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Conserved domains on  [gi|119395750|ref|NP_006112|]
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keratin, type II cytoskeletal 1 [Homo sapiens]

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;
180-492 1.43e-128

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 381.19  E-value: 1.43e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  340 DNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395750  420 SNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
145-176 2.13e-19

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 85.48  E-value: 2.13e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119395750  145 PVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 176
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
Keratin_2_tail super family cl23814
Keratin type II cytoskeletal 1 tail;
493-512 3.08e-07

Keratin type II cytoskeletal 1 tail;


The actual alignment was detected with superfamily member pfam16210:

Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 49.97  E-value: 3.08e-07
                          10        20
                  ....*....|....*....|
gi 119395750  493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
180-492 1.43e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 381.19  E-value: 1.43e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  340 DNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395750  420 SNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
145-176 2.13e-19

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 85.48  E-value: 2.13e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119395750  145 PVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 176
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-487 1.83e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   235 INNLRRRVDQLKSDQSRLDSELknmqdmvedyrNKYEDEinkRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDF 314
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKAL-----------AELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   315 LTALY---QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDI---AQKSKAEAESLyQSKYEELQITAGRHG 388
Cdd:TIGR02168  745 LEERIaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeeLKALREALDEL-RAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   389 DSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKdaknKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEEL 899

                          250
                   ....*....|....*....
gi 119395750   469 MNTKLALDLEIATYRTLLE 487
Cdd:TIGR02168  900 SEELRELESKRSELRRELE 918
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
493-512 3.08e-07

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 49.97  E-value: 3.08e-07
                          10        20
                  ....*....|....*....|
gi 119395750  493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
232-487 9.41e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 9.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 232 ESFIN-NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQ 310
Cdd:COG3206  159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 311 EIDFLtalyQAELSQMQTQISETNVILSMDNNrsldlDSIIAEVKAQYEDIAQKsKAEAESLYQSKYEElqitagrhgds 390
Cdd:COG3206  234 ELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAE-LAELSARYTPNHPD----------- 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 391 vrnskieiselnrvIQRLRSEIDNVKKQIsnlQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmn 470
Cdd:COG3206  293 --------------VIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL-- 353

                        250
                 ....*....|....*....
gi 119395750 471 TKLALDLEIA--TYRTLLE 487
Cdd:COG3206  354 RRLEREVEVAreLYESLLQ 372
PRK09039 PRK09039
peptidoglycan -binding protein;
320-460 1.24e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDiAQKSKAEAESLYQSKYEELQITAGRHGD---SVRNSKI 396
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750 397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGenalKDAKNKLND----LEDALQQAKEDLAR 460
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
180-492 1.43e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 381.19  E-value: 1.43e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  340 DNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395750  420 SNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
145-176 2.13e-19

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 85.48  E-value: 2.13e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119395750  145 PVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 176
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-487 1.83e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   235 INNLRRRVDQLKSDQSRLDSELknmqdmvedyrNKYEDEinkRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDF 314
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKAL-----------AELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   315 LTALY---QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDI---AQKSKAEAESLyQSKYEELQITAGRHG 388
Cdd:TIGR02168  745 LEERIaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeeLKALREALDEL-RAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   389 DSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKdaknKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEEL 899

                          250
                   ....*....|....*....
gi 119395750   469 MNTKLALDLEIATYRTLLE 487
Cdd:TIGR02168  900 SEELRELESKRSELRRELE 918
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-468 2.16e-08

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: 57.39  E-value: 2.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   179 REREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQvDTSTRTHNLEpYFESFINNLRRRVDQLKSDQSRLDSELKN 258
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   259 MQDMVEDYRNK---YEDEINKRTNAENEfvtIKKDvdgaymtkvDLQAKLDNLQQEIDFLtalyQAELSQMQTQISETNV 335
Cdd:TIGR02169  756 VKSELKELEARieeLEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   336 ILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLyqskyEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNV 415
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 119395750   416 KKQISNLQQSISDAEQrgenALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02169  895 EAQLRELERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-492 3.00e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   237 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLt 316
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL- 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   317 alyQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDI---AQKSKAEAESLyQSKYEELQITAGRHGDSVRN 393
Cdd:TIGR02168  753 ---SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeeLKALREALDEL-RAELTLLNEEAANLRERLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   394 SKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLND----------LEDALQQAKEDLARLLR 463
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealalLRSELEELSEELRELES 908

                          250       260
                   ....*....|....*....|....*....
gi 119395750   464 DYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVR 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-492 1.17e-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: 55.06  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   241 RVDQLKSDQSRLDSELKNMQDMVEDYrnkyEDEINKrtnAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLT---A 317
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEEL----TAELQE---LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   318 LYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLyQSKYEELQitagrhgdsvrNSKIE 397
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELEAELE-----------ELESR 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   398 ISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenalkdaknkLNDLEDALQQAKEDLARLLRDYQElmNTKLALDL 477
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-----------LERLEDRRERLQQEIEELLKKLEE--AELKELQA 440

                          250
                   ....*....|....*
gi 119395750   478 EIATYRTLLEGEESR 492
Cdd:TIGR02168  441 ELEELEEELEELQEE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 178-468 1.74e-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: 54.68  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   178 SREREqIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQV---------DTSTRTHNLEPYFEsfinNLRRRVDQLKSD 248
Cdd:TIGR02168  674 ERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleELSRQISALRKDLA----RLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   249 QSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQA---ELSQ 325
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   326 MQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQ---KSKAEAESLYQSKyEELQITAGRHGDSVRNSKIEISELN 402
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELE 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119395750   403 RVIQRLRSEIDNVKKQISNLQQSISDAEQRGEN-----------ALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
493-512 3.08e-07

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 49.97  E-value: 3.08e-07
                          10        20
                  ....*....|....*....|
gi 119395750  493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
232-487 9.41e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 9.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 232 ESFIN-NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQ 310
Cdd:COG3206  159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 311 EIDFLtalyQAELSQMQTQISETNVILSMDNNrsldlDSIIAEVKAQYEDIAQKsKAEAESLYQSKYEElqitagrhgds 390
Cdd:COG3206  234 ELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAE-LAELSARYTPNHPD----------- 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 391 vrnskieiselnrvIQRLRSEIDNVKKQIsnlQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmn 470
Cdd:COG3206  293 --------------VIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL-- 353

                        250
                 ....*....|....*....
gi 119395750 471 TKLALDLEIA--TYRTLLE 487
Cdd:COG3206  354 RRLEREVEVAreLYESLLQ 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-487 1.10e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 240 RRVDQLKSDQSRLDSELKNMQDmvEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDfltaLY 319
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----EA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESL---------YQSKYEELQITAGRHGDS 390
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeeleeeleeAEEELEEAEAELAEAEEA 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 391 VRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMN 470
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250
                 ....*....|....*..
gi 119395750 471 TKLALDLEIATYRTLLE 487
Cdd:COG1196  447 AAEEEAELEEEEEALLE 463
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-471 2.54e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   168 EIDPEIQKVKsREREQIKSLNNQFASFIDKVRfleQQNQVLQT-KWELLQQVDTSTRTHNLEPYFESF-INNLRRRVDQL 245
Cdd:TIGR02169  167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR---QQLERLRReREKAERYQALLKEKREYEGYELLKeKEALERQKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   246 KSDQSRLDSELKNMQDMVEDYRNKYE------DEINKRTNA--ENEFVTIKKDVDgaymtkvDLQAKLDNLQQEIDFlta 317
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSIAE--- 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   318 lYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEV---KAQYEDIAQKSKAEAESLyQSKYEELQITAGRHGDSVRNS 394
Cdd:TIGR02169  313 -KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDL-RAELEEVDKEFAETRDELKDY 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   395 KIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEqrgeNALKDAKNKLNDLEDA--------------LQQAKEDLAR 460
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEkedkaleikkqewkLEQLAADLSK 466

                          330
                   ....*....|.
gi 119395750   461 LLRDYQELMNT 471
Cdd:TIGR02169  467 YEQELYDLKEE 477
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 232-460 4.75e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.44  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 232 ESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrtnAENEFVTIKKDVDgaymtkvDLQAKLDNLQQE 311
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEID-------KLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 312 IDFLTALYQAELSQMQTQ---ISETNVILSMDN-----NRSLDLDSIIAEVKAQYEDI--AQKSKAEAESLYQSKYEELQ 381
Cdd:COG3883   81 IEERREELGERARALYRSggsVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119395750 382 ITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLAR 460
Cdd:COG3883  161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
PRK09039 PRK09039
peptidoglycan -binding protein;
320-460 1.24e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDiAQKSKAEAESLYQSKYEELQITAGRHGD---SVRNSKI 396
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750 397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGenalKDAKNKLND----LEDALQQAKEDLAR 460
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
46 PHA02562
endonuclease subunit; Provisional
 196-482 2.12e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.70  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 196 DKVRFLEQQNQVLQTKWELL-QQVDTSTRthnlepyfesFINNLRRRVDQLKSD-QSRLDSELKNMQDmvedyrnkYEDE 273
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYNK----------NIEEQRKKNGENIARkQNKYDELVEEAKT--------IKAE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 274 INKRTNAENEFVTIKKDVDGAY----MTKVDLQAKLDNLQQEIDFLTAlyQAELSQMQTQISETNVILsmdnnrsldlds 349
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRI------------ 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 350 iiaevkaqyEDIAQKSKAeaeslYQSKYEELQItagrHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDA 429
Cdd:PHA02562 302 ---------TKIKDKLKE-----LQHSLEKLDT----AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119395750 430 EQRGENALKDAKNKlndledalqqaKEDLARLLRDYQELMNTKLALDLEIATY 482
Cdd:PHA02562 364 KAAIEELQAEFVDN-----------AEELAKLQDELDKIVKTKSELVKEKYHR 405
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 172-454 2.16e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.51  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  172 EIQKVKSREREQIKSLNNQFAsfiDKVRFLEQQNQVLQTKWELLQqVDTSTRthnlepyfESFINNLRRRVDQLKSDQSR 251
Cdd:pfam10174 447 EKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQ-PELTEK--------ESSLIDLKEHASSLASSGLK 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  252 LDSELKNMQDMVEDYR---NKYEDEINKRTNAENefvtikkdvdgAYMTKVDLQAKLDNLQQEIdfltALYQAELSQMQT 328
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKeecSKLENQLKKAHNAEE-----------AVRTNPEINDRIRLLEQEV----ARYKEESGKAQA 579

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  329 QISETNVILSMDNNRSLDLDSIIAE--------VKAQYEDIAQKSKAEAEsLYQSKYEELQITAGRHGDSVRNS-KIEIS 399
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDKKIAElesltlrqMKEQNKKVANIKHGQQE-MKKKGAQLLEEARRREDNLADNSqQLQLE 658

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119395750  400 ELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQA 454
Cdd:pfam10174 659 ELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEA 713
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 243-468 3.29e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 243 DQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLtalyQAE 322
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 323 LSQMQTQISETNVILSMDNNRSldldsiIAEVKAQYEDIAQKSKAEAesLYQSKYEELQitagRHGDSVRNSKIEISELN 402
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALR 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119395750 403 RVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 300-492 3.74e-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: 46.97  E-value: 3.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   300 DLQAKLDNLQQeidfltALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIaQKSKAEAESLYQSKYEE 379
Cdd:TIGR02168  217 ELKAELRELEL------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   380 LQitagrhgdsvrNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLA 459
Cdd:TIGR02168  290 LY-----------ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK----LDELAEELAELEEKLEELKEELE 354

                          170       180       190
                   ....*....|....*....|....*....|...
gi 119395750   460 RLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSK 387
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-453 4.04e-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: 46.97  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   153 QEVTINQSLLQPLNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQ--VDTSTRTHNLEPY 230
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESklDELAEELAELEEK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   231 FESfinnLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQ 310
Cdd:TIGR02168  346 LEE----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   311 EI-DFLTALYQAELSQMQTQISETNVILsmdnnrsLDLDSIIAEVKAQYEdIAQKSKAEAESLYQSKYEELqitagrhgd 389
Cdd:TIGR02168  422 EIeELLKKLEEAELKELQAELEELEEEL-------EELQEELERLEEALE-ELREELEEAEQALDAAEREL--------- 484

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395750   390 svrnskieiselnrviQRLRSEIDNVKKQISNLQQsisdaEQRGENALKDAKNKLNDLEDALQQ 453
Cdd:TIGR02168  485 ----------------AQLQARLDSLERLQENLEG-----FSEGVKALLKNQSGLSGILGVLSE 527
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-487 8.50e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 165 LNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVdtSTRTHNLEPYFESfINNLRRRVDQ 244
Cdd:PRK03918 174 IKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL--EKEVKELEELKEE-IEELEKELES 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 245 LKSDQSRLDSELKNmqdmVEDYRNKYEDEINKRTNAENEFVTIKKDVDgAYMTKVDLQAKLDNLQQEIDFLTALYQAELS 324
Cdd:PRK03918 250 LEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 325 QMQTQISEtnviLSMDNNRSLDLDSIIAEVKAQYEDIaqKSKAEAESLYQSKYEELQ-ITAGRHGDSVRNSKIEISELNR 403
Cdd:PRK03918 325 GIEERIKE----LEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEK 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 404 VIQRLRSEIDNVKKQISNLQQSISDAEqRGENALKDAKNK-----------------------LNDLEDALQQAKEDLAR 460
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELK-KAIEELKKAKGKcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERK 477

                        330       340
                 ....*....|....*....|....*..
gi 119395750 461 LLRDYQELmNTKLALDLEIATYRTLLE 487
Cdd:PRK03918 478 LRKELREL-EKVLKKESELIKLKELAE 503
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 201-480 8.66e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 8.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   201 LEQQNQVLQTKWELLQQVDTstrthnLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKyeDEINKRTNA 280
Cdd:pfam15921  446 MERQMAAIQGKNESLEKVSS------LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   281 EnefvtIKKdvdgaYMTKVDLQ-AKLDNLQQEIDFLTALyQAELSQMQTQISETnvilsmdnnrsldlDSIIAEVKAQYE 359
Cdd:pfam15921  518 E-----ITK-----LRSRVDLKlQELQHLKNEGDHLRNV-QTECEALKLQMAEK--------------DKVIEILRQQIE 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   360 DIAQKSKAEAESLYQSKYEELQITagrhgDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQ--------------QS 425
Cdd:pfam15921  573 NMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRA 647

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750   426 ISDAEQRGENALKDAKNKLNDLeDALQQAKEDLARLLRDYQELMNT---KLALDLEIA 480
Cdd:pfam15921  648 VKDIKQERDQLLNEVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETttnKLKMQLKSA 704
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 343-493 1.21e-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: 45.43  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   343 RSLDLDSIIAEVKAQYEDIAQKSKAEAEslYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNL 422
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395750   423 QQSISDAEQRGENALKDAKNKLNDLEDALQQ---AKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRM 493
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 397-471 1.25e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750 397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQR---GENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNT 471
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
PRK01156 PRK01156
chromosome segregation protein; Provisional
 168-490 1.29e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 45.28  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 168 EIDPEIQKVKSRE-REQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQ----------QVDTSTRTHNLEPYFESfIN 236
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgtTLGEEKSNHIINHYNEK-KS 479

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 237 NLRRRVDQLKSDQSRLDSELKNMQDMvEDYRNKyeDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLT 316
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKR-KEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 317 ALYQAELSQMQTQISETNVILS---MDNNRSL---------DLDSIIAEVKAQYEDIaqksKAEAESLYQSKYEELqita 384
Cdd:PRK01156 557 SLKLEDLDSKRTSWLNALAVISlidIETNRSRsneikkqlnDLESRLQEIEIGFPDD----KSYIDKSIREIENEA---- 628

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 385 grhgDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLqQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRD 464
Cdd:PRK01156 629 ----NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703

                        330       340
                 ....*....|....*....|....*.
gi 119395750 465 YQELMNTKLALDLEIATYRTLLEGEE 490
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMK 729
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 232-487 1.37e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  232 ESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQE 311
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  312 IDFLTALYQ------AELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLyQSKYEELQitag 385
Cdd:TIGR04523 203 LSNLKKKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL-SEKQKELE---- 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  386 rhgdsvrNSKIEISELNRVIQRLRSEIDNVKKQ-ISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRD 464
Cdd:TIGR04523 278 -------QNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350

                         250       260
                  ....*....|....*....|...
gi 119395750  465 YQELMNTKLALDLEIATYRTLLE 487
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIE 373
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-471 1.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  300 DLQAKLDNLQQEIDFLTALY---QAELSQMQTQISETNVILSMDNNRsLDLDSI---IAEVKAQYEDIaQKSKAEAESLy 373
Cdd:COG4913   614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERL-DASSDDLAAL- 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  374 QSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSIS-----DAEQRGENALKDA--KNKLND 446
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAveRELREN 770

                         170       180
                  ....*....|....*....|....*
gi 119395750  447 LEDALQQAKEDLARLLRDYQELMNT 471
Cdd:COG4913   771 LEERIDALRARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 362-466 1.86e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 362 AQKSKAEAEslyQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAK 441
Cdd:COG4942   17 AQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89

                         90       100
                 ....*....|....*....|....*
gi 119395750 442 NKLNDLEDALQQAKEDLARLLRDYQ 466
Cdd:COG4942   90 KEIAELRAELEAQKEELAELLRALY 114
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 237-461 2.09e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   237 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVT-IKKDVDGAYMTKV--------DLQAKLDN 307
Cdd:pfam12128  654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeQKEQKREARTEKQaywqvvegALDAQLAL 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   308 LQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKsKAEAESLYQSKYEELQITAGRH 387
Cdd:pfam12128  734 LKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYFDWYQETWLQRRPRL 812

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395750   388 GDSVRNSKIEISELNRVIQRLRSEidnVKKQISNLqqsisdaeQRGENALKDAKNKLNDLEDALQQAKEDLARL 461
Cdd:pfam12128  813 ATQLSNIERAISELQQQLARLIAD---TKLRRAKL--------EMERKASEKQQVRLSENLRGLRCEMSKLATL 875
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-446 2.24e-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: 44.66  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   153 QEVTINQSLLQPLNVEIDPEIQKVKSRErEQIKSLNNQFASFIDkvRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFE 232
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   233 SFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDgaymtkvDLQAKLDNLQQEI 312
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-------ELSEELRELESKR 910

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   313 DFLTALYQA---ELSQMQTQISETNVilsmdnnrslDLDSIIAEVKAQYEDIAQkskaEAESLYQSKYEELQiTAGRHGD 389
Cdd:TIGR02168  911 SELRRELEElreKLAQLELRLEGLEV----------RIDNLQERLSEEYSLTLE----EAEALENKIEDDEE-EARRRLK 975

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750   390 SVRNSKIEISELN--------RVIQR---LRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLND 446
Cdd:TIGR02168  976 RLENKIKELGPVNlaaieeyeELKERydfLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNE 1043
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 347-492 3.34e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 347 LDSIIAEVKAQYEDI-AQKSKAEAE-SLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQ 424
Cdd:COG1196  244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750 425 SISDAEQRGENA----------LKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:COG1196  324 ELAELEEELEELeeeleeleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 389-480 6.35e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 389 DSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90
                 ....*....|..
gi 119395750 469 MNTKLALDLEIA 480
Cdd:COG4942   96 RAELEAQKEELA 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-493 8.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 8.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  302 QAKLDNLQQEIDFLtalyQAELSQMQTQISETNVILSmDNNRSLDLDSIIAEVKAQYEDIAQkskAEAEslYQSKYEELq 381
Cdd:COG4913   609 RAKLAALEAELAEL----EEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVAS---AERE--IAELEAEL- 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  382 itagrhgDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDL-AR 460
Cdd:COG4913   678 -------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrAL 750

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 119395750  461 LLRDYQELMNTKL------ALDLEIATYRTLLEGEESRM 493
Cdd:COG4913   751 LEERFAAALGDAVerelreNLEERIDALRARLNRAEEEL 789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 347-492 1.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 347 LDSIIAEVKAQYEDIA-QKSKAE------AE------SLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEID 413
Cdd:COG1196  191 LEDILGELERQLEPLErQAEKAEryrelkEElkeleaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 414 NVKKQISNLQQSISDA---EQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEE 490
Cdd:COG1196  271 ELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350


                 ..
gi 119395750 491 SR 492
Cdd:COG1196  351 EE 352
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 346-492 1.41e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 346 DLDSIIAEVKAQYEDI-AQKSKAEAE-SLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVK--KQISN 421
Cdd:COG1579   14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395750 422 LQQSISDAEQR---GENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmntKLALDLEIATYRTLLEGEESR 492
Cdd:COG1579   94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAE 164
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 182-479 2.64e-03

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: 40.77  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  182 EQIKSLNNQFASFIDKVRFLEQQNQVLQTKWEllqqvDTSTRTHNLEPY---FESFINNLRRRVDQLKSDQSRLDSELKN 258
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-----DLKKQKEELENElnlLEKEKLNIQKNIDKIKNKLLKLELLLSN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  259 MQDMVEDYRnKYEDEINkrtNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQ---AELSQMQTQISETNV 335
Cdd:TIGR04523 206 LKKKIQKNK-SLESQIS---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNkikKQLSEKQKELEQNNK 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  336 ILSMDNNRSLDLDSIIAEVKAQYE-DIAQKSKAEAESLyQSKYEELQitagrhgDSVRNSKIEISELNRVIQRLRSEIDN 414
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqDWNKELKSELKNQ-EKKLEEIQ-------NQISQNNKIISQLNEQISQLKKELTN 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750  415 V----------------------------KKQISNLQQSISDAEQRGENALKDAKNKlndlEDALQQAKEDLARLLRDYQ 466
Cdd:TIGR04523 354 SesensekqreleekqneieklkkenqsyKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEKELLEKEIE 429

                         330
                  ....*....|...
gi 119395750  467 ELMNTKLALDLEI 479
Cdd:TIGR04523 430 RLKETIIKNNSEI 442
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-468 2.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 172 EIQKVKSREREQIKSLNNQFASFIDKVRFLEQqnqvLQTKWELLQQvdtstRTHNLEPYFESFiNNLRRRVDQLKSDQSR 251
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEK-----RLEELEERHELY-EEAKAKKEELERLKKR 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 252 LD----SELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEID-----FLTALYQAE 322
Cdd:PRK03918 381 LTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkELLEEYTAE 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 323 LSQMQTQISETNVILSMDNNRSLDLDSIIAEVK--AQYEDIAQKSKAEAESLYQSKYEELqitagrhgdsvrnskieiSE 400
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEEL------------------EK 522

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119395750 401 LNRVIQRLRSEIDNVKKQISNLQQSIsdaeqrgeNALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
351-469 3.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750 351 IAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNskiEISELNRVIQRLRSEIDNVKKQISNLQQSISDAE 430
Cdd:COG4717  390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLE 466

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119395750 431 QRGEnalkdaknkLNDLEDALQQAKEDLARLLRDYQELM 469
Cdd:COG4717  467 EDGE---------LAELLQELEELKAELRELAEEWAALK 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 397-487 3.54e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALD 476
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRK----IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|.
gi 119395750   477 LEIATYRTLLE 487
Cdd:TIGR02169  758 SELKELEARIE 768
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 235-468 4.12e-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: 40.49  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   235 INNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGA--YMTKV--DLQAK---LDN 307
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTkeMLRKVveELTAKkmtLES 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   308 LQQEIDFLTALYQ----------AELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAeAESLYQsKY 377
Cdd:pfam15921  494 SERTVSDLTASLQekeraieatnAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV-IEILRQ-QI 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395750   378 EELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVK-------KQISNLQQSISDAE----------QRGENALKDA 440
Cdd:pfam15921  572 ENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLElekvklvnagSERLRAVKDI 651

                          250       260
                   ....*....|....*....|....*...
gi 119395750   441 KNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:pfam15921  652 KQERDQLLNEVKTSRNELNSLSEDYEVL 679
 
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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