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Conserved domains on  [gi|113195684|ref|NP_034799|]
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keratin, type II cytoskeletal 6B [Mus musculus]

Protein Classification

type II keratin( domain architecture ID 12177255)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
151-464 7.13e-156

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 447.83  E-value: 7.13e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  151 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRqNLEPMFEQYISNLRRQLDSIIGERGRLDSELRN 230
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  231 MQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRVIYEAELSQMQTHISDTSVVLS 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  311 MDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113195684  391 CANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-148 1.59e-27

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.20  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   15 GYSASSARVPGLNRSGFSSVSVCRSRGSGGSSAMCGGAGFGSRSLYGVGSSKRISIGGGSCGIGGGYGSRFGGSFGIGGG 94
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113195684   95 AGSGFGFGGGVGFGG----------------------GYGGAGFPVCPPGGIQEVTINQNLLTPLNVQIDPTIQRV 148
Cdd:pfam16208  81 GGFGGGGGGGFGGGGgfgggfggggyggggfggggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
151-464 7.13e-156

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 447.83  E-value: 7.13e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  151 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRqNLEPMFEQYISNLRRQLDSIIGERGRLDSELRN 230
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  231 MQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRVIYEAELSQMQTHISDTSVVLS 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  311 MDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113195684  391 CANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-148 1.59e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.20  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   15 GYSASSARVPGLNRSGFSSVSVCRSRGSGGSSAMCGGAGFGSRSLYGVGSSKRISIGGGSCGIGGGYGSRFGGSFGIGGG 94
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113195684   95 AGSGFGFGGGVGFGG----------------------GYGGAGFPVCPPGGIQEVTINQNLLTPLNVQIDPTIQRV 148
Cdd:pfam16208  81 GGFGGGGGGGFGGGGgfgggfggggyggggfggggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 148-446 2.99e-11

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: 66.62  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   148 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRQNLEpmFEQYISNLRRQLDSIIGERGRLDSE 227
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   228 LRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDvdaaymtKVELQAKADSLADEINFLRVIY---EAELSQMQTHISD 304
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALdelRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   305 TSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQR-----------------SRAEAESWYQtKYEELQVTAGRHGDDLRNTK 367
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDieslaaeieeleelieeLESELEALLN-ERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   368 QEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-----------GEMALKDARGKLEGLEDALQKAKQEMARLLKE 436
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980

                          330
                   ....*....|
gi 113195684   437 YQELMNVKLA 446
Cdd:TIGR02168  981 IKELGPVNLA 990
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-462 5.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 149 RTEE-REQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgtktvRQNLEPMFEQyISNLRRQLDSIIGERGRLDSE 227
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 228 LRNMQDTVEDYKSKYEdEINKRTKAENEfvtVKKDVDaAYMTKVELQAKADSLADEINFLRVIYEAELSQMQTHISDtsv 307
Cdd:PRK03918 261 IRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 308 vLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRS 382
Cdd:PRK03918 333 -LEEKEERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEK 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 383 EIDHVKKQCANLQAAIADAEQRGE------MALKDARGKL---------EGLEDALQKAKQEMARLLKEYQELMNVKLAL 447
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478

                        330
                 ....*....|....*
gi 113195684 448 DVEIATYRKLLEGEE 462
Cdd:PRK03918 479 RKELRELEKVLKKES 493
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 362-443 3.97e-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: 45.91  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 362 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLEDALQKAKQEMARLLKEYQ 438
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107


                 ....*
gi 113195684 439 ELMNV 443
Cdd:COG4942  108 ELLRA 112
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
151-464 7.13e-156

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 447.83  E-value: 7.13e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  151 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRqNLEPMFEQYISNLRRQLDSIIGERGRLDSELRN 230
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  231 MQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRVIYEAELSQMQTHISDTSVVLS 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  311 MDNNRSLDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQ 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113195684  391 CANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEECR 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
15-148 1.59e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 108.20  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   15 GYSASSARVPGLNRSGFSSVSVCRSRGSGGSSAMCGGAGFGSRSLYGVGSSKRISIGGGSCGIGGGYGSRFGGSFGIGGG 94
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113195684   95 AGSGFGFGGGVGFGG----------------------GYGGAGFPVCPPGGIQEVTINQNLLTPLNVQIDPTIQRV 148
Cdd:pfam16208  81 GGFGGGGGGGFGGGGgfgggfggggyggggfggggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 148-446 2.99e-11

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: 66.62  E-value: 2.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   148 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTVRQNLEpmFEQYISNLRRQLDSIIGERGRLDSE 227
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   228 LRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDvdaaymtKVELQAKADSLADEINFLRVIY---EAELSQMQTHISD 304
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALdelRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   305 TSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQR-----------------SRAEAESWYQtKYEELQVTAGRHGDDLRNTK 367
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDieslaaeieeleelieeLESELEALLN-ERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   368 QEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR-----------GEMALKDARGKLEGLEDALQKAKQEMARLLKE 436
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980

                          330
                   ....*....|
gi 113195684   437 YQELMNVKLA 446
Cdd:TIGR02168  981 IKELGPVNLA 990
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 145-440 4.24e-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: 59.70  E-value: 4.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   145 IQRVRTEEREQIKTLNNKFAsfiDKVRFLEQQNKVLDTKWALLQEQGTKTVRQnlepmfeqyISNLRRQLDSIIGERGRL 224
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRRERE---KAERYQALLKEKREYEGYELLKEKEALERQ---------KEAIERQLASLEEELEKL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   225 DSELRNMQDTVEDYKSKYEdEINKRTKA--ENEFVTVKKDVDaaymtkvELQAKADSLADEINFL----------RVIYE 292
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLE-ELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSIAEKereledaeerLAKLE 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   293 AELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIaqRSRAEAESwyqTKYEELQVTAGRHGDDLRNTKQEIAE 372
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD---KEFAETRDELKDYREKLEKLKREINE 403

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113195684   373 INRMIQRLRSEIDHVKKQCANLQAAIADAEQR----------GEMALKDARGKLEGLEDALQKAKQEMARLLKEYQEL 440
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-462 5.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 5.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 149 RTEE-REQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgtktvRQNLEPMFEQyISNLRRQLDSIIGERGRLDSE 227
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 228 LRNMQDTVEDYKSKYEdEINKRTKAENEfvtVKKDVDaAYMTKVELQAKADSLADEINFLRVIYEAELSQMQTHISDtsv 307
Cdd:PRK03918 261 IRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--- 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 308 vLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAeaeswyqtkYEELQVTAGRhgddLRNTKQEIA-----EINRMIQRLRS 382
Cdd:PRK03918 333 -LEEKEERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKKEE----LERLKKRLTgltpeKLEKELEELEK 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 383 EIDHVKKQCANLQAAIADAEQRGE------MALKDARGKL---------EGLEDALQKAKQEMARLLKEYQELMNVKLAL 447
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478

                        330
                 ....*....|....*
gi 113195684 448 DVEIATYRKLLEGEE 462
Cdd:PRK03918 479 RKELRELEKVLKKES 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 210-459 5.60e-07

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: 52.76  E-value: 5.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   210 LRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRV 289
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   290 I---YEAELSQMQTHISdtSVVLSMDNNRSLDLDSIIAEVKAQYEDI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 365
Cdd:TIGR02169  759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   366 TKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKL 445
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906

                          250
                   ....*....|....
gi 113195684   446 ALDVEIATYRKLLE 459
Cdd:TIGR02169  907 ELEAQIEKKRKRLS 920
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 180-466 3.14e-06

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: 50.06  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   180 LDTKWALLQEQGTKTVRqnlepmFEQYISNLRR-QLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVT 258
Cdd:TIGR02168  198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   259 VKKDVDAAYMTKVELQAKADSLADEINFLRV---IYEAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQ 335
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQqkqILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   336 RSRAEAEswyqtKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemalkdargk 415
Cdd:TIGR02168  352 ELESLEA-----ELEELE-------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----------- 408

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 113195684   416 LEGLEDALQKAKQEMARLLKEYQElmNVKLALDVEIATYRKLLEGEECRLN 466
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELE 457
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
204-436 3.87e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 204 EQYISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEdeinkrtkaenEFVTVKKDVDAAYMTKVELQAKADSLADE 283
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREELAEE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 284 INFLRVIYEaELSQMQTHISDTSVVLSMDNN----RSLDLDSIIAEVKAQYEDI---AQRSRAEAESW------YQTKYE 350
Cdd:PRK02224 281 VRDLRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAE 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 351 ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALK---DARGKLEGLEDALQKAK 427
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTAR 439

                        250
                 ....*....|..
gi 113195684 428 ---QEMARLLKE 436
Cdd:PRK02224 440 ervEEAEALLEA 451
PRK09039 PRK09039
peptidoglycan -binding protein;
292-432 4.55e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 48.81  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 292 EAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 368
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113195684 369 EIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGemalKDARGKLEG----LEDALQKAKQEMAR 432
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 319-468 1.29e-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: 48.13  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   319 LDSIIAEVKAQYEDIAQRSRAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQA 396
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113195684   397 AIADAEQRGEMA---LKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 468
Cdd:TIGR02168  324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 193-460 1.77e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   193 KTVRQNLEpMFEQYISNLRRQLDSIIGERGRLDsELRNMQDTVEDYKskYEDEINKRTKAENEFVTVKKDVDAAYMTKVE 272
Cdd:TIGR02169  180 EEVEENIE-RLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   273 LQAKADSLADEINFLrviyEAELSQMQTHISDtsvvlsMDNNRSLDLDSIIAEVKAQyedIAQRSRAEAESwyqtkyeel 352
Cdd:TIGR02169  256 LTEEISELEKRLEEI----EQLLEELNKKIKD------LGEEEQLRVKEKIGELEAE---IASLERSIAEK--------- 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   353 qvtagrhgddlrntKQEIAEINRMIQRLRSEIDHVKKQCANLqaaiadaeqrgEMALKDARGKLEGLEDALQKAKQEMAR 432
Cdd:TIGR02169  314 --------------ERELEDAEERLAKLEAEIDKLLAEIEEL-----------EREIEEERKRRDKLTEEYAELKEELED 368

                          250       260
                   ....*....|....*....|....*...
gi 113195684   433 LLKEYQELMNVKLALDVEIATYRKLLEG 460
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLEK 396
46 PHA02562
endonuclease subunit; Provisional
 168-436 2.26e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.32  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 168 DKVRFLEQQNKVLDTKWALLQEQgtktvrqnLEpMFEQYISNLRRQLDSIIgergrldSELRNMQDTVEDYKSKYEDEIN 247
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ--------IK-TYNKNIEEQRKKNGENI-------ARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 248 KRTKAENEFVTVKKDVDAAY----MTKVELQAKADSLADEINFLRVIYEAElSQMQThISDTsvvlsmdnnrsldlDSII 323
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ-ISEG--------------PDRI 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 324 AEVKAQYEDIAQRSRAEaeswyQTKYEELQVTAGRHgDDLRNTKQE----IAEINRMIQRLRSEIDHVKKQCANLQAAIA 399
Cdd:PHA02562 302 TKIKDKLKELQHSLEKL-----DTAIDELEEIMDEF-NEQSKKLLElknkISTNKQSLITLVDKAKKVKAAIEELQAEFV 375

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 113195684 400 DAEqrgemalkdarGKLEGLEDALQKAKQEMARLLKE 436
Cdd:PHA02562 376 DNA-----------EELAKLQDELDKIVKTKSELVKE 401
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 146-433 2.80e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.09  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   146 QRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALL-------QEQGTKTVRQNLE-----PMFEQYISNLRRQ 213
Cdd:pfam01576  425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqlqdtQELLQEETRQKLNlstrlRQLEDERNSLQEQ 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   214 LDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLadeinflrviyEA 293
Cdd:pfam01576  505 LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-----------EK 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   294 ELSQMQTHISDTSVVLsmDNNRSL---------DLDSIIAEVK---AQYEDiaQRSRAEAESwyqTKYEELQVTAGRHGD 361
Cdd:pfam01576  574 TKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARALE 646

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113195684   362 DLRNTKQEIAEINRMIQ----RLRSEIDHVKKQCANLQAAIADAEQrgemALKDARGKLEGLEDALQKAKQEMARL 433
Cdd:pfam01576  647 EALEAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 204-461 3.21e-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: 47.04  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   204 EQYISNLRRQLDS---IIGERGRLDSELRnmqdtVEdyKSKYEDEINKRTKAENEFVTVKKDVDAAYMtkvELQAKADSL 280
Cdd:pfam15921  561 DKVIEILRQQIENmtqLVGQHGRTAGAMQ-----VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDL 630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   281 adeinflrviyeaELSQMQThISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAEA--ESWYQTKYEELQVTAGR 358
Cdd:pfam15921  631 -------------ELEKVKL-VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNK 696

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   359 HGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIadAEQRGEMalkDA-RGKLEGLEDALQKAKQEmARLLKEY 437
Cdd:pfam15921  697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI--TAKRGQI---DAlQSKIQFLEEAMTNANKE-KHFLKEE 770

                          250       260
                   ....*....|....*....|....
gi 113195684   438 QELMNVKLAldvEIATYRKLLEGE 461
Cdd:pfam15921  771 KNKLSQELS---TVATEKNKMAGE 791
PRK01156 PRK01156
chromosome segregation protein; Provisional
 141-462 3.69e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 46.82  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 141 IDPT-IQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQ------GTKTVRQNLEPMFEQY---ISNL 210
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYnekKSRL 481

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 211 RRQLDSIIGERGRLDSELRNmQDTVEDYKSKyeDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRVI 290
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVD-LKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 291 YEAELSQMQTHISDTSVVLS---MDNNRSLDldsiiAEVKAQYEDIAQRSRaEAESWYQTKYEELQVTAGRHGDD---LR 364
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISlidIETNRSRS-----NEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEannLN 632

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 365 NTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALkDARGKLEGLEDALQKAKQEMARLLKEYQELMNVK 444
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN-DIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711

                        330
                 ....*....|....*...
gi 113195684 445 LALDVEIATYRKLLEGEE 462
Cdd:PRK01156 712 NELSDRINDINETLESMK 729
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 362-443 3.97e-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: 45.91  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 362 DLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLEDALQKAKQEMARLLKEYQ 438
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107


                 ....*
gi 113195684 439 ELMNV 443
Cdd:COG4942  108 ELLRA 112
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 207-432 5.62e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 207 ISNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAymtKVELQAKADSLADeinF 286
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGE---R 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 287 LRVIYEAELSqmqthISDTSVVLSMDN-----NRSLDLDSII----AEVKAQYEDIAQRSRAEAEswYQTKYEELQVTAG 357
Cdd:COG3883   92 ARALYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIAdadaDLLEELKADKAELEAKKAE--LEAKLAELEALKA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113195684 358 RHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMAR 432
Cdd:COG3883  165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
204-479 8.21e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 204 EQYI-SNLRRQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDeinkrTKAENEFVTVKKDVDAAYMTKVELQAKADSLAD 282
Cdd:COG3206  159 EAYLeQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 283 EINFLrviyEAELSQMQTHISDTSVVLSMDNNrsldlDSIIAEVKAQYEDiAQRSRAEAESWYQTKYEElqvtagrhgdd 362
Cdd:COG3206  234 ELAEA----EARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-LEAELAELSARYTPNHPD----------- 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 363 lrntkqeiaeinrmIQRLRSEIDHVKKQcanLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMN 442
Cdd:COG3206  293 --------------VIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 113195684 443 VKLALDVEIATYRKLLEG-EECRLNgEGVGPVNISVVQ 479
Cdd:COG3206  356 LEREVEVARELYESLLQRlEEARLA-EALTVGNVRVID 392
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 361-440 8.50e-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: 45.14  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 361 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQEMARLLKEYQEL 440
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
314-456 1.20e-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: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  314 NRSLDLDSIIAEVKAQYEDIAQRsRAEAEswyqTKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCA 392
Cdd:COG4913   295 AELEELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 113195684  393 NLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG4913   370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
PLN02939 PLN02939
transferase, transferring glycosyl groups
 137-441 1.56e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.89  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 137 LNVQIDPTIQRVRTEEReQIKTLNNKfasfidKVRFLEQQNKVLDTKWALLQEqgtktvrqnlepmfeqyISNLRRQLdS 216
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEK-NILLLNQA------RLQALEDLEKILTEKEALQGK-----------------INILEMRL-S 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 217 IIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTvkkdvdAAYMTKVELQAKADSLADEINFLRviyeAELS 296
Cdd:PLN02939 181 ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVH------SLSKELDVLKEENMLLKDDIQFLK----AELI 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 297 QMQThiSDTSVVLsMDNNRSLdLDSIIAEVKAQY----EDIAQRSRAEAESWYQtKYEELQVTAGRhgddLRNTKQEIAE 372
Cdd:PLN02939 251 EVAE--TEERVFK-LEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWWE-KVENLQDLLDR----ATNQVEKAAL 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113195684 373 INRMIQRLRSEIDHVKkqcANLQAAIADAEQRGEMALkdARGKLEGLEDALQKAKQEMARLLKEYQELM 441
Cdd:PLN02939 322 VLDQNQDLRDKVDKLE---ASLKEANVSKFSSYKVEL--LQQKLKLLEERLQASDHEIHSYIQLYQESI 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
361-467 3.59e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  361 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANL----------------QAAIADAEQRGEmALKDARGKLEGLEDALQ 424
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 113195684  425 KAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 467
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 190-433 3.87e-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: 43.29  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   190 QGTKTVRQNLEPMFEQYiSNLRRQLDSIIGERGRLDSELRN---MQDTVEDYKSKYEDEINKRTKAENefvtvkKDVDAA 266
Cdd:pfam12128  646 TALKNARLDLRRLFDEK-QSEKDKKNKALAERKDSANERLNsleAQLKQLDKKHQAWLEEQKEQKREA------RTEKQA 718

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   267 YMTKVE--LQAKADSLADEINFLRVIYEAELSQMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRsRAEAESW 344
Cdd:pfam12128  719 YWQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRY 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   345 YQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEidhVKKQCANLqaaiadaeqrgEMALKDARGKLEGLEDALQ 424
Cdd:pfam12128  798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD---TKLRRAKL-----------EMERKASEKQQVRLSENLR 863


                   ....*....
gi 113195684   425 KAKQEMARL 433
Cdd:pfam12128  864 GLRCEMSKL 872
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
323-456 4.12e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 323 IAEVKAQYEDIAQRsRAEAESWYQTKYEELQVTAGRHgdDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 402
Cdd:COG4717  390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 113195684 403 QRGEmalkdargkLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG4717  467 EDGE---------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-442 4.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  272 ELQAKADSLADEINFLRVIYE---AELSQMQTHISDTSVVLSMDNNRsLDLDSI---IAEVKAQYEDI---------AQR 336
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEaleAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERLdassddlaaLEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  337 SRAEAESWYQTKYEELQVTAGRHGDdlrnTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKL 416
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                         170       180
                  ....*....|....*....|....*.
gi 113195684  417 EGLEDALQKAKQEMARLLKEYQELMN 442
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERAMR 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 323-453 6.84e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 323 IAEVKAQYEDIAQRSRAEAEswyqtKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAE 402
Cdd:COG1196  262 LAELEAELEELRLELEELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 113195684 403 QR---GEMALKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIAT 453
Cdd:COG1196  337 EEleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-440 9.47e-04

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: 9.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 319 LDSIIAEVKAQYEDI-AQRSRAEAEswyqtkYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAA 397
Cdd:COG1196  244 LEAELEELEAELEELeAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 113195684 398 IADAEQRgemaLKDARGKLEGLEDALQKAKQEMARLLKEYQEL 440
Cdd:COG1196  318 LEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEA 356
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-462 1.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 325 EVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQR 404
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 113195684 405 gemaLKDARGKLEGLEDALQKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEE 462
Cdd:COG1196  297 ----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 272-456 1.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 272 ELQAKADSLADEINFLrviyEAELSQMQTHISDTSVvlsmdnnrslDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEE 351
Cdd:COG3883   41 ALQAELEELNEEYNEL----QAELEALQAEIDKLQA----------EIAEAEAEIEERREELGERARALYRSGGSVSYLD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 352 LQVTAGRHGDDLRNtkqeIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDARGKLEGLEDALQKAKQE-- 429
Cdd:COG3883  107 VLLGSESFSDFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLA-ELEALKAELEAAKAELEAQQAEqe 181

                        170       180
                 ....*....|....*....|....*....
gi 113195684 430 --MARLLKEYQELMNVKLALDVEIATYRK 456
Cdd:COG3883  182 alLAQLSAEEAAAEAQLAELEAELAAAEA 210
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 347-468 1.89e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 347 TKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGE------MALKDARgKLEGLE 420
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlGNVRNNK-EYEALQ 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 113195684 421 DALQKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGE 468
Cdd:COG1579   96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 220-432 2.48e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 220 ERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDAAYMTKVELQAKADSLADEINFLRviyeAELSQMQ 299
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 300 THISDTSVVLSMDNNRS-----LDLDSIIAEVKAQ--YEDIAQRSRAEAESwYQTKYEELQVTAGRHGDDLRNTKQEIAE 372
Cdd:COG4942  104 EELAELLRALYRLGRQPplallLSPEDFLDAVRRLqyLKYLAPARREQAEE-LRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 373 INRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEmALKDARGKLEGLEDALQKAKQEMAR 432
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 361-470 3.84e-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: 40.05  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684   361 DDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQ-------RGEMALKD---ARGKLEGLEDALQKAKQEM 430
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiekEIEQLEQEeekLKERLEELEEDLSSLEQEI 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 113195684   431 ARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGV 470
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
286-462 4.43e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 286 FLRVIYEAELSQMQTHISDTSVVLSMDNNRSLD-LDSIIAEVKAQYEDIAQ---------RSRAEAESWYQTKYEEL--- 352
Cdd:COG4717   42 FIRAMLLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAElqeeleeleEELEELEAELEELREELekl 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 353 --QVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVK---KQCANLQAAIADAEQRGEMALKD----ARGKLEGLEDAL 423
Cdd:COG4717  122 ekLLQLLPLYQELEALEAELAELPERLEELEERLEELReleEELEELEAELAELQEELEELLEQlslaTEEELQDLAEEL 201

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 113195684 424 QKAKQEMARLLKEYQELMNVKLALDVEIATYRKLLEGEE 462
Cdd:COG4717  202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 212-440 4.58e-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: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 212 RQLDSIIGERGRLDSELRNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDVDaaymtkvELQAKADSladeinflrviY 291
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKK-----------Y 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 292 EAELSQMQthisdtsvvlsmdNNRslDLDSIIAEVkaqyeDIAQRSRAEAEswyqtkyeelqvtagrhgddlrntkQEIA 371
Cdd:COG1579   79 EEQLGNVR-------------NNK--EYEALQKEI-----ESLKRRISDLE-------------------------DEIL 113

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 372 EINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDARGKLEGLEDALQKAKQEM-ARLLKEYQEL 440
Cdd:COG1579  114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERI 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 377-462 5.06e-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: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 377 IQRLRSEIDHVKKQCANLQAAIADAEQR---GEMALKDARGKLEGLEDALQKAKQEMA---RLLKEYQE-LMNVK----- 444
Cdd:COG1579   12 LQELDSELDRLEHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEeveARIKKYEEqLGNVRnnkey 91

                         90
                 ....*....|....*...
gi 113195684 445 LALDVEIATYRKLLEGEE 462
Cdd:COG1579   92 EALQKEIESLKRRISDLE 109
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 144-448 5.70e-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: 39.62  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  144 TIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKwalLQEQgtktvrQNLEPMFEQYISNLRRQLDSIIGERGR 223
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQ------EKLNQQKDEQIKKLQQEKELLEKEIER 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  224 LDSElrnmqdtvedyKSKYEDEINKRTKAENEFVTVKKDVDAaymTKVELQAKADSLADEINFLrviyEAELSQMQTHIS 303
Cdd:TIGR04523 431 LKET-----------IIKNNSEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKI----KQNLEQKQKELK 492

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  304 DTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSR------AEAESWYQTKYEELQvtagrhGDDLRNTKQ----EIAEI 373
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklesekKEKESKISDLEDELN------KDDFELKKEnlekEIDEK 566

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  374 NRMIQRLRSEIDHVKKQCANLQAAIADAEQ-----RGEMALKDArgKLEGLEDALQKAKQEMARLLkeyQELMNVKLALD 448
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKekkdlIKEIEEKEK--KISSLEKELEKAKKENEKLS---SIIKNIKSKKN 641
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 126-451 6.77e-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: 39.23  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  126 EVTINQNLLTPLNVQIDPTIQRVRTEEREQIKTLNNKfasfidkvrfLEQQNKVLDTKWALLQEQGTKTVrqnlepmFEQ 205
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK----------LNIQKNIDKIKNKLLKLELLLSN-------LKK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  206 YISnLRRQLDSIIgergrldSELRNMQDTVEDYKSKYEDEINKRT----KAENEFVTVKKDVDAaymTKVELQAKADSLa 281
Cdd:TIGR04523 209 KIQ-KNKSLESQI-------SELKKQNNQLKDNIEKKQQEINEKTteisNTQTQLNQLKDEQNK---IKKQLSEKQKEL- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  282 DEINFLRVIYEAELSQMQTHISDTSVVLSMDNNRslDLDSIIAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGD 361
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  362 DLRNTK--QEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRgemaLKDARGKLEGLEDALQKAKQEMARLLKEYQE 439
Cdd:TIGR04523 355 ESENSEkqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK----IQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430

                         330
                  ....*....|..
gi 113195684  440 LMNVKLALDVEI 451
Cdd:TIGR04523 431 LKETIIKNNSEI 442
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 149-385 8.17e-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: 39.23  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  149 RTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQgTKTVRQNLEPMfEQYISNLRRQLDSIIGERGRLDSEL 228
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS-INKIKQNLEQK-QKELKSKEKELKKLNEEKKELEEKV 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  229 RNMQDTVEDYKSKYEDEINKRTKAENEFVTVKKDV--DAAYMTKVELQAKADSLADEINFLRVIYEA----------ELS 296
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSlkkkqeekqeLID 592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684  297 QMQTHISDTSVVLSMDNNRSLDLDSIIAEVKAQYEDIAQRSRAeaeswYQTKYEELQVTAGRHGDDLRNTKQEIAEINRM 376
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN-----IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667


                  ....*....
gi 113195684  377 IQRLRSEID 385
Cdd:TIGR04523 668 IKESKTKID 676
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
323-430 8.88e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113195684 323 IAEVKAQYEDIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQ-EIAEINRMIQRLRSEIDHVKKQCANLQAAIADA 401
Cdd:COG2268  246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325

                         90       100
                 ....*....|....*....|....*....
gi 113195684 402 EQRGEMALKDARGKLEGLEdALQKAKQEM 430
Cdd:COG2268  326 EAEAEAIRAKGLAEAEGKR-ALAEAWNKL 353
 
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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