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Conserved domains on  [gi|51092293|ref|NP_001003667|]
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keratin, type II cytoskeletal 1b [Mus musculus]

Protein Classification

type II keratin( domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
166-479 9.67e-122

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 9.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   166 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRtSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEP-SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   246 MQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILS 325
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   326 MDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQ 405
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092293   406 VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
132-163 3.43e-17

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 78.93  E-value: 3.43e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51092293   132 PSYPPGGIHEVTINQSLLEPLHLEVDPEIQRV 163
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
166-479 9.67e-122

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 9.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   166 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRtSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEP-SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   246 MQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILS 325
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   326 MDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQ 405
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092293   406 VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
132-163 3.43e-17

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 78.93  E-value: 3.43e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51092293   132 PSYPPGGIHEVTINQSLLEPLHLEVDPEIQRV 163
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
338-484 3.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 338 IDAVRAQYEIIAQKSKDEAEAL--YQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISD 415
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51092293 416 AEERGERA---LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGAL 484
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
219-474 6.19e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   219 EEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDvdaafmgKSDLQSKVDTLYGE 298
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNK 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   299 INFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDavraqyeiiAQKSKDEAEALYQTKYQELQITAGKHGD-- 376
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK---------KQQEINEKTTEISNTQTQLNQLKDEQNKik 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   377 --------DLKNSKMEISELNRNIQRLRAEIANIKKQ-VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAK 447
Cdd:TIGR04523 267 kqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
                         250       260
                  ....*....|....*....|....*..
gi 51092293   448 LLRDYQAMLGAKLSLDVEIATYRQLLE 474
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIE 373
PRK09039 PRK09039
peptidoglycan -binding protein;
307-447 3.36e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  307 DTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEiIAQKSKDEAEALYQTKYQELQITAGKHGD---DLKNSKM 383
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293  384 EISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGeralQNAKQKLQDMEE----ALQQAKEDLAK 447
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRrlnvALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
166-479 9.67e-122

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 9.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   166 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRtSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEP-SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   246 MQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILS 325
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   326 MDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQ 405
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51092293   406 VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
132-163 3.43e-17

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 78.93  E-value: 3.43e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51092293   132 PSYPPGGIHEVTINQSLLEPLHLEVDPEIQRV 163
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
338-484 3.64e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 338 IDAVRAQYEIIAQKSKDEAEAL--YQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISD 415
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51092293 416 AEERGERA---LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGAL 484
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
219-474 6.19e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   219 EEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDvdaafmgKSDLQSKVDTLYGE 298
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNK 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   299 INFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDavraqyeiiAQKSKDEAEALYQTKYQELQITAGKHGD-- 376
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK---------KQQEINEKTTEISNTQTQLNQLKDEQNKik 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   377 --------DLKNSKMEISELNRNIQRLRAEIANIKKQ-VEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAK 447
Cdd:TIGR04523 267 kqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
                         250       260
                  ....*....|....*....|....*..
gi 51092293   448 LLRDYQAMLGAKLSLDVEIATYRQLLE 474
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIE 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
237-474 2.14e-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: 44.28  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    237 LRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVdaafmgkSDLQSKVDTLYGEINFLKYLFDTELSQIQTh 316
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL-------EQLRKELEELSRQISALRKDLARLEAEVEQ- 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    317 vsdtnviLSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKyQELQITAGKHGDDLKNSKMEISELNRNIQRLR 396
Cdd:TIGR02168  745 -------LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLN 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    397 AEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEA---LQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLL 473
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSEL 896

                   .
gi 51092293    474 E 474
Cdd:TIGR02168  897 E 897
PRK09039 PRK09039
peptidoglycan -binding protein;
307-447 3.36e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  307 DTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEiIAQKSKDEAEALYQTKYQELQITAGKHGD---DLKNSKM 383
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS-AAEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293  384 EISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGeralQNAKQKLQDMEE----ALQQAKEDLAK 447
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRrlnvALAQRVQELNR 194
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
212-407 3.58e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  212 SSLEPVFEEF--ISQLQRQVDVLTTEQLRQnteirnmqdVVEDYKNKYEDEINKRTNAendfvvlkkdvdaafmgKSDLQ 289
Cdd:PRK05771  60 DKLRSYLPKLnpLREEKKKVSVKSLEELIK---------DVEEELEKIEKEIKELEEE-----------------ISELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  290 SKVDTLYGEINFLKYL--FDTELSQIQTHvSDTNVILSMDNNRSLDLDSIIDAVRAQYEI----------IAQKSKDEAE 357
Cdd:PRK05771 114 NEIKELEQEIERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDE 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 51092293  358 ALYQTK---YQELQITAGKHGDD-LKNSKMEISELNRNIQRLRAEIANIKKQVE 407
Cdd:PRK05771 193 VEEELKklgFERLELEEEGTPSElIREIKEELEEIEKERESLLEELKELAKKYL 246
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
170-405 6.45e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 43.12  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    170 QIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTS-SLEPVFEE---FISQLQRQVDVLTTEQLRQNTEIRN 245
Cdd:TIGR01612  580 EIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAiDLKKIIENnnaYIDELAKISPYQVPEHLKNKDKIYS 659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    246 MqdVVEDYKNKYEDEINKRTNaENDFVVLKKDVDAA--FMGKSDLQSKVDTLYGEINflkylfDTELSQIQTHVSdtnvi 323
Cdd:TIGR01612  660 T--IKSELSKIYEDDIDALYN-ELSSIVKENAIDNTedKAKLDDLKSKIDKEYDKIQ------NMETATVELHLS----- 725
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    324 lSMDNNRSLDLDSIidaVRAQYEIIAQKSKDEAEALYQTKYQELQITA-----GKHGDDLKNSKMEISELnRNIQRLRAE 398
Cdd:TIGR01612  726 -NIENKKNELLDII---VEIKKHIHGEINKDLNKILEDFKNKEKELSNkindyAKEKDELNKYKSKISEI-KNHYNDQIN 800

                   ....*..
gi 51092293    399 IANIKKQ 405
Cdd:TIGR01612  801 IDNIKDE 807
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-471 1.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  329 NRSLDLDSIIDAVRAQYEIiAQKSKDEAEALYQTKYQELQiTAGkhGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEG 408
Cdd:COG4913  295 AELEELRAELARLEAELER-LEARLDALREELDELEAQIR-GNG--GDRLEQLEREIERLERELEERERRRARLEALLAA 370
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51092293  409 MHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQ 471
Cdd:COG4913  371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
156-481 1.14e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 41.76  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  156 VDPEiQRVKTQEREQIKTLNNKFASFIDKVRfleqqNQVLQTKwellqqvNTSTRTSslEPVFEEFISQLQRQVD----- 230
Cdd:PLN03229 413 VDPE-RKVNMKKREAVKTPVRELEGEVEKLK-----EQILKAK-------ESSSKPS--ELALNEMIEKLKKEIDleyte 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  231 ------------VLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFM-----GKSDLQSKVD 293
Cdd:PLN03229 478 aviamglqerleNLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEfsrakALSEKKSKAE 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  294 TLYGEIN-FLKYLFD-----------------TELSQIQTHVSDT-NVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKD 354
Cdd:PLN03229 558 KLKAEINkKFKEVMDrpeikekmealkaevasSGASSGDELDDDLkEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKD 637
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  355 EAEAL----YQTKYQELQITAGKHGDDLKNSkmeiSELNRNIQRLRAEIAnikkqvegmhglisdaeERGERALQNAKQK 430
Cdd:PLN03229 638 TAEQTpppnLQEKIESLNEEINKKIERVIRS----SDLKSKIELLKLEVA-----------------KASKTPDVTEKEK 696
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51092293  431 LQDMEealQQAKEDLAKLLrDYQAMLGAKLSLDVEIATYRQLLEGEESRMS 481
Cdd:PLN03229 697 IEALE---QQIKQKIAEAL-NSSELKEKFEELEAELAAARETAAESNGSLK 743
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
309-478 1.23e-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: 41.97  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    309 ELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEII--AQKSKDEAEALYQTKYQELQItagkhgddlknskmEIS 386
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEEEIEELQKELYALAN--------------EIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    387 ELNRNIQRLRAEIANIKKQVEgmhgLISDAEERGERALQNAKQKLQDMEEALQQAKED-------LAKLLRDYQAMLGAK 459
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLE----ELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRL 374
                          170       180
                   ....*....|....*....|...
gi 51092293    460 LSLDVEIATYR----QLLEGEES 478
Cdd:TIGR02168  375 EELEEQLETLRskvaQLELQIAS 397
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
296-451 1.39e-03

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


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 41.25  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   296 YGEINFLKYL-FDTEL-SQIQTHVSDTNVILSMDNNRSLDldSIIDAVRAQYEIIAQKskdeaEALYQTKYQELQITAGK 373
Cdd:TIGR04320 207 DDKINAGAYLgVSISNdGGVTIHFVNFNDSYIADGNKFDK--TPIPNPPNSLAALQAK-----LATAQADLAAAQTALNT 279
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293   374 HGDDLKNSKMEISELNRNIQRLRAEIANIKKQvegmhglisdAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRD 451
Cdd:TIGR04320 280 AQAALTSAQTAYAAAQAALATAQKELANAQAQ----------ALQTAQNNLATAQAALANAEARLAKAKEALANLNAD 347
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
349-455 1.66e-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: 40.90  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 349 AQKSKDEAEALyQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERgeraLQNAK 428
Cdd:COG4942  15 AAAQADAAAEA-EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89
                        90       100
                ....*....|....*....|....*..
gi 51092293 429 QKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:COG4942  90 KEIAELRAELEAQKEELAELLRALYRL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
346-479 3.25e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 346 EIIAQKSKDEAE-ALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERA- 423
Cdd:COG1196 257 ELEAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELe 336
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51092293 424 --LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESR 479
Cdd:COG1196 337 eeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
149-449 3.71e-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: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    149 LEPLHLEVDP--EIQRVKTQERE-QIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQvNTSTRTSSLEpVFEEFISQL 225
Cdd:TIGR02168  202 LKSLERQAEKaeRYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA-ELQELEEKLE-ELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    226 QRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYL 305
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    306 FDTELSQIQ---THVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSK 382
Cdd:TIGR02168  360 LEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51092293    383 MEISELNRNIQRLRAEIANIKKQVEGMHGLISDAE------ERGERALQNAKQKLQDMEEALQQAKEDLAKLL 449
Cdd:TIGR02168  440 AELEELEEELEELQEELERLEEALEELREELEEAEqaldaaERELAQLQARLDSLERLQENLEGFSEGVKALL 512
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
305-484 4.18e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 305 LFDTELSQIQTHVSDTNVILSMDNNRsldLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQitagkhgddlknskME 384
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEAR---LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE--------------AE 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 385 ISELNRN-------IQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAmlg 457
Cdd:COG3206 279 LAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--- 355
                       170       180       190
                ....*....|....*....|....*....|
gi 51092293 458 akLSLDVEIA--TYRQLLEG-EESRMSGAL 484
Cdd:COG3206 356 --LEREVEVAreLYESLLQRlEEARLAEAL 383
HAUS5 pfam14817
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ...
364-460 4.38e-03

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464332 [Multi-domain]  Cd Length: 643  Bit Score: 40.03  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293   364 YQELQITAGKHGDdlKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQ---NAKQKlQDMEEALQQ 440
Cdd:pfam14817  60 YGGLQDKGKAESR--QSAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDeisDSRHR-QLLLEAYDQ 136
                          90       100
                  ....*....|....*....|
gi 51092293   441 AKEDLAKLLRDYQAMLGAKL 460
Cdd:pfam14817 137 QCEEARKILAEDHQRLQGQL 156
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
188-455 4.87e-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: 40.10  E-value: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    188 LEQQNQVLQTKWELLQQVntSTRTSSLEPVFEefisQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKyeDEINKRTNA 267
Cdd:pfam15921  446 MERQMAAIQGKNESLEKV--SSLTAQLESTKE----MLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    268 EndfvvlkkdvdaafmgKSDLQSKVDTLYGEINFLKYLFDtELSQIQTHVSDTNVILSmdnnrslDLDSIIDAVRAQYEI 347
Cdd:pfam15921  518 E----------------ITKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMA-------EKDKVIEILRQQIEN 573
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293    348 IAQKSKDEAEALYQTKYQELQITagkhgDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMH----GLISDAEERgERA 423
Cdd:pfam15921  574 MTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSER-LRA 647
                          250       260       270
                   ....*....|....*....|....*....|..
gi 51092293    424 LQNAKQKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:pfam15921  648 VKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
PRK01156 PRK01156
chromosome segregation protein; Provisional
155-477 6.59e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  155 EVDPEIQRVKTQE-REQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVN------TSTRTSSLEPVFEEF---ISQ 224
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  225 LQRQVDVLTTEQLRQNTEIRNMQDVvEDYKNKyeDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKY 304
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKR-KEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  305 LFDTELSQIQTHVSDTNVILSmdnnrSLDldsiIDAVRAQYEIIAQKSKDEAEALYQTK--------YQELQITA-GKHG 375
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LID----IETNRSRSNEIKKQLNDLESRLQEIEigfpddksYIDKSIREiENEA 628
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  376 DDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQnAKQKLQDMEEALQQAKEDLAKLLRDYQAM 455
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEIL 707
                        330       340
                 ....*....|....*....|..
gi 51092293  456 LGAKLSLDVEIATYRQLLEGEE 477
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK 729
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
222-479 6.72e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 222 ISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFvvlkkdvdaafmgkSDLQSKVDTLYGEINF 301
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE--------------YELLAELARLEQDIAR 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 302 LKylfdTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLkns 381
Cdd:COG1196 307 LE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE--- 379
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 382 kmEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLS 461
Cdd:COG1196 380 --ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                       250
                ....*....|....*...
gi 51092293 462 LDVEIATYRQLLEGEESR 479
Cdd:COG1196 458 EEALLELLAELLEEAALL 475
46 PHA02562
endonuclease subunit; Provisional
331-479 9.24e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 9.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  331 SLDLDSIIDAVRAQYEII--AQKSKDEAEALYQTKYQELQITAGKH-------GDDLKNSKMEISELNRNIQRLRAEIAN 401
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIeeQRKKNGENIARKQNKYDELVEEAKTIkaeieelTDELLNLVMDIEDPSAALNKLNTAAAK 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  402 IKKQVEGMHGL----------------ISDAEERGERALQNAKQkLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVE 465
Cdd:PHA02562 267 IKSKIEQFQKVikmyekggvcptctqqISEGPDRITKIKDKLKE-LQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK 345
                        170
                 ....*....|....
gi 51092293  466 IATYRQLLEGEESR 479
Cdd:PHA02562 346 ISTNKQSLITLVDK 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
338-484 9.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293 338 IDAVRAQYEIiAQKSKDEAEALYQTKYQELQITAGKhgddLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAE 417
Cdd:COG1196 234 LRELEAELEE-LEAELEELEAELEELEAELAELEAE----LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51092293 418 ERgeraLQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGAL 484
Cdd:COG1196 309 ER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-483 9.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51092293  333 DLDSIIDAVRAQ---YEIIAQKSKDEAEALY-QTKYQELQITAgkhgDDLKNSKMEISELNRNIQRLRAEIANIKKQVEG 408
Cdd:COG4913  635 ALEAELDALQERreaLQRLAEYSWDEIDVASaEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDE 710
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51092293  409 MHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGA 483
Cdd:COG4913  711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
 
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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