELEDLESMNSVLMTKERQSNDEIQAARQ 484
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
PTZ00121 PTZ00121
MAEBL; Provisional
 290-487 1.89e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   290 DEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEAL---TELERQKLDEDKRKSDAM 366
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkkVEQLKKKEAEEKKKAEEL 1652

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   367 NKSLQL-----------ASREQKKADEsvLRLVEEHQRQKEDALNKilLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDD 435
Cdd:PTZ00121 1653 KKAEEEnkikaaeeakkAEEDKKKAEE--AKKAEEDEKKAAEALKK--EAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42566188   436 DDEAVQTKMKEmndELDDKKAE--LEDLESMNSV--LMTKERQSNDEIQAARQKMI 487
Cdd:PTZ00121 1729 KIKAEEAKKEA---EEDKKKAEeaKKDEEEKKKIahLKKEEEKKAEEIRKEKEAVI 1781
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 301-486 1.48e-05

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: 48.19  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    301 EETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELE----RQKLDEDKRKSDAMNKSLQ-LASR 375
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSElteaRTERDQFSQESGNLDDQLQkLLAD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    376 EQKKADESVLRLVEEHQRQKEDALNKILL--LEKQLDTKQtleMEIQELKGKLQVMKhlgddddEAVQTKMKEMNDELDD 453
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLWDRDTGNSITIdhLRRELDDRN---MEVQRLEALLKAMK-------SECQGQMERQMAAIQG 455

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 42566188    454 KKAELEDLESMNSVL-MTKE--RQSNDEIQAARQKM 486
Cdd:pfam15921  456 KNESLEKVSSLTAQLeSTKEmlRKVVEELTAKKMTL 491
 
Name Accession Description Interval E-value
XH pfam03469
XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins ...
 503-633 9.93e-70

XH domain; The XH (rice gene X Homology) domain is found in a family of plant proteins including gene X. The molecular function of these proteins is unknown. However these proteins usually contain an XS domain that is also found in the PTGS protein SGS3. This domain contains a conserved glutamate residue that may be functionally important.


Pssm-ID: 460934 [Multi-domain]  Cd Length: 131  Bit Score: 222.08  E-value: 9.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   503 KRMGELDEKPFLDVCKLRYSANEARVEAATLCSTWKENLKNPSWQPFKREGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 582
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 42566188   583 AVKAALVEMNEYNASGRYPTSELWNFKEGRKATLKEVITFISTDIKNLKRK 633
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 119-223 6.11e-38

RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X and SGS3) domain is a single-stranded RNA-binding domain (RBD) and possesses a unique version of a RNA recognition motif (RRM) fold. It is conserved in a family of plant proteins including gene X and SGS3. Although its function is still unknown, the plant SGS3 proteins are thought to be involved in post-transcriptional gene silencing (PTGS) pathways. In addition, they contain a conserved aspartate residue that may be functionally important.


Pssm-ID: 409710  Cd Length: 107  Bit Score: 135.95  E-value: 6.11e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 119 YVWPWMGIVVNPLKETDD--KELLLDSVYWLQTLSKFKPVEVNAFWVEQDSIVGVIAKFDSDWSGFAAATELEKEFETQG 196
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDnrKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEVDG 80

                        90       100
                ....*....|....*....|....*..
gi 42566188 197 SCKKEWTERSGDSESKAYGWCARADDF 223
Cdd:cd12266  81 HGKKDWRNKKGGRKSKLYGWLARADDY 107
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 118-225 4.31e-37

XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins including gene X and SGS3. SGS3 is thought to be involved in post-transcriptional gene silencing (PTGS). This domain contains a conserved aspartate residue that may be functionally important. The XS domain has recently been predicted to possess an RRM-like RNA-binding domain by fold recognition.


Pssm-ID: 460933  Cd Length: 113  Bit Score: 133.84  E-value: 4.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   118 VYVWPWMGIVVNPLKETD-DKELLLDSVYWLQT-LSKFKPVEVNAFWVEQDSIVGVIAKFDSDWSGFAAATELEKEFETQ 195
Cdd:pfam03468   3 LFVWPWMGIVVNIPTEQDeDGRWVGMSGEELKDkLSRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKHFEAQ 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 42566188   196 GSCKKEWTE-RSGDSESKAYGWCARADDFQS 225
Cdd:pfam03468  83 GHGKKDWGGkRNRGSGSKLYGWVARADDYNS 113
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 42-84 1.25e-19

XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in proteins that also contain an XS domain.


Pssm-ID: 251981  Cd Length: 43  Bit Score: 82.18  E-value: 1.25e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42566188    42 CPFCVGKKKQDYKYKELHAHATGVSKGSATRSALQKSNHLALA 84
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-486 1.86e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    251 QDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMS--LRHIQRILYDKEKLRNEL 328
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEeeIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    329 DRKMRDLESRAKQLEKHEALTELER----QKLDEDKRKSDAMNKSLQlasrEQKKADESVLRLVEEHQRQKEDALNKILL 404
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLeeleSKLDELAEELAELEEKLE----ELKEELESLEAELEELEAELEELESRLEE 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    405 LEKQLDTKQT----LEMEIQELKGKLQVMK---------------HLGDDDDEAVQTKMKEMNDELDDKKAELEDLESMN 465
Cdd:TIGR02168  377 LEEQLETLRSkvaqLELQIASLNNEIERLEarlerledrrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456

                          250       260
                   ....*....|....*....|.
gi 42566188    466 SVLMTKERQSNDEIQAARQKM 486
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQAL 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-484 2.07e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 296 HQAFAEETKKMQ-QMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLAS 374
Cdd:COG1196 215 YRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 375 REQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDEAVQTKMKEMNDELDDK 454
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190
                ....*....|....*....|....*....|
gi 42566188 455 KAELEDLESMNSVLMTKERQSNDEIQAARQ 484
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
PTZ00121 PTZ00121
MAEBL; Provisional
 290-487 1.89e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   290 DEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEAL---TELERQKLDEDKRKSDAM 366
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkkVEQLKKKEAEEKKKAEEL 1652

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   367 NKSLQL-----------ASREQKKADEsvLRLVEEHQRQKEDALNKilLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDD 435
Cdd:PTZ00121 1653 KKAEEEnkikaaeeakkAEEDKKKAEE--AKKAEEDEKKAAEALKK--EAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 42566188   436 DDEAVQTKMKEmndELDDKKAE--LEDLESMNSV--LMTKERQSNDEIQAARQKMI 487
Cdd:PTZ00121 1729 KIKAEEAKKEA---EEDKKKAEeaKKDEEEKKKIahLKKEEEKKAEEIRKEKEAVI 1781
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 282-501 5.89e-06

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: 49.68  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    282 AMSLQRVLDEKKNLHQAFAEETKKMQQM--SLRHIQRILYDKEKLRNELDR---KMRDLESRAKQLEKHEALTeleRQKL 356
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAEIeeLEREIEEERKRRDKLTEEYAElkeELEDLRAELEEVDKEFAET---RDEL 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    357 DEDKRKSDAMNKSLQLASREQKKADESVLRL---VEEHQRQKEDALNKILLLEKQLDTKQtleMEIQELKGKL-QVMKHL 432
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLseeLADLNAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLeQLAADL 464

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42566188    433 GDDDDE--AVQTKMKEMNDELDDKKAELEDLESMNSVLMTKERQSndeiQAARQKMIAGLTGLLGAESDIG 501
Cdd:TIGR02169  465 SKYEQElyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG----RAVEEVLKASIQGVHGTVAQLG 531
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 301-486 1.48e-05

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: 48.19  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    301 EETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELE----RQKLDEDKRKSDAMNKSLQ-LASR 375
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSElteaRTERDQFSQESGNLDDQLQkLLAD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    376 EQKKADESVLRLVEEHQRQKEDALNKILL--LEKQLDTKQtleMEIQELKGKLQVMKhlgddddEAVQTKMKEMNDELDD 453
Cdd:pfam15921  386 LHKREKELSLEKEQNKRLWDRDTGNSITIdhLRRELDDRN---MEVQRLEALLKAMK-------SECQGQMERQMAAIQG 455

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 42566188    454 KKAELEDLESMNSVL-MTKE--RQSNDEIQAARQKM 486
Cdd:pfam15921  456 KNESLEKVSSLTAQLeSTKEmlRKVVEELTAKKMTL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 311-596 2.61e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    311 LRHIQRILYDKEKLRNELDRKMRDLESRAKQ----LEKHEALTELE-----------RQKLDEDKRKSDAMNKSLQLASR 375
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKaeryKELKAELRELElallvlrleelREELEELQEELKEAEEELEELTA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    376 EQKKADESVLRLVEEHQ--RQKEDALNKILLLEKQLdtKQTLEMEIQELKGKLQVMkhlgDDDDEAVQTKMKEMNDELDD 453
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSelEEEIEELQKELYALANE--ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDE 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    454 KKAELEDLESMNSVLMTKERQSNDEIQAARQKMIAGLTGLLGAESDIGVKRMGELDEKPFLDVCKLRYSANEARVEAAT- 532
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEd 414

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566188    533 ----LCSTWKENLKNPSWQPFKR-----EGTGDGAEEVV--DEDDEQLKKLKREWGKEVHNAVKAALVEMNEYNA 596
Cdd:TIGR02168  415 rrerLQQEIEELLKKLEEAELKElqaelEELEEELEELQeeLERLEEALEELREELEEAEQALDAAERELAQLQA 489
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 235-494 4.78e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   235 KEGTLRTVSDILQNNVQDRNTLLDVLSNMIDMTNEDLNKAqHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMS---- 310
Cdd:pfam10174 357 KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI-NVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSsntd 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   311 --LRHIQRILYDKEK----LRNELDR----KMRDLESRAKQL-EKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKK 379
Cdd:pfam10174 436 taLTTLEEALSEKERiierLKEQRERedreRLEELESLKKENkDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   380 adESVLRLVEEHQRQKEDALNKillLEKQLDTKQTLEMEIQ---ELKGKLQVM-KHLGDDDDEAVQTK---------MKE 446
Cdd:pfam10174 516 --DSKLKSLEIAVEQKKEECSK---LENQLKKAHNAEEAVRtnpEINDRIRLLeQEVARYKEESGKAQaeverllgiLRE 590

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 42566188   447 MNDELDDKKAELEDLESMNSVLMTKERQSNDEIQAARQKMIAGLTGLL 494
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 285-464 6.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 285 LQRVLDEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSD 364
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 365 AMNKSLQLASREQKKAD--ESVLRLVEEHQRQKEDALNKILLLEKQLDTK-QTLEMEIQELKGKLQVmkhLGD------D 435
Cdd:COG1196 712 AEEERLEEELEEEALEEqlEAEREELLEELLEEEELLEEEALEELPEPPDlEELERELERLEREIEA---LGPvnllaiE 788

                       170       180
                ....*....|....*....|....*....
gi 42566188 436 DDEAVQTKMKEMNDELDDKKAELEDLESM 464
Cdd:COG1196 789 EYEELEERYDFLSEQREDLEEARETLEEA 817
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 300-484 7.44e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   300 AEETKKMQQMSLRHIQRILYDKEKLRNELD----RKMRDLES-RAKQLEKHEaLTELERQKLDEDKRKSDAMNKSLQLA- 373
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVEMEQIRAEQEearqREVRRLEEeRAREMERVR-LEEQERQQQVERLRQQEEERKRKKLEl 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   374 ---SREQKKADESVLRLVEEHQRQKEDAL----NKILLLEKQLDTKQT-LEMEIQELKGKLQVMKHLGDDDDEAVQTKMK 445
Cdd:pfam17380 480 ekeKRDRKRAEEQRRKILEKELEERKQAMieeeRKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMR 559

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 42566188   446 EMNDELDDKKAELEDLESMNSVLMTKERQSndEIQAARQ 484
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKARA--EYEATTP 596
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-564 1.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 244 DILQNNVQDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQmslrhIQRILYDKEK 323
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 324 LRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKKadesvlRLVEEHQRQKEDALNKIL 403
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEE 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 404 LLEKQLDTKQTLEMEIQELKGKLQVMKHLgDDDDEAVQTKMKEMNDELDDKKAELEDLESMNSVLMTKERQSNDEIQAAR 483
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 484 QKMIAGLTGLLGAESDIGVKRMGELDEKPfldvckLRYSANEARVEAATLCSTWKENLKNPSWqpfkREGTGDGAEEVVD 563
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAA------RLLLLLEAEADYEGFLEGVKAALLLAGL----RGLAGAVAVLIGV 532


                .
gi 42566188 564 E 564
Cdd:COG1196 533 E 533
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-500 1.47e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 301 EET-KKMQQMSlRHIQRIlydkEKLRNELDRKMRDLESRAKQLEKHEAL-TELERQKLDEDKRKSDAMNKSLQLASREQK 378
Cdd:COG1196 175 EEAeRKLEATE-ENLERL----EDILGELERQLEPLERQAEKAERYRELkEELKELEAELLLLKLRELEAELEELEAELE 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 379 KADESVLRLVEEHQR---QKEDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDEAVQTKMKEMNDELDDKK 455
Cdd:COG1196 250 ELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42566188 456 AELEDLESMNSVLMTKERQSNDEIQAARQKMIAGLTGLLGAESDI 500
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
293-432 2.18e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 2.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 293 KNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHeaLTELERqKLDEDKRKSDAMNKSLQL 372
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE--VEELEA-ELEEKDERIERLERELSE 452

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 373 ASREQKkadESVLRLVEEHQRQKEdalnkILLLEKQLDTkqtLEMEIQELKGKLQVMKHL 432
Cdd:COG2433 453 ARSEER---REIRKDREISRLDRE-----IERLERELEE---ERERIEELKRKLERLKEL 501
PTZ00121 PTZ00121
MAEBL; Provisional
 262-475 2.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   262 NMIDMTNEDLNKAQHSYNRTAMSLQRVlDEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQ 341
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   342 LEKHEALTELERQKLDEDKRKSDAMNKslqlASREQKKADESVLRlvEEHQRQKEDALNKILLLEKQldTKQTLEMEIQE 421
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKK----AEEDEKKAAEALKK--EAEEAKKAEELKKKEAEEKK--KAEELKKAEEE 1727

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 42566188   422 LKGKLQVMKHLGDDDDEAVQTKMKEmnDELDDKKAELEDLESMNSVLMTKERQS 475
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 229-462 3.34e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    229 IGEYLSKEGTLRTVSDILQNNVQDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQ 308
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    309 mslrhiqrilydkekLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKKADESvLRLV 388
Cdd:TIGR02168  843 ---------------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE-LREL 906

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566188    389 EEHQRQKEDALNKILLLEKQLDTK-QTLEMEIQELKGKLQVmkhLGDDDDEAVQTKMKEMNDELDDKKAELEDLE 462
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 298-488 3.43e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 298 AFAEETKKMQQMSLRHIQRilyDKEKLRNELDRKMRDLESRAKQLEKhealtelERQKLDEDKRKSDAMNKSLQLASREQ 377
Cdd:COG3883  12 AFADPQIQAKQKELSELQA---ELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKLQAEIAEAEAEI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 378 KKADESVLRLVEEHQRQK---------------EDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKhlgdDDDEAVQT 442
Cdd:COG3883  82 EERREELGERARALYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKK----AELEAKLA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42566188 443 KMKEMNDELDDKKAELEDLESMNSVLMTKERQSNDEIQAARQKMIA 488
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 289-511 3.82e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    289 LDEKKNLHQAFAEETKKMQQMS-LRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMN 367
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    368 KSLQLASREQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDT----KQTLEMEIQELKGKLQVMKHLGDDDDEAVQTK 443
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaqLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566188    444 mKEMNDELDDKKAELEDLESMNSVLmtkerqsnDEIQAARQKMIAGLTGL----LGA--ESDIGVKRMGELDEK 511
Cdd:TIGR02169  930 -EEELSEIEDPKGEDEEIPEEELSL--------EDVQAELQRVEEEIRALepvnMLAiqEYEEVLKRLDELKEK 994
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 246-422 9.40e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 9.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 246 LQNNVQDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMSLR------------- 312
Cdd:COG4942  53 LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfl 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 313 HIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKKadesvlrLVEEHQ 392
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK-------LLARLE 205

                       170       180       190
                ....*....|....*....|....*....|
gi 42566188 393 RQKEDALNKILLLEKQldtKQTLEMEIQEL 422
Cdd:COG4942 206 KELAELAAELAELQQE---AEELEALIARL 232
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 285-486 1.23e-03

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: 41.80  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   285 LQRVLDEKKNLHQAfaeetkkmQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKhealtelERQKLDEDKRKSD 364
Cdd:pfam07888  36 LEECLQERAELLQA--------QEAANRQREKEKERYKRDREQWERQRRELESRVAELKE-------ELRQSREKHEELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   365 AMNKSLQLASREQKKADESVLRLVEEH-QRQKEDALNKILLLEKQLDTKQTLEMEIQELKgKLQVMKHLGDDDDEAVQTK 443
Cdd:pfam07888 101 EKYKELSASSEELSEEKDALLAQRAAHeARIRELEEDIKTLTQRVLERETELERMKERAK-KAGAQRKEEEAERKQLQAK 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 42566188   444 MKEMNDELDDKKAELEDLESMNSVLMTKERQSNDEIQAARQKM 486
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 327-633 1.29e-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: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    327 ELDRK----MRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKKADESVLRLVEEHQRQKEDALNKI 402
Cdd:TIGR02169  167 EFDRKkekaLEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    403 LLLEKQLDTKQT----LEMEIQELKGKL-----QVMKhLGDDDDEAVQTKMKEMNDEL-------DDKKAELEDLEsmns 466
Cdd:TIGR02169  247 ASLEEELEKLTEeiseLEKRLEEIEQLLeelnkKIKD-LGEEEQLRVKEKIGELEAEIaslersiAEKERELEDAE---- 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    467 vlmtkERQSNDEIQAARQKM-IAGLTGLLGAESDIGVKRMGELDEKpfldvcKLRYSANEARVEA-ATLCSTWKENLKNp 544
Cdd:TIGR02169  322 -----ERLAKLEAEIDKLLAeIEELEREIEEERKRRDKLTEEYAEL------KEELEDLRAELEEvDKEFAETRDELKD- 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    545 swQPFKREGTGDGAEEVVDEDDEQLKKLKR--EWGKEVHNAVKAALVEMNEYNASGRYPTSELWNfKEGRKATLKEVITF 622
Cdd:TIGR02169  390 --YREKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAGIEAKINELEEEKEDKALEIKK-QEWKLEQLAADLSK 466

                          330
                   ....*....|.
gi 42566188    623 ISTDIKNLKRK 633
Cdd:TIGR02169  467 YEQELYDLKEE 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
330-492 1.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  330 RKMRDLESRAKQLEkhEALTELERQkLDEDKRKSDAMNKSLQLASREQKKADESV-LRLVEEHQRQKEDALNKILL---- 404
Cdd:COG4913  610 AKLAALEAELAELE--EELAEAEER-LEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERLDAssdd 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  405 ---LEKQLDtkqTLEMEIQELKGKLQVMKhlgdDDDEAVQTKMKEMNDELDDKKAELEDLESMNSVLMT---KERQSNDE 478
Cdd:COG4913  687 laaLEEQLE---ELEAELEELEEELDELK----GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAAL 759

                        170
                 ....*....|....
gi 42566188  479 IQAARQKMIAGLTG 492
Cdd:COG4913  760 GDAVERELRENLEE 773
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 307-463 1.84e-03

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: 40.29  E-value: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 307 QQMSLRHIQRI---LYDKEKLRNELDRKMRDLESRAKQLEK-----HEALTELERQ--KLDEDKRKSDAMNKSLQLASRE 376
Cdd:COG1579   5 DLRALLDLQELdseLDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEikRLELEIEEVEARIKKYEEQLGN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 377 QKKADE--SVLRLVEEHQRQKEDALNKILLLEKQLDTKQTlemEIQELKGKLQVMKHLGDDDDEAVQTKMKEMNDELDDK 454
Cdd:COG1579  85 VRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEE---ELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161


                ....*....
gi 42566188 455 KAELEDLES 463
Cdd:COG1579 162 EAEREELAA 170
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 231-478 2.23e-03

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: 41.26  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    231 EYLSKEG----TLRTVSDILQNNVQDRNTLLDVLSNMIdmtnEDLNKAQHSYNRTAMSLQRvldEKKNLHQAFAEETKKM 306
Cdd:pfam15921  534 QHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQI----ENMTQLVGQHGRTAGAMQV---EKAQLEKEINDRRLEL 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    307 QQMslrhiqRILYDKEklrnelDRKMRDLESRAKQLekhealtELERQKL----DEDKRKSDAMNKSLQLASREQKKADE 382
Cdd:pfam15921  607 QEF------KILKDKK------DAKIRELEARVSDL-------ELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRN 667

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    383 SVLRLVEEHQRQKEDALNKIlllEKQLDTKQTLEMEIQELKGKLQ----VMKHLGDDDDEAVQTKMKeMNDELDDKKAEL 458
Cdd:pfam15921  668 ELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEqtrnTLKSMEGSDGHAMKVAMG-MQKQITAKRGQI 743

                          250       260
                   ....*....|....*....|
gi 42566188    459 EDLESMNSVLMTKERQSNDE 478
Cdd:pfam15921  744 DALQSKIQFLEEAMTNANKE 763
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 290-490 2.35e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 290 DEKKNLHQAFAEETKKMQQmslrhIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKS 369
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAE-----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 370 LQLASREQKKADESVLRLVEEHQRQkedalNKILLLEKQLDTKQTLEMeiqelkgkLQVMKHLGDDDDE------AVQTK 443
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDFLDAVRR--------LQYLKYLAPARREqaeelrADLAE 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42566188 444 MKEMNDELDDKKAELEDLESMNSvlmtKERQSNDEIQAARQKMIAGL 490
Cdd:COG4942 162 LAALRAELEAERAELEALLAELE----EERAALEALKAERQKLLARL 204
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 244-485 2.54e-03

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: 40.88  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   244 DILQNNVQDRNTLLDVLSNMIDMTNEDLNKAQHSYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMSLRHIQriLYDKEK 323
Cdd:pfam05557  86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN--LEKQQS 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   324 LRNELDRKMRDLESRAKQLEKHEALTELERQKL------DEDKRKSDAMNKSLqlasREQKKADEsvlrLVEEhqrQKED 397
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripelEKELERLREHNKHL----NENIENKL----LLKE---EVED 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   398 ALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDD------EAVQTKMKEMNDELDDKKAELEDLESMNSVLMTK 471
Cdd:pfam05557 233 LKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKA 312

                         250
                  ....*....|....
gi 42566188   472 ERQSNDEIQAARQK 485
Cdd:pfam05557 313 RRELEQELAQYLKK 326
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 320-488 2.83e-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: 41.09  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  320 DKEKLRNELDRKMRDLEsraKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASReqkKADESVLRLVEEHQRQKEDAL 399
Cdd:COG3096  833 DPEAELAALRQRRSELE---RELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANL---LADETLADRLEELREELDAAQ 906

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  400 ----------NKILLLEKQLDTKQT-------LEMEIQELKGKLQVMK--------------HLGDDDDEAVQTKMKEMN 448
Cdd:COG3096  907 eaqafiqqhgKALAQLEPLVAVLQSdpeqfeqLQADYLQAKEQQRRLKqqifalsevvqrrpHFSYEDAVGLLGENSDLN 986

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 42566188  449 DELddkKAELEDLESMNSVLMTKERQSNDEIQAARQKMIA 488
Cdd:COG3096  987 EKL---RARLEQAEEARREAREQLRQAQAQYSQYNQVLAS 1023
PRK09841 PRK09841
tyrosine-protein kinase;
210-429 3.00e-03

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 40.66  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  210 ESKAYGwcARADDFQSQGPIGEYLSKEGTLRTVSDI-----LQNNVQDRNTL--LDVLSNMIDMTNEDLNKAQHSYNRTA 282
Cdd:PRK09841 159 ENGHYT--LEGEEFTVNGMVGQRLEKDGVALTIADIkakpgTQFVLSQRTELeaINALQETFTVSERSKESGMLELTMTG 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  283 MSLQ---RVLDEKKN--LHQAFAEETKKMQQmSLRHIQRILydkEKLRNELDrkmrdlesrakqlekhealteLERQKLD 357
Cdd:PRK09841 237 DDPQlitRILNSIANnyLQQNIARQAAQDSQ-SLEFLQRQL---PEVRSELD---------------------QAEEKLN 291

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42566188  358 EDKRKSDAMNKSLQLAS-REQ-----KKADESVLRLVEEHQRQKEDALNKILLLEKqldtKQTLEMEIQELKGKLQVM 429
Cdd:PRK09841 292 VYRQQRDSVDLNLEAKAvLEQivnvdNQLNELTFREAEISQLYKKDHPTYRALLEK----RQTLEQERKRLNKRVSAM 365
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 253-486 3.52e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   253 RNTLLDVLSNMIDMTNEDLNKaqhsYNRTAMSLQRVLDEKKNL--HQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDR 330
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEYTVR----YNGQTMTENEFLNQLLHIvqHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   331 KmRDLE----SRAKQLEKHEAL------------TELERQKLDEDKRKSDAMNKslQLASREQKKADEsVLRLVEEHQRQ 394
Cdd:pfam17380 315 R-RKLEeaekARQAEMDRQAAIyaeqermamereRELERIRQEERKRELERIRQ--EEIAMEISRMRE-LERLQMERQQK 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   395 KEDALNKILLLEKQldtkQTLEMEIQ-ELKGKLQVMKHLGDDDDEAVQTKMKEMNDE--LDDKKAELEDLESMNSVlmtk 471
Cdd:pfam17380 391 NERVRQELEAARKV----KILEEERQrKIQQQKVEMEQIRAEQEEARQREVRRLEEEraREMERVRLEEQERQQQV---- 462

                         250
                  ....*....|....*
gi 42566188   472 ERQSNDEIQAARQKM 486
Cdd:pfam17380 463 ERLRQQEEERKRKKL 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 327-488 3.60e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    327 ELDRKMRDLESRAKQLEK-----HEALTELE------RQKLDEDKRKSDAMNKSLQLASREQKKADESVLRLVEEHQRQK 395
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKalaelRKELEELEeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    396 EDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDE---AVQTKMKEMNDELDDKKAELEDLESMNSVLMTKE 472
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRL 840

                          170
                   ....*....|....*.
gi 42566188    473 RQSNDEIQAARQKMIA 488
Cdd:TIGR02168  841 EDLEEQIEELSEDIES 856
PTZ00121 PTZ00121
MAEBL; Provisional
 269-457 4.52e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   269 EDLNKAQHSynRTAMSLQRVLDEKKNlhqafAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEAL 348
Cdd:PTZ00121 1293 DEAKKAEEK--KKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   349 TELERQKLDEDKRKSDAMNKSlqlaSREQKKADEsvLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQ---ELKGK 425
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKK----AEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKK 1439

                         170       180       190
                  ....*....|....*....|....*....|..
gi 42566188   426 LQVMKHLgdddDEAVQTKMKEMNDELDDKKAE 457
Cdd:PTZ00121 1440 AEEAKKA----DEAKKKAEEAKKAEEAKKKAE 1467
PTZ00121 PTZ00121
MAEBL; Provisional
 280-586 5.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   280 RTAMSLQRVLDEKKNlhqafAEETKKMQQMSLRHIQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDED 359
Cdd:PTZ00121 1470 KKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   360 KRKSDAMNKslqlaSREQKKADEsvLRLVEEHQRQKEDalnKILLLEKQLDTKQTLEMEIQElkgklqVMKHLGDDDDEA 439
Cdd:PTZ00121 1545 KKKADELKK-----AEELKKAEE--KKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEE------VMKLYEEEKKMK 1608

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188   440 VQTKMKEmnDELDDKKAELEDLESMNSVLMTKERQSNDEIQAARQKMIAGLTGLLGAESDigvKRMGELDEKpfldvckl 519
Cdd:PTZ00121 1609 AEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE---AKKAEEDKK-------- 1675

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42566188   520 rySANEARVEaatlcstwKENLKNPSWQPFKREGTGDGAEEVVDEDDEQLKKLKREWGKEVHNAVKA 586
Cdd:PTZ00121 1676 --KAEEAKKA--------EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 183-450 5.85e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    183 AAATELEKEFETQGSCKKEWTERSGDSEskaygwcARADDFQSQGPIGEYLSKE--------GTLRTVSDILQNNVQDRN 254
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIE-------QLKEELKALREALDELRAEltllneeaANLRERLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    255 TLLDVLSNMIDMTNEDLNKAQHSYNrtamSLQRVLDEkknLHQAFAEETKKMQQMslrhiQRILYDKEKLRNELDRKMRD 334
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIE----ELEELIEE---LESELEALLNERASL-----EEALALLRSELEELSEELRE 905

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188    335 LESRAKQLEK--HEALTELERQKLDEDKRKSDAMNKSLQLASREQKKADEsVLRLVEEHQRQKEDALNKILLLEKQLDTK 412
Cdd:TIGR02168  906 LESKRSELRRelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRLENKIKEL 984

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 42566188    413 QTLEM----EIQELKGKLQVMKHLGDDDDEAVQTKMK---EMNDE 450
Cdd:TIGR02168  985 GPVNLaaieEYEELKERYDFLTAQKEDLTEAKETLEEaieEIDRE 1029
COG5022 COG5022
Myosin heavy chain [General function prediction only];
277-493 7.26e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.68  E-value: 7.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  277 SYNRTAMSLQRVLDEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRnELDRKMRDLESRAKQLEKHEALTELErqkl 356
Cdd:COG5022  814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS-LLKKETIYLQSAQRVELAERQLQELK---- 888

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  357 DEDKRKSDAMNKSLQLASR--EQKKADESVLRLVEEHQRQkEDALNKILLLEKQLDTKQTLEMEIQELKGKLQvmkhlgd 434
Cdd:COG5022  889 IDVKSISSLKLVNLELESEiiELKKSLSSDLIENLEFKTE-LIARLKKLLNNIDLEEGPSIEYVKLPELNKLH------- 960

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 42566188  435 dddeavqtkmkEMNDELDDKKAELEDLESMNSVLMTKERQSNDEIQAARQKMIAGLTGL 493
Cdd:COG5022  961 -----------EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQY 1008
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
280-493 8.24e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  280 RTAMSLQRVLDEKKNLHQAFAEETKKMQQMSLRHIQRILYDKEKLRNELDR---KMRDLESRAKQLEKHEALTELERQKL 356
Cdd:COG4913  249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElraELARLEAELERLEARLDALREELDEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188  357 DEDKRKSDamNKSLQLASREQKKADESVLRLVEEHQRQKEDA--------LNKILLLEKQLDTKQTLEmEIQELKGKLQv 428
Cdd:COG4913  329 EAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLaalglplpASAEEFAALRAEAAALLE-ALEEELEALE- 404

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42566188  429 mkhlgDDDDEAVQTKmKEMNDELDDKKAELEDLESmnsvlmtkeRQSN--DEIQAARqKMIAGLTGL 493
Cdd:COG4913  405 -----EALAEAEAAL-RDLRRELRELEAEIASLER---------RKSNipARLLALR-DALAEALGL 455
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
232-434 8.29e-03

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 39.34  E-value: 8.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 232 YLSKEGTLRTVSDILQNNVQDRNTLLDVLSNMIDMTNEDLNkaqhsyNRTAMSLQRVLDEKKNL--HQAFAEETKKMQQM 309
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLK------SRIDLIMKSIISGTFERkkLLKEEGWKYKSTLQ 433

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566188 310 SLRH--IQRILYDKEKLRNELDRKMRDLESRAKQLEKHEALTELERQKLDEDKRKSDAMNKSLQLASREQKKADESVLRL 387
Cdd:COG5059 434 FLRIeiDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRDHL 513

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42566188 388 VEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGD 434
Cdd:COG5059 514 NGSNSSTKELSLNQVDLAGSERKVSQSVGELLRETQSLNKSLSSLGD 560
 
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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