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Conserved domains on  [gi|15218369|ref|NP_173043|]
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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 ...
 502-632 3.12e-71

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: 225.93  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   502 KRMGELDEKPFLDVCKLRYSANEAAVEAATLCSTWQENLKNPSWQPFKHEGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 581
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15218369   582 AVKTALVEMNEYNASGRYTTPELWNFKEGRKATLKEVITFISNDIKILKRK 632
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 117-224 2.24e-40

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: 143.08  E-value: 2.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   117 VYVWPWMGIVVNPLKE-ADDKELLLDSAYWLQT-LSKFKPIEVNAFWVEQDSIVGVIAKFNGDWSGFAGATELEKEFETQ 194
Cdd:pfam03468   3 LFVWPWMGIVVNIPTEqDEDGRWVGMSGEELKDkLSRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKHFEAQ 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15218369   195 GSSKKEWTE-RSGDSESKAYGWCARADDFES 224
Cdd:pfam03468  83 GHGKKDWGGkRNRGSGSKLYGWVARADDYNS 113
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 41-83 9.05e-20

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: 82.57  E-value: 9.05e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15218369    41 CPFCAGKKKQDYKYKELYAHATGVSKGSATRSALQKANHLALA 83
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-499 3.14e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 295 HQAFADETKKMQ-QMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLAS 373
Cdd:COG1196 215 YRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 374 REQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLqvmkhlgddddEAVQKKMKEMNDELDDK 453
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-----------EEAEEELEEAEAELAEA 363

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15218369 454 KAELEGLESMNSVLMTKERQSNDEIQAARKKLIAGLTGLLGAETDI 499
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
 
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 ...
 502-632 3.12e-71

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: 225.93  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   502 KRMGELDEKPFLDVCKLRYSANEAAVEAATLCSTWQENLKNPSWQPFKHEGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 581
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15218369   582 AVKTALVEMNEYNASGRYTTPELWNFKEGRKATLKEVITFISNDIKILKRK 632
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 117-224 2.24e-40

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: 143.08  E-value: 2.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   117 VYVWPWMGIVVNPLKE-ADDKELLLDSAYWLQT-LSKFKPIEVNAFWVEQDSIVGVIAKFNGDWSGFAGATELEKEFETQ 194
Cdd:pfam03468   3 LFVWPWMGIVVNIPTEqDEDGRWVGMSGEELKDkLSRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKHFEAQ 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15218369   195 GSSKKEWTE-RSGDSESKAYGWCARADDFES 224
Cdd:pfam03468  83 GHGKKDWGGkRNRGSGSKLYGWVARADDYNS 113
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 118-222 9.76e-40

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: 140.95  E-value: 9.76e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 118 YVWPWMGIVVNPLKEADD--KELLLDSAYWLQTLSKFKPIEVNAFWVEQDSIVGVIAKFNGDWSGFAGATELEKEFETQG 195
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDnrKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEVDG 80

                        90       100
                ....*....|....*....|....*..
gi 15218369 196 SSKKEWTERSGDSESKAYGWCARADDF 222
Cdd:cd12266  81 HGKKDWRNKKGGRKSKLYGWLARADDY 107
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 41-83 9.05e-20

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: 82.57  E-value: 9.05e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15218369    41 CPFCAGKKKQDYKYKELYAHATGVSKGSATRSALQKANHLALA 83
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-499 3.14e-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: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 295 HQAFADETKKMQ-QMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLAS 373
Cdd:COG1196 215 YRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 374 REQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLqvmkhlgddddEAVQKKMKEMNDELDDK 453
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-----------EEAEEELEEAEAELAEA 363

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15218369 454 KAELEGLESMNSVLMTKERQSNDEIQAARKKLIAGLTGLLGAETDI 499
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-485 7.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    230 EYLSKEGQLRTVS-DISQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADetkkmqqm 308
Cdd:TIGR02168  214 RYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-------- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    309 slrhIQKILYDKEKLSNELDRKMRDLESRAKQLEKH----EALTELDRQKLDEDKRKSDAMNKSLQlasrEQKKADESVL 384
Cdd:TIGR02168  286 ----LQKELYALANEISRLEQQKQILRERLANLERQleelEAQLEELESKLDELAEELAELEEKLE----ELKEELESLE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    385 RLVEEHQRQKEDALNKILLLEKQLDTKQT----LEMEIQELKGKLQVMK---------------HLGDDDDEAVQKKMKE 445
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEIERLEarlerledrrerlqqEIEELLKKLEEAELKE 437

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 15218369    446 MNDELDDKKAELEGLESMNSVLMTKERQSNDEIQAARKKL 485
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 229-485 1.24e-04

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: 45.49  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    229 GEYLSKEGQLRTVSDISQKNV-------QDRntvLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLdekknlhQAFADE 301
Cdd:pfam15921  238 GRIFPVEDQLEALKSESQNKIelllqqhQDR---IEQLISEHEVEITGLTEKASSARSQANSIQSQL-------EIIQEQ 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    302 TKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEAL--TELDRQKLDEDK--RKSDAMNKSLQ-LASREQ 376
Cdd:pfam15921  308 ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLanSELTEARTERDQfsQESGNLDDQLQkLLADLH 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    377 KKADESVLRLVEEHQRQKEDALNKILL--LEKQLDTKQtleMEIQELKGKLQVMKhlgddddEAVQKKMKEMNDELDDKK 454
Cdd:pfam15921  388 KREKELSLEKEQNKRLWDRDTGNSITIdhLRRELDDRN---MEVQRLEALLKAMK-------SECQGQMERQMAAIQGKN 457

                          250       260       270
                   ....*....|....*....|....*....|....
gi 15218369    455 AELEGLESMNSVL-MTKE--RQSNDEIQAARKKL 485
Cdd:pfam15921  458 ESLEKVSSLTAQLeSTKEmlRKVVEELTAKKMTL 491
PTZ00121 PTZ00121
MAEBL; Provisional
 279-456 6.78e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   279 RTAMSLQRVLDEKKNlhqafADETKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDED 358
Cdd:PTZ00121 1302 KKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   359 KRKSDAMNKSlqlaSREQKKADEsvLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQ---ELKGKLQVMKHLgddd 435
Cdd:PTZ00121 1377 KKKADAAKKK----AEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAKKA---- 1446

                         170       180
                  ....*....|....*....|.
gi 15218369   436 DEAVQKKMKEMNDELDDKKAE 456
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAE 1467
 
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 ...
 502-632 3.12e-71

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: 225.93  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   502 KRMGELDEKPFLDVCKLRYSANEAAVEAATLCSTWQENLKNPSWQPFKHEGTGDGAEEVVDEDDEQLKKLKREWGKEVHN 581
Cdd:pfam03469   1 KRMGELDEKPFLNACKQKFSNEEAEVKAAELCSLWEEELKDPEWHPFKVVMVDGKHKEVIDEDDEKLKELKEEYGEEVYN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15218369   582 AVKTALVEMNEYNASGRYTTPELWNFKEGRKATLKEVITFISNDIKILKRK 632
Cdd:pfam03469  81 AVTTALLELNEYNPSGRYPVPELWNFKEGRKATLKEGVDYILKQWKALKRK 131
XS pfam03468
XS domain; The XS (rice gene X and SGS3) domain is found in a family of plant proteins ...
 117-224 2.24e-40

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: 143.08  E-value: 2.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   117 VYVWPWMGIVVNPLKE-ADDKELLLDSAYWLQT-LSKFKPIEVNAFWVEQDSIVGVIAKFNGDWSGFAGATELEKEFETQ 194
Cdd:pfam03468   3 LFVWPWMGIVVNIPTEqDEDGRWVGMSGEELKDkLSRFNPLKVKPLYGPQGHTGIAIVEFNKDWSGFKNAERFEKHFEAQ 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15218369   195 GSSKKEWTE-RSGDSESKAYGWCARADDFES 224
Cdd:pfam03468  83 GHGKKDWGGkRNRGSGSKLYGWVARADDYNS 113
RRM_like_XS cd12266
RNA recognition motif (RRM)-like XS domain found in plants; This XS (named after rice gene X ...
 118-222 9.76e-40

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: 140.95  E-value: 9.76e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 118 YVWPWMGIVVNPLKEADD--KELLLDSAYWLQTLSKFKPIEVNAFWVEQDSIVGVIAKFNGDWSGFAGATELEKEFETQG 195
Cdd:cd12266   1 IVWPWMGIVVNTPTTKDDnrKMEGGSNKELLERLIKFGPTRVKPLWNPQGHTGTAIVKFNSDWNGFRNALRFEKAFEVDG 80

                        90       100
                ....*....|....*....|....*..
gi 15218369 196 SSKKEWTERSGDSESKAYGWCARADDF 222
Cdd:cd12266  81 HGKKDWRNKKGGRKSKLYGWLARADDY 107
zf-XS pfam03470
XS zinc finger domain; This domain is a putative nucleic acid binding zinc finger found in ...
 41-83 9.05e-20

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: 82.57  E-value: 9.05e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15218369    41 CPFCAGKKKQDYKYKELYAHATGVSKGSATRSALQKANHLALA 83
Cdd:pfam03470   1 CPFCPGKKKQDYKYKDLLQHASGVGASSNRRSAKEKASHRALA 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-499 3.14e-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: 3.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 295 HQAFADETKKMQ-QMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLAS 373
Cdd:COG1196 215 YRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 374 REQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLqvmkhlgddddEAVQKKMKEMNDELDDK 453
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-----------EEAEEELEEAEAELAEA 363

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15218369 454 KAELEGLESMNSVLMTKERQSNDEIQAARKKLIAGLTGLLGAETDI 499
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-485 7.03e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    230 EYLSKEGQLRTVS-DISQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADetkkmqqm 308
Cdd:TIGR02168  214 RYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-------- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    309 slrhIQKILYDKEKLSNELDRKMRDLESRAKQLEKH----EALTELDRQKLDEDKRKSDAMNKSLQlasrEQKKADESVL 384
Cdd:TIGR02168  286 ----LQKELYALANEISRLEQQKQILRERLANLERQleelEAQLEELESKLDELAEELAELEEKLE----ELKEELESLE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    385 RLVEEHQRQKEDALNKILLLEKQLDTKQT----LEMEIQELKGKLQVMK---------------HLGDDDDEAVQKKMKE 445
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEIERLEarlerledrrerlqqEIEELLKKLEEAELKE 437

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 15218369    446 MNDELDDKKAELEGLESMNSVLMTKERQSNDEIQAARKKL 485
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 281-500 2.32e-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: 47.76  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    281 AMSLQRVLDEKKNLHQAFADETKKMQQM--SLRHIQKILYDKEKLSNELDR---KMRDLESRAKQLEKHEALTeldRQKL 355
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAEIeeLEREIEEERKRRDKLTEEYAElkeELEDLRAELEEVDKEFAET---RDEL 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    356 DEDKRKSDAMNKSLQLASREQKKADESVLRL---VEEHQRQKEDALNKILLLEKQLDTKQtleMEIQELKGKL-QVMKHL 431
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLseeLADLNAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLeQLAADL 464

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218369    432 GDDDDE--AVQKKMKEMNDELDDKKAELEGLESMNSVLMTKERQSndeiQAARKKLIAGLTGLLGAETDIG 500
Cdd:TIGR02169  465 SKYEQElyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG----RAVEEVLKASIQGVHGTVAQLG 531
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-485 7.11e-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: 46.20  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    223 ESQGPIGEYLSKEGQLRTVSDISQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADET 302
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    303 KKMQQmslrhiqkilydkekLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLASREQKKADES 382
Cdd:TIGR02168  838 RRLED---------------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    383 vLRLVEEHQRQKEDALNKILLLEKQLDTK-QTLEMEIQELKGKLQVMKHLGDDDDEAVQKKMKEMNDELDDKKAELEG-- 459
Cdd:TIGR02168  903 -LRELESKRSELRRELEELREKLAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENki 981

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 15218369    460 -------LESMNSVLMTKERQSN-----DEIQAARKKL 485
Cdd:TIGR02168  982 kelgpvnLAAIEEYEELKERYDFltaqkEDLTEAKETL 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 310-487 7.24e-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: 46.20  E-value: 7.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    310 LRHIQKILYDKEKLSNELDRKMRDLESRAKQ----LEKHEALTELD-----------RQKLDEDKRKSDAMNKSLQLASR 374
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKaeryKELKAELRELElallvlrleelREELEELQEELKEAEEELEELTA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    375 EQKKADESVLRLVEEHQ--RQKEDALNKILLLEKQLdtKQTLEMEIQELKGKL----QVMKHLGDDDDEAVQKK------ 442
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSelEEEIEELQKELYALANE--ISRLEQQKQILRERLanleRQLEELEAQLEELESKLdelaee 338

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 15218369    443 MKEMNDELDDKKAELEGLESMNSVLMTKERQSNDEIQAARKKLIA 487
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 229-485 1.24e-04

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: 45.49  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    229 GEYLSKEGQLRTVSDISQKNV-------QDRntvLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLdekknlhQAFADE 301
Cdd:pfam15921  238 GRIFPVEDQLEALKSESQNKIelllqqhQDR---IEQLISEHEVEITGLTEKASSARSQANSIQSQL-------EIIQEQ 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    302 TKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEAL--TELDRQKLDEDK--RKSDAMNKSLQ-LASREQ 376
Cdd:pfam15921  308 ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLanSELTEARTERDQfsQESGNLDDQLQkLLADLH 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    377 KKADESVLRLVEEHQRQKEDALNKILL--LEKQLDTKQtleMEIQELKGKLQVMKhlgddddEAVQKKMKEMNDELDDKK 454
Cdd:pfam15921  388 KREKELSLEKEQNKRLWDRDTGNSITIdhLRRELDDRN---MEVQRLEALLKAMK-------SECQGQMERQMAAIQGKN 457

                          250       260       270
                   ....*....|....*....|....*....|....
gi 15218369    455 AELEGLESMNSVL-MTKE--RQSNDEIQAARKKL 485
Cdd:pfam15921  458 ESLEKVSSLTAQLeSTKEmlRKVVEELTAKKMTL 491
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 297-487 3.37e-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: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 297 AFADETKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEkhealteldrQKLDEDKRKSDAMNKSLQLASREQ 376
Cdd:COG3883  12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----------AELEALQAEIDKLQAEIAEAEAEI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 377 KKADESVLRLVEEHQRQK---------------EDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKhlgdDDDEAVQK 441
Cdd:COG3883  82 EERREELGERARALYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKK----AELEAKLA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15218369 442 KMKEMNDELDDKKAELEGLESMNSVLMTKERQSNDEIQAARKKLIA 487
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
325-431 4.11e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 325 NELDRKMRDLESRAKQLEKHeaLTELdRQKLDEDKRKSDAMNKSLQLASREQKkadESVLRLVEEHQRQKEdalnkILLL 404
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAE--VEEL-EAELEEKDERIERLERELSEARSEER---REIRKDREISRLDRE-----IERL 477

                        90       100
                ....*....|....*....|....*..
gi 15218369 405 EKQLDTkqtLEMEIQELKGKLQVMKHL 431
Cdd:COG2433 478 ERELEE---ERERIEELKRKLERLKEL 501
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 252-485 5.06e-04

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: 43.19  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   252 RNTVLEELSDMIAMTNEDLNKvqysYNRTAMSLQRVLDEKKNL--HQAFADETKKMQQMSLRHIQKILYDKEKLSNELDR 329
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEYTVR----YNGQTMTENEFLNQLLHIvqHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   330 KmRDLE----SRAKQLEKHEAL------------TELDRQKLDEDKRKSDAMNKslQLASREQKKADEsVLRLVEEHQRQ 393
Cdd:pfam17380 315 R-RKLEeaekARQAEMDRQAAIyaeqermamereRELERIRQEERKRELERIRQ--EEIAMEISRMRE-LERLQMERQQK 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   394 KEDALNKILLLEKQldtkQTLEMEIQ-ELKGKLQVMKHLGDDDDEAVQKKMKEMNDE--LDDKKAELEGLESMNSVlmtk 470
Cdd:pfam17380 391 NERVRQELEAARKV----KILEEERQrKIQQQKVEMEQIRAEQEEARQREVRRLEEEraREMERVRLEEQERQQQV---- 462

                         250
                  ....*....|....*
gi 15218369   471 ERQSNDEIQAARKKL 485
Cdd:pfam17380 463 ERLRQQEEERKRKKL 477
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 237-485 5.56e-04

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: 43.19  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   237 QLRTVSDISQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADETKKMQQMSLRHIQki 316
Cdd:pfam05557  80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN-- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   317 LYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKL------DEDKRKSDAMNKSLqlasREQKKADEsvlrLVEEh 390
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripelEKELERLREHNKHL----NENIENKL----LLKE- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   391 qrQKEDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDD------EAVQKKMKEMNDELDDKKAELEGLESMN 464
Cdd:pfam05557 229 --EVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnlrspEDLSRRIEQLQQREIVLKEENSSLTSSA 306

                         250       260
                  ....*....|....*....|.
gi 15218369   465 SVLMTKERQSNDEIQAARKKL 485
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKI 327
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 285-484 5.96e-04

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: 42.80  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   285 QRVLDEKKNLHQAFADETKKMQQMSLRHIQkilydkEKLSNELDRKMRDLESRAKQLEKHealteldRQKLDEDKRKSDA 364
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLE------EERAREMERVRLEEQERQQQVERL-------RQQEEERKRKKLE 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   365 MNKSlqlaSREQKKADESVLRLVEEHQRQKEDAL----NKILLLEKQLDTKQT-LEMEIQELKGKLQVMKHLGDDDDEAV 439
Cdd:pfam17380 479 LEKE----KRDRKRAEEQRRKILEKELEERKQAMieeeRKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRI 554

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15218369   440 QKKMKEMNDElddkKAELEGLEsmnsvlmtKERQSNDEIQAARKK 484
Cdd:pfam17380 555 QEQMRKATEE----RSRLEAME--------REREMMRQIVESEKA 587
PTZ00121 PTZ00121
MAEBL; Provisional
 279-456 6.78e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   279 RTAMSLQRVLDEKKNlhqafADETKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDED 358
Cdd:PTZ00121 1302 KKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   359 KRKSDAMNKSlqlaSREQKKADEsvLRLVEEHQRQKEDALNKILLLEKQLDTKQTLEMEIQ---ELKGKLQVMKHLgddd 435
Cdd:PTZ00121 1377 KKKADAAKKK----AEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAKKA---- 1446

                         170       180
                  ....*....|....*....|.
gi 15218369   436 DEAVQKKMKEMNDELDDKKAE 456
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAE 1467
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 245-487 6.91e-04

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: 42.80  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    245 SQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFAD-ETKKMQQMSLRHIQKILYDK--- 320
Cdd:pfam15921  494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQien 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    321 -EKLSNELDRKMRDLESRAKQLEK--HEALTELDRQKLDEDK-----RKSDAMNKSLQLASREQKKADESVLRLVEEHQR 392
Cdd:pfam15921  574 mTQLVGQHGRTAGAMQVEKAQLEKeiNDRRLELQEFKILKDKkdakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    393 QKEDALNKILLLEKQLDtkqTLEMEIQELKGKLQVMKHLGDDDDEAVQKKMKEMNDELDDKKAELEGLESMNSVLMTKER 472
Cdd:pfam15921  654 ERDQLLNEVKTSRNELN---SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730

                          250
                   ....*....|....*
gi 15218369    473 QSNDEIQAARKKLIA 487
Cdd:pfam15921  731 GMQKQITAKRGQIDA 745
PTZ00121 PTZ00121
MAEBL; Provisional
 257-474 8.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   257 EELSDMIAMTNEDLNKVQYSYNRTAMSLQRVlDEKKNLHQAFADETKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLES 336
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   337 RAKQLEKHEALTELDRQKLDEDKRKSDAMNKslqlASREQKKADESVLRlvEEHQRQKEDALNKILLLEKQldTKQTLEM 416
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKK----AEEDEKKAAEALKK--EAEEAKKAEELKKKEAEEKK--KAEELKK 1723

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   417 EIQELKGKLQVMKHLGDDDdeavQKKMKEMNDELDDKK--AELEGLESMNSVLMTKERQS 474
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEED----KKKAEEAKKDEEEKKkiAHLKKEEEKKAEEIRKEKEA 1779
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-499 9.27e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 325 NELDRKMRDLESRAKQLEKHEAL-TELDRQKLDEDKRKSDAMNKSLQLASREQKKADESVLRLVEEHQR---QKEDALNK 400
Cdd:COG1196 196 GELERQLEPLERQAEKAERYRELkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaELEELRLE 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 401 ILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDEAVQKKMKEMNDELDDKKAELEGLESMNSVLMTKERQSNDEIQA 480
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                       170
                ....*....|....*....
gi 15218369 481 ARKKLIAGLTGLLGAETDI 499
Cdd:COG1196 356 AEAELAEAEEALLEAEAEL 374
PRK01156 PRK01156
chromosome segregation protein; Provisional
 256-510 1.09e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  256 LEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADETKKMQQmslrhiqkILYDKEKLSNELDRKMRDLE 335
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI--------TLKEIERLSIEYNNAMDDYN 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  336 SRAKQLEKHEALTELdRQKLDEDKRKSDAMNKSLQLASREQKKADESVLRLVEEHQRQKEDALNKILLLEKQL-DTKQTL 414
Cdd:PRK01156 236 NLKSALNELSSLEDM-KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIeNKKQIL 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  415 EMEIQELKGKLQVMKHLGD-DDDEAVQKKMKEMNDELDDKKAELEGLESMNSVLMTKERQSNDEIQAARKKL------IA 487
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIermsafIS 394

                        250       260
                 ....*....|....*....|...
gi 15218369  488 GLTGLLGAETDIGVKRMGELDEK 510
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNEINVK 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-463 1.85e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 284 LQRVLDEKKNLHQAFADETKKMQQMSLRHIQKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSD 363
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 364 AMNKSLQLASREQKKADESVLRLVEEHQRQKEDALNKILLLEKQLDTK---QTLEMEIQELKGKLQVmkhLGD------D 434
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELERELERLEREIEA---LGPvnllaiE 788

                       170       180
                ....*....|....*....|....*....
gi 15218369 435 DDEAVQKKMKEMNDELDDKKAELEGLESM 463
Cdd:COG1196 789 EYEELEERYDFLSEQREDLEEARETLEEA 817
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 286-469 3.12e-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: 40.49  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   286 RVLDEKK--NLHQAFADETKKMQ--QMSLRHIQKILYDKEKLSNE----LDRKMRDLESRAKQLEKHEALTELDRQKLDE 357
Cdd:pfam05557  29 RIELEKKasALKRQLDRESDRNQelQKRIRLLEKREAEAEEALREqaelNRLKKKYLEALNKKLNEKESQLADAREVISC 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369   358 DKRKSDAMNKSLQLASREQKKADESVLRLVEEHQRQKEDALN---KILLLEKQLDTKQTLEMEIQELKGKLQVMkhlgdD 434
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEaeqLRQNLEKQQSSLAEAEQRIKELEFEIQSQ-----E 183

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15218369   435 DDEAVQKKMKEMNDELDDKKAELEGLESMNSVLMT 469
Cdd:pfam05557 184 QDSEIVKNSKSELARIPELEKELERLREHNKHLNE 218
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 314-489 3.21e-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: 39.52  E-value: 3.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 314 QKILYDKEKLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLASREQKKADEsvlRLVEEHQRQ 393
Cdd:COG1579   6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 394 KEDALNKILL-LEKQLDT----KQTLEMEIQELKGKLqvmkhlgddddEAVQKKMKEMNDELDDKKAELEGLESMNSVLM 468
Cdd:COG1579  83 GNVRNNKEYEaLQKEIESlkrrISDLEDEILELMERI-----------EELEEELAELEAELAELEAELEEKKAELDEEL 151

                       170       180
                ....*....|....*....|.
gi 15218369 469 TKERQSNDEIQAARKKLIAGL 489
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
285-489 5.19e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  285 QRVLDEKKNLHQAFAD-ETKKMQQMSLRHIQKILYDKEKLSNELDRKmRDLESRAKQLEKHEALTELdRQKLDEDKRKSD 363
Cdd:COG4913  228 DALVEHFDDLERAHEAlEDAREQIELLEPIRELAERYAAARERLAEL-EYLRAALRLWFAQRRLELL-EAELEELRAELA 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  364 AMNKSLQLASREQKKADESVLRLVEEHQ----RQKEDALNKILLLEKQLDTKQ-----------TLEMEI-------QEL 421
Cdd:COG4913  306 RLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERErrrarleallaALGLPLpasaeefAAL 385

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218369  422 KGKLQVMKHLGDDDDEAVQKKM-------KEMNDELDDKKAELEGLESmnsvlmtkeRQSN--DEIQAARKKLIAGL 489
Cdd:COG4913  386 RAEAAALLEALEEELEALEEALaeaeaalRDLRRELRELEAEIASLER---------RKSNipARLLALRDALAEAL 453
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 237-421 6.26e-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: 39.36  E-value: 6.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 237 QLRTVSDISQKNVQDRNTVLEELSDMIAMTNEDLNKVQYSYNRTAMSLQRVLDEKKNLHQAFADETKKMQQMSLRHIQKI 316
Cdd:COG4942  45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369 317 LYDKE-------------KLSNELDRKMRDLESRAKQLEKHEALTELDRQKLDEDKRKSDAMNKSLQLASREQKKadesv 383
Cdd:COG4942 125 LLSPEdfldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK----- 199

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15218369 384 lrLVEEHQRQKEDALNKILLLEKQldtKQTLEMEIQEL 421
Cdd:COG4942 200 --LLARLEKELAELAAELAELQQE---AEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 326-493 6.52e-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: 39.65  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    326 ELDRKMRDLESRAKQLEKH--EALTELD---------RQKLDEDKRKSDAMNKSLQLASREQKKADESVLRLVEEHQRQK 394
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKAlaELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369    395 EDALNKILLLEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDE---AVQKKMKEMNDELDDKKAELEGLESmNSVLMTKE 471
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLER-RIAATERR 839

                          170       180
                   ....*....|....*....|..
gi 15218369    472 RQSNDEIQAARKKLIAGLTGLL 493
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEI 861
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
310-485 6.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  310 LRHIQKILYDKEKLSNELDRKMRDLES---RAKQLEKHEALTELDRQKLDEDKRK-SDAMNKSLQLASREQKKADESV-- 383
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPek 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218369  384 ----LRLVEEHQRQKEDALNKILL----LEKQLDTKQTLEMEIQELKGKLQVMKHLGDDDDEA------------VQKKM 443
Cdd:PRK03918 389 lekeLEELEKAKEEIEEEISKITArigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeytaelkrIEKEL 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15218369  444 KEMNDELDDKKAELEGLESM--NSVLMTKERQSNDEIQAARKKL 485
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKL 512
 
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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