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Conserved domains on  [gi|7331218|gb|AAF60327|]
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keratin 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 8.64e-127

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 376.57  E-value: 8.64e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    340 DNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7331218    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 7331218    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 7331218    493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
180-492 8.64e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 376.57  E-value: 8.64e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    340 DNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7331218    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 7331218    145 PVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 176
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-468 7.30e-09

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: 58.93  E-value: 7.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     179 REREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQvDTSTRTHNLEpYFESFINNLRRRVDQLKSDQSRLDSELKN 258
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     259 MQDMVEDYRNK---YEDEINKRTNAENEfvtIKKDvdgaymtkvDLQAKLDNLQQEIDFLtalyQAELSQMQTQISETNV 335
Cdd:TIGR02169  756 VKSELKELEARieeLEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     336 ILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLyqskyEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNV 415
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 7331218     416 KKQISNLQQSISDAEQrgenALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02169  895 EAQLRELERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
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 7331218    493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-487 5.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  240 RRVDQLKSDQSRLDSELKNMQDmvEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDfltaLY 319
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----EA 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESL---------YQSKYEELQITAGRHGDS 390
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeeleeeleeAEEELEEAEAELAEAEEA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  391 VRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMN 470
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                       250
                ....*....|....*..
gi 7331218  471 TKLALDLEIATYRTLLE 487
Cdd:COG1196 447 AAEEEAELEEEEEALLE 463
46 PHA02562
endonuclease subunit; Provisional
 196-482 1.74e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.70  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   196 DKVRFLEQQNQVLQTKWELL-QQVDTSTRthnlepyfesFINNLRRRVDQLKSD-QSRLDSELKNMQDmvedyrnkYEDE 273
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYNK----------NIEEQRKKNGENIARkQNKYDELVEEAKT--------IKAE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   274 INKRTNAENEFVTIKKDVDGAY----MTKVDLQAKLDNLQQEIDFLTAlyQAELSQMQTQISETnvilsmdnnrsldlDS 349
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEG--------------PD 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   350 IIAEVKAQNEDIAQKSKAEAEslyqsKYEELQitagrhgdsvrNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDA 429
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDT-----AIDELE-----------EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7331218   430 EQRGENALKDAKNKlndledalqqaKEDLARLLRDYQELMNTKLALDLEIATY 482
Cdd:PHA02562 364 KAAIEELQAEFVDN-----------AEELAKLQDELDKIVKTKSELVKEKYHR 405
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
180-492 8.64e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 376.57  E-value: 8.64e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    180 EREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRThNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNM 259
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    260 QDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSM 339
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    340 DNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQI 419
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7331218    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 7331218    145 PVCPPGGIQEVTINQSLLQPLNVEIDPEIQKV 176
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-468 7.30e-09

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: 58.93  E-value: 7.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     179 REREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQvDTSTRTHNLEpYFESFINNLRRRVDQLKSDQSRLDSELKN 258
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIEN 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     259 MQDMVEDYRNK---YEDEINKRTNAENEfvtIKKDvdgaymtkvDLQAKLDNLQQEIDFLtalyQAELSQMQTQISETNV 335
Cdd:TIGR02169  756 VKSELKELEARieeLEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKL----EEEVSRIEARLREIEQ 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     336 ILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLyqskyEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNV 415
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 7331218     416 KKQISNLQQSISDAEQrgenALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02169  895 EAQLRELERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-487 2.06e-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: 2.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     235 INNLRRRVDQLKSDQSRLDSELknmqdmvedyrNKYEDEinkRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDF 314
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKAL-----------AELRKE---LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     315 LTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQ------KSKAEAESLyQSKYEELQITAGRHG 388
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkALREALDEL-RAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     389 DSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKdaknKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES----ELEALLNERASLEEALALLRSELEEL 899

                          250
                   ....*....|....*....
gi 7331218     469 MNTKLALDLEIATYRTLLE 487
Cdd:TIGR02168  900 SEELRELESKRSELRRELE 918
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-492 3.87e-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: 56.60  E-value: 3.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     237 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKyedeinkRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLT 316
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     317 ALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQ------KSKAEAESLyQSKYEELQITAGRHGDS 390
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkALREALDEL-RAELTLLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     391 VRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLND----------LEDALQQAKEDLAR 460
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleealalLRSELEELSEELRE 905

                          250       260       270
                   ....*....|....*....|....*....|..
gi 7331218     461 LLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVR 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 178-468 2.93e-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: 53.91  E-value: 2.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     178 SREREqIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQV---------DTSTRTHNLEPYFEsfinNLRRRVDQLKSD 248
Cdd:TIGR02168  674 ERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleELSRQISALRKDLA----RLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     249 QSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQA---ELSQ 325
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLES 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     326 MQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQ---KSKAEAESLYQSKyEELQITAGRHGDSVRNSKIEISELN 402
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELE 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7331218     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 7331218    493 MSGECAPNVSVSVSTSHTTI 512
Cdd:pfam16210   1 MSGECAPNVSVSVSTSHTSI 20
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-492 4.65e-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: 53.14  E-value: 4.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     241 RVDQLKSDQSRLDSELKNMQDMVEDYrnkyEDEINKrtnAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLT---A 317
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEEL----TAELQE---LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     318 LYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLyQSKYEELQitagrhgdsvrNSKIE 397
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELEAELE-----------ELESR 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     398 ISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenalkdaknkLNDLEDALQQAKEDLARLLRDYQElmNTKLALDL 477
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-----------LERLEDRRERLQQEIEELLKKLEE--AELKELQA 440

                          250
                   ....*....|....*
gi 7331218     478 EIATYRTLLEGEESR 492
Cdd:TIGR02168  441 ELEELEEELEELQEE 455
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-487 5.80e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  240 RRVDQLKSDQSRLDSELKNMQDmvEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDfltaLY 319
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----EA 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESL---------YQSKYEELQITAGRHGDS 390
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeeleeeleeAEEELEEAEAELAEAEEA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  391 VRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMN 470
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                       250
                ....*....|....*..
gi 7331218  471 TKLALDLEIATYRTLLE 487
Cdd:COG1196 447 AAEEEAELEEEEEALLE 463
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 172-454 3.34e-06

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: 50.21  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    172 EIQKVKSREREQIKSLNNQFAsfiDKVRFLEQQNQVLQTKWELLQqVDTSTRthnlepyfESFINNLRRRVDQLKSDQSR 251
Cdd:pfam10174 447 EKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQ-PELTEK--------ESSLIDLKEHASSLASSGLK 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    252 LDSELKNMQDMVEDYR---NKYEDEINKRTNAENefvtikkdvdgAYMTKVDLQAKLDNLQQEIdfltALYQAELSQMQT 328
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKeecSKLENQLKKAHNAEE-----------AVRTNPEINDRIRLLEQEV----ARYKEESGKAQA 579

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    329 QISETNVILSMDNNRSLDLDSIIAE--------VKAQNEDIAQKSKAEAEsLYQSKYEELQITAGRHGDSVRNS-KIEIS 399
Cdd:pfam10174 580 EVERLLGILREVENEKNDKDKKIAElesltlrqMKEQNKKVANIKHGQQE-MKKKGAQLLEEARRREDNLADNSqQLQLE 658

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 7331218    400 ELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQA 454
Cdd:pfam10174 659 ELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEA 713
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 280-480 4.16e-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: 4.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  280 AENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALY---QAELSQMQTQISETNVilsmdnnrslDLDSIIAEVKA 356
Cdd:COG3883  14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQA----------EIAEAEAEIEE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  357 QNEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNskieISELNRVIQRLRSEIDNV---KKQISNLQQSISDAEQRG 433
Cdd:COG3883  84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELkadKAELEAKKAELEAKLAEL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 7331218  434 ENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIA 480
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 232-460 4.66e-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: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  232 ESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrtnAENEFVTIKKDVDgaymtkvDLQAKLDNLQQE 311
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEID-------KLQAEIAEAEAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  312 IDFLTALYQAELSQMQTQ---ISETNVILSMDN-----NRSLDLDSII----AEVKAQNEDIAQKSKAEAEslYQSKYEE 379
Cdd:COG3883  81 IEERREELGERARALYRSggsVSYLDVLLGSESfsdflDRLSALSKIAdadaDLLEELKADKAELEAKKAE--LEAKLAE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  380 LQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLA 459
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238


                .
gi 7331218  460 R 460
Cdd:COG3883 239 A 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-471 5.07e-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: 50.07  E-value: 5.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     168 EIDPEIQKVKsREREQIKSLNNQFASFIDKVRfleQQNQVLQT-KWELLQQVDTSTRTHNLEPYFESF-INNLRRRVDQL 245
Cdd:TIGR02169  167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR---QQLERLRReREKAERYQALLKEKREYEGYELLKeKEALERQKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     246 KSDQSRLDSELKNMQDMVEDYRNKYE------DEINKRTNA--ENEFVTIKKDVDgaymtkvDLQAKLDNLQQEIDFlta 317
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSIAE--- 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     318 lYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNE---DIAQKSKAEAESLyQSKYEELQITAGRHGDSVRNS 394
Cdd:TIGR02169  313 -KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDkltEEYAELKEELEDL-RAELEEVDKEFAETRDELKDY 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     395 KIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEqrgeNALKDAKNKLNDLEDA--------------LQQAKEDLAR 460
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLN----AAIAGIEAKINELEEEkedkaleikkqewkLEQLAADLSK 466

                          330
                   ....*....|.
gi 7331218     461 LLRDYQELMNT 471
Cdd:TIGR02169  467 YEQELYDLKEE 477
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
232-487 8.49e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 8.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  232 ESFIN-NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDeinkrTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQ 310
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  311 EIDFLtalyQAELSQMQTQISETNVILSMDNNrsldlDSIIAEVKAQNEDIAQKsKAEAESLYQSKYEElqitagrhgds 390
Cdd:COG3206 234 ELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAE-LAELSARYTPNHPD----------- 292

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  391 vrnskieiselnrvIQRLRSEIDNVKKQIsnlQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmn 470
Cdd:COG3206 293 --------------VIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL-- 353

                       250
                ....*....|....*....
gi 7331218  471 TKLALDLEIA--TYRTLLE 487
Cdd:COG3206 354 RRLEREVEVAreLYESLLQ 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 243-468 1.20e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  243 DQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLtalyQAE 322
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  323 LSQMQTQISETNVILSMDNNRSldldsiIAEVKAQNEDIAQKSKAEAesLYQSKYEELQitagRHGDSVRNSKIEISELN 402
Cdd:COG4942  99 LEAQKEELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALR 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7331218  403 RVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
46 PHA02562
endonuclease subunit; Provisional
 196-482 1.74e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.70  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   196 DKVRFLEQQNQVLQTKWELL-QQVDTSTRthnlepyfesFINNLRRRVDQLKSD-QSRLDSELKNMQDmvedyrnkYEDE 273
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYNK----------NIEEQRKKNGENIARkQNKYDELVEEAKT--------IKAE 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   274 INKRTNAENEFVTIKKDVDGAY----MTKVDLQAKLDNLQQEIDFLTAlyQAELSQMQTQISETnvilsmdnnrsldlDS 349
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEG--------------PD 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   350 IIAEVKAQNEDIAQKSKAEAEslyqsKYEELQitagrhgdsvrNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDA 429
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDT-----AIDELE-----------EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7331218   430 EQRGENALKDAKNKlndledalqqaKEDLARLLRDYQELMNTKLALDLEIATY 482
Cdd:PHA02562 364 KAAIEELQAEFVDN-----------AEELAKLQDELDKIVKTKSELVKEKYHR 405
PRK09039 PRK09039
peptidoglycan -binding protein;
320-460 1.96e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.27  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   320 QAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDiAQKSKAEAESLYQSKYEELQITAGRHGD---SVRNSKI 396
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7331218   397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGenalKDAKNKLND----LEDALQQAKEDLAR 460
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 343-493 2.85e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     343 RSLDLDSIIAEVKAQNEDIAQKSKAEAEslYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNL 422
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7331218     423 QQSISDAEQRGENALKDAKNKLNDLEDALQQ---AKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRM 493
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-453 1.16e-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: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     153 QEVTINQSLLQPLNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQ--VDTSTRTHNLEPY 230
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESklDELAEELAELEEK 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     231 FESfinnLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQ 310
Cdd:TIGR02168  346 LEE----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     311 EI-DFLTALYQAELSQMQTQISETNVILsmdnnrsLDLDSIIAEVKAQNEdIAQKSKAEAESLYQSKYEELqitagrhgd 389
Cdd:TIGR02168  422 EIeELLKKLEEAELKELQAELEELEEEL-------EELQEELERLEEALE-ELREELEEAEQALDAAEREL--------- 484

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7331218     390 svrnskieiselnrviQRLRSEIDNVKKQISNLQQsisdaEQRGENALKDAKNKLNDLEDALQQ 453
Cdd:TIGR02168  485 ----------------AQLQARLDSLERLQENLEG-----FSEGVKALLKNQSGLSGILGVLSE 527
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 397-471 1.36e-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: 1.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7331218  397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQR---GENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNT 471
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 300-492 1.75e-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: 45.05  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     300 DLQAKLDNLQQeidfltALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIaQKSKAEAESLYQSKYEE 379
Cdd:TIGR02168  217 ELKAELRELEL------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     380 LQitagrhgdsvrNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLA 459
Cdd:TIGR02168  290 LY-----------ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK----LDELAEELAELEEKLEELKEELE 354

                          170       180       190
                   ....*....|....*....|....*....|...
gi 7331218     460 RLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSK 387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
300-471 1.89e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   300 DLQAKLDNLQQEIDFLTALY---QAELSQMQTQISETNVILSMDNNRsLDLDSIIAEVKAQNEDIAQ--KSKAEAESLyQ 374
Cdd:COG4913  614 ALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERldASSDDLAAL-E 691

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   375 SKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSIS-----DAEQRGENALKDA--KNKLNDL 447
Cdd:COG4913  692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAveRELRENL 771

                        170       180
                 ....*....|....*....|....
gi 7331218   448 EDALQQAKEDLARLLRDYQELMNT 471
Cdd:COG4913  772 EERIDALRARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 362-466 1.96e-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: 43.98  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  362 AQKSKAEAEslyQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAK 441
Cdd:COG4942  17 AQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELE 89

                        90       100
                ....*....|....*....|....*
gi 7331218  442 NKLNDLEDALQQAKEDLARLLRDYQ 466
Cdd:COG4942  90 KEIAELRAELEAQKEELAELLRALY 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 347-492 3.67e-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: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  347 LDSIIAEVKAQNEDI-AQKSKAEAE-SLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQ 424
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7331218  425 SISDAEQRGENA----------LKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESR 492
Cdd:COG1196 324 ELAELEEELEELeeeleeleeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
PRK01156 PRK01156
chromosome segregation protein; Provisional
 168-490 4.08e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   168 EIDPEIQKVKSRE-REQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQ----------QVDTSTRTHNLEPYFESfIN 236
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgtTLGEEKSNHIINHYNEK-KS 479

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   237 NLRRRVDQLKSDQSRLDSELKNMQDMvEDYRNKyeDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLT 316
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKR-KEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   317 ALYQAELSQMQTQISETNVILS---MDNNRSLDldsiiAEVKAQNEDIaQKSKAEAESLYQSKYEELQITAGRHGD---S 390
Cdd:PRK01156 557 SLKLEDLDSKRTSWLNALAVISlidIETNRSRS-----NEIKKQLNDL-ESRLQEIEIGFPDDKSYIDKSIREIENeanN 630

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   391 VRNSKIEISELNRVIQRLRSEIDNVKKQISNLqQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMN 470
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709

                        330       340
                 ....*....|....*....|
gi 7331218   471 TKLALDLEIATYRTLLEGEE 490
Cdd:PRK01156 710 RINELSDRINDINETLESMK 729
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 237-461 4.23e-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: 43.67  E-value: 4.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     237 NLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVT-IKKDVDGAYMTKV--------DLQAKLDN 307
Cdd:pfam12128  654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeQKEQKREARTEKQaywqvvegALDAQLAL 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     308 LQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQNEDIAQKsKAEAESLYQSKYEELQITAGRH 387
Cdd:pfam12128  734 LKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYFDWYQETWLQRRPRL 812

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7331218     388 GDSVRNSKIEISELNRVIQRLRSEidnVKKQISNLqqsisdaeQRGENALKDAKNKLNDLEDALQQAKEDLARL 461
Cdd:pfam12128  813 ATQLSNIERAISELQQQLARLIAD---TKLRRAKL--------EMERKASEKQQVRLSENLRGLRCEMSKLATL 875
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 201-468 4.34e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     201 LEQQNQVLQTKWELLQQVDTstrthnLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKyeDEINKRTNA 280
Cdd:pfam15921  446 MERQMAAIQGKNESLEKVSS------LTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     281 EnefvtIKKdvdgaYMTKVDLQ-AKLDNLQQEIDFLTALyQAELSQMQTQISETnvilsmdnnrsldlDSIIAEVKAQNE 359
Cdd:pfam15921  518 E-----ITK-----LRSRVDLKlQELQHLKNEGDHLRNV-QTECEALKLQMAEK--------------DKVIEILRQQIE 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     360 DIAQKSKAEAESLYQSKYEELQITagrhgDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQS---ISDAEQRGENA 436
Cdd:pfam15921  573 NMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvkLVNAGSERLRA 647

                          250       260       270
                   ....*....|....*....|....*....|..
gi 7331218     437 LKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:pfam15921  648 VKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-487 5.72e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   165 LNVEIDpEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVdtSTRTHNLEPYFESfINNLRRRVDQ 244
Cdd:PRK03918 174 IKRRIE-RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKL--EKEVKELEELKEE-IEELEKELES 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   245 LKSDQSRLDSELKNmqdmVEDYRNKYEDEINKRTNAENEFVTIKKDVDgAYMTKVDLQAKLDNLQQEIDFLTALYQAELS 324
Cdd:PRK03918 250 LEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   325 QMQTQISEtnviLSMDNNRSLDLDSIIAEVKAQNEDIaqKSKAEAESLYQSKYEELQ-ITAGRHGDSVRNSKIEISELNR 403
Cdd:PRK03918 325 GIEERIKE----LEEKEERLEELKKKLKELEKRLEEL--EERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEK 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   404 VIQRLRSEIDNVKKQISNLQQSISDAEqRGENALKDAKNK-----------------------LNDLEDALQQAKEDLAR 460
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELK-KAIEELKKAKGKcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERK 477

                        330       340
                 ....*....|....*....|....*..
gi 7331218   461 LLRDYQELmNTKLALDLEIATYRTLLE 487
Cdd:PRK03918 478 LRKELREL-EKVLKKESELIKLKELAE 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 389-480 6.58e-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: 6.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  389 DSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95

                        90
                ....*....|..
gi 7331218  469 MNTKLALDLEIA 480
Cdd:COG4942  96 RAELEAQKEELA 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-493 1.08e-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: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   302 QAKLDNLQQEIDFLtalyQAELSQMQTQISETNVILSmDNNRSLDLDSIIAEVKAQNEDIAQkskAEAEslYQSKYEELq 381
Cdd:COG4913  609 RAKLAALEAELAEL----EEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVAS---AERE--IAELEAEL- 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   382 itagrhgDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDL-AR 460
Cdd:COG4913  678 -------ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrAL 750

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 7331218   461 LLRDYQELMNTKL------ALDLEIATYRTLLEGEESRM 493
Cdd:COG4913  751 LEERFAAALGDAVerelreNLEERIDALRARLNRAEEEL 789
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 346-492 1.16e-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: 41.06  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  346 DLDSIIAEVKAQNEDI-AQKSKAEAE-SLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVK--KQISN 421
Cdd:COG1579  14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7331218  422 LQQSISDAEQR---GENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELmntKLALDLEIATYRTLLEGEESR 492
Cdd:COG1579  94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAE 164
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-468 1.99e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   172 EIQKVKSREREQIKSLNNQFASFIDKVRFLEQqnqvLQTKWELLQQvdtstRTHNLEPYFESFiNNLRRRVDQLKSDQSR 251
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEK-----RLEELEERHELY-EEAKAKKEELERLKKR 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   252 LD----SELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEID-----FLTALYQAE 322
Cdd:PRK03918 381 LTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkELLEEYTAE 460

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218   323 LSQMQTQISETNVILSMDNNRSLDLDSIIAEvkaQNEDIAQKSKAEAESLYQSKYEELQITagrhgdsvrnskiEISELN 402
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKK---ESELIKLKELAEQLKELEEKLKKYNLE-------------ELEKKA 524

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7331218   403 RVIQRLRSEIDNVKKQISNLQQSIsdaeqrgeNALKDAKNKLNDLEDALQQAKEDLARLLRDYQEL 468
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 153-446 2.48e-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: 41.20  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     153 QEVTINQSLLQPLNVEIDPEIQKVKSRErEQIKSLNNQFASFIDkvRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFE 232
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     233 SFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDgaymtkvDLQAKLDNLQQEI 312
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-------ELSEELRELESKR 910

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     313 DFLTALYQA---ELSQMQTQISETNV----ILSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAESLyQSKYEELqitag 385
Cdd:TIGR02168  911 SELRRELEElreKLAQLELRLEGLEVridnLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL-ENKIKEL----- 984

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7331218     386 rhGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLND 446
Cdd:TIGR02168  985 --GPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNE 1043
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 397-487 3.57e-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: 40.44  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218     397 EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRgenaLKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALD 476
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRK----IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|.
gi 7331218     477 LEIATYRTLLE 487
Cdd:TIGR02169  758 SELKELEARIE 768
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 301-472 6.79e-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: 38.75  E-value: 6.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  301 LQAKLDNLQQEIDFLtalyQAELSQMQTQISETNVilsmdnnrslDLDSIIAEVKAQNEDIAQKSKAEAeslyqsKYEEL 380
Cdd:COG1579  22 LEHRLKELPAELAEL----EDELAALEARLEAAKT----------ELEDLEKEIKRLELEIEEVEARIK------KYEEQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  381 QitagrhgDSVRNSKI-------------EISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGE---NALKDAKNKL 444
Cdd:COG1579  82 L-------GNVRNNKEyealqkeieslkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEekkAELDEELAEL 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 7331218  445 NDLEDALQQAKEDLA-----RLLRDYQELMNTK 472
Cdd:COG1579 155 EAELEELEAEREELAakippELLALYERIRKRK 187
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
 266-451 7.64e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 38.80  E-value: 7.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    266 YRNKYEDEINKRT--NAENEFVTIKKDVDGAYMTKVD---LQAKL-DNLQQEIDFLTALYQAELSQMQTQISE---TNVI 336
Cdd:pfam17060  66 YKESFSEMFNGLVgnNFKTVINKIFEDCDGIPASFISaleLKEDVkSSPRSEADSLGTPIKVDLLRNLKPQESpetPRRI 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218    337 LSMDNNRSLDLDSIIAEVKAQNEDIAQKSKAEAE-----SLYQSKYE----ELQITAGRHGDSVRNSKIEISELNRVIQR 407
Cdd:pfam17060 146 NRKYKSLELRVESMKDELEFKDETIMEKDRELTEltstiSKLKDKYDflsrEFEFYKQHHEHGGNNSIKTATKHEFIISE 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 7331218    408 LRSEIDNVKKQISNLQQSIsdaeQRGENALKDAKNKLNDLEDAL 451
Cdd:pfam17060 226 LKRKLQEQNRLIRILQEQI----QFDPGALHDNGPKNLVLNGAI 265
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
302-469 7.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 7.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  302 QAKLDNLQQEIDFLTALYQAELSQMQTQISEtnvilsmdnnRSLDLDSIIAEVKAQNEDIAQKSKAEAESLYQSKYEELq 381
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALE----------QAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL- 430

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7331218  382 itagrhgdsvrnsKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGEnalkdaknkLNDLEDALQQAKEDLARL 461
Cdd:COG4717 431 -------------EEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAELREL 488


                ....*...
gi 7331218  462 LRDYQELM 469
Cdd:COG4717 489 AEEWAALK 496
 
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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