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Conserved domains on  [gi|74315985|ref|NP_034797|]
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keratin, type II cuticular Hb6 [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;
105-416 4.07e-131

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 382.35  E-value: 4.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   105 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNMEPLFEGYIEALRREAECVEADSGRLAAELNHA 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   184 QESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDTSIVVKM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   264 DNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQN 343
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74315985   344 TKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQR 416
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
3-102 1.60e-14

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 70.84  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985     3 CGSYCGGRAFSCASACGPRPGrccisaapYRGIScyrGLSGGFGSQSVCGAfrsGSCGRSFGYRsGGICGPSPP--CITT 80
Cdd:pfam16208  70 GFGGGGGGGFGGGFGGGGGGG--------FGGGG---GFGGGFGGGGYGGG---GFGGGGFGGR-GGFGGPPCPpgGIQE 134

                          90       100
                  ....*....|....*....|..
gi 74315985    81 VSVNESLLTPLNLEIDPNAQCV 102
Cdd:pfam16208 135 VTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
105-416 4.07e-131

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 382.35  E-value: 4.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   105 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNMEPLFEGYIEALRREAECVEADSGRLAAELNHA 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   184 QESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDTSIVVKM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   264 DNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQN 343
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74315985   344 TKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQR 416
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
3-102 1.60e-14

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 70.84  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985     3 CGSYCGGRAFSCASACGPRPGrccisaapYRGIScyrGLSGGFGSQSVCGAfrsGSCGRSFGYRsGGICGPSPP--CITT 80
Cdd:pfam16208  70 GFGGGGGGGFGGGFGGGGGGG--------FGGGG---GFGGGFGGGGYGGG---GFGGGGFGGR-GGFGGPPCPpgGIQE 134

                          90       100
                  ....*....|....*....|..
gi 74315985    81 VSVNESLLTPLNLEIDPNAQCV 102
Cdd:pfam16208 135 VTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-389 2.81e-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: 2.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    155 FEGYI-----EALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSLRATA--------ENEFVALKKDVDCAYLR 221
Cdd:TIGR02169  223 YEGYEllkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    222 KSDLEANAEALTQETDFL---RRMYDEETRILHSHISDTSIVVKMDNSRDLNMDCVVAEIKAQYDDIasRSRAEAESwyr 298
Cdd:TIGR02169  303 IASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD--- 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    299 TKCEEIKATVIRHGETLRRTREEINELNRMI-------QRLTAEIENAKCQNTKLEAAVTQSeqqgEAALADARCKLAEL 371
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQ 453

                          250
                   ....*....|....*...
gi 74315985    372 EGALQKAKQDMACLLKEY 389
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQEL 471
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
315-417 8.11e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 8.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 315 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 391
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                        90       100
                ....*....|....*....|....*.
gi 74315985 392 VMNSKLGLDVEITTYRRLLEGEEQRL 417
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 155-340 2.17e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985  155 FEGYIEALRREAECVEADSGRLaaELNHAQESMEGYKKR----Y---EEEVslraTAENeFVALKKDVDCAYLRKsdLEA 227
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREV----KARK-YVEKNSDTLPDFLEH--AKE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985  228 NAEALTQETDFLRRMYdeetrilhsHISDTSIvvkmDNSRDLNMDcvVAEIKAQYDDIASRS----------RAEAESWY 297
Cdd:PRK04778 325 QNKELKEEIDRVKQSY---------TLNESEL----ESVRQLEKQ--LESLEKQYDEITERIaeqeiayselQEELEEIL 389

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 74315985  298 RTkCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 340
Cdd:PRK04778 390 KQ-LEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
105-416 4.07e-131

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 382.35  E-value: 4.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   105 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNMEPLFEGYIEALRREAECVEADSGRLAAELNHA 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   184 QESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDTSIVVKM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   264 DNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQN 343
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74315985   344 TKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQR 416
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
3-102 1.60e-14

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 70.84  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985     3 CGSYCGGRAFSCASACGPRPGrccisaapYRGIScyrGLSGGFGSQSVCGAfrsGSCGRSFGYRsGGICGPSPP--CITT 80
Cdd:pfam16208  70 GFGGGGGGGFGGGFGGGGGGG--------FGGGG---GFGGGFGGGGYGGG---GFGGGGFGGR-GGFGGPPCPpgGIQE 134

                          90       100
                  ....*....|....*....|..
gi 74315985    81 VSVNESLLTPLNLEIDPNAQCV 102
Cdd:pfam16208 135 VTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-389 2.81e-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: 2.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    155 FEGYI-----EALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSLRATA--------ENEFVALKKDVDCAYLR 221
Cdd:TIGR02169  223 YEGYEllkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    222 KSDLEANAEALTQETDFL---RRMYDEETRILHSHISDTSIVVKMDNSRDLNMDCVVAEIKAQYDDIasRSRAEAESwyr 298
Cdd:TIGR02169  303 IASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD--- 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    299 TKCEEIKATVIRHGETLRRTREEINELNRMI-------QRLTAEIENAKCQNTKLEAAVTQSeqqgEAALADARCKLAEL 371
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQ 453

                          250
                   ....*....|....*...
gi 74315985    372 EGALQKAKQDMACLLKEY 389
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQEL 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-417 3.30e-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: 3.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985     94 EIDPNAQCVKhEEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQfYQNRKCCESNMEplfegyIEALRREAECVEADS 173
Cdd:TIGR02168  678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKD------LARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    174 GRLAAELNHAQESMEGYKKRYEEEVSLRATAENEfvalkkdvdcaylrKSDLEANAEALTQETDFLRRMYDEETRILhsh 253
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------------IEELEAQIEQLKEELKALREALDELRAEL--- 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    254 isdtsivvkmdnsRDLNmdcvvaeikaqyddiasRSRAEAeswyRTKCEEIKATVIRHGETLRRTREEINELNRMIQRLT 333
Cdd:TIGR02168  813 -------------TLLN-----------------EEAANL----RERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    334 AEIENAKCQNTKLEAAV---TQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEvmnsklgLDVEITTYRRLL 410
Cdd:TIGR02168  859 AEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-------LREKLAQLELRL 931


                   ....*..
gi 74315985    411 EGEEQRL 417
Cdd:TIGR02168  932 EGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 125-399 8.96e-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: 51.60  E-value: 8.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    125 RFLEQQNKLLETKWQFYQNR-KCCESNMEPLFEGY------IEALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEE 197
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRlEELREELEELQEELkeaeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    198 VSLRATAENEFVALKKdvdcaylRKSDLEANAEALTQETDFLRRMYDEETRILHShiSDTSIVVKMDNSRDLNMDcvVAE 277
Cdd:TIGR02168  294 ANEISRLEQQKQILRE-------RLANLERQLEELEAQLEELESKLDELAEELAE--LEEKLEELKEELESLEAE--LEE 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    278 IKAQYDDIASRSRAEAESW--YRTKCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIE--NAKCQNTKLEAAVTQS 353
Cdd:TIGR02168  363 LEAELEELESRLEELEEQLetLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAEL 442

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 74315985    354 EQ------QGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGL 399
Cdd:TIGR02168  443 EEleeeleELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-419 3.23e-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: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    155 FEGYIEALRREAECVEADSG--------------RLAAELNHAQESMEGYKKRYEEEVSLRA----TAENEFVALKKDVD 216
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIErldliidekrqqleRLRREREKAERYQALLKEKREYEGYELLkekeALERQKEAIERQLA 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    217 CAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDTSIVVKMDnsrdlnmdcvVAEIKAQyddIASRSRAEAEsw 296
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK----------IGELEAE---IASLERSIAE-- 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    297 YRTKCEEIKATVIRHGETLRRTREEINELNRMIQR-------LTAEIENAKcqnTKLEAAVTQSEQQgEAALADARCKLA 369
Cdd:TIGR02169  313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELK---EELEDLRAELEEV-DKEFAETRDELK 388

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 74315985    370 ELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQRLCE 419
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-417 1.63e-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: 47.74  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    190 YKKRYEE-EVSLRATAEN----EFVA--LKKDVDcaylrksDLEANAEAlTQETDFLRrmydEETRILHSHISDTSIVVK 262
Cdd:TIGR02168  170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEK-AERYKELK----AELRELELALLVLRLEEL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    263 MDNSRDLNMDcvVAEIKAQYDDIASRSRAEAESWYRTKCE--EIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 340
Cdd:TIGR02168  238 REELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    341 CQNTKLEAAVTQSEQQGE---AALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQRL 417
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 161-378 4.10e-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: 46.32  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    161 ALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLR 240
Cdd:pfam01576  500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    241 RMYDEetrilhshisdtsIVVKMDNSRDL--NM-------DCVVAE---IKAQYDDiaSRSRAEAESwyRTKceEIKA-T 307
Cdd:pfam01576  580 QELDD-------------LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74315985    308 VIRHGETLRRTREEINELNRMiqrLTAEIE---NAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKA 378
Cdd:pfam01576  641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
315-417 8.11e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 8.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 315 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 391
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                        90       100
                ....*....|....*....|....*.
gi 74315985 392 VMNSKLGLDVEITTYRRLLEGEEQRL 417
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 315-383 1.18e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 42.30  E-value: 1.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74315985   315 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMA 383
Cdd:pfam11559  47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQ 118
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 155-340 2.17e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985  155 FEGYIEALRREAECVEADSGRLaaELNHAQESMEGYKKR----Y---EEEVslraTAENeFVALKKDVDCAYLRKsdLEA 227
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREV----KARK-YVEKNSDTLPDFLEH--AKE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985  228 NAEALTQETDFLRRMYdeetrilhsHISDTSIvvkmDNSRDLNMDcvVAEIKAQYDDIASRS----------RAEAESWY 297
Cdd:PRK04778 325 QNKELKEEIDRVKQSY---------TLNESEL----ESVRQLEKQ--LESLEKQYDEITERIaeqeiayselQEELEEIL 389

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 74315985  298 RTkCEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 340
Cdd:PRK04778 390 KQ-LEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 315-395 2.79e-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: 43.21  E-value: 2.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 315 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 391
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108


                ....
gi 74315985 392 VMNS 395
Cdd:COG4942 109 LLRA 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 275-417 6.21e-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: 6.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 275 VAEIKAQYDDIASRSRAEAESWYrtkceEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSE 354
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74315985 355 QQG----------EAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQRL 417
Cdd:COG1196 344 EELeeaeeeleeaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 127-393 8.46e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   127 LEQQNKLLETKWQFYQNRKccesNMEPLFEGYIEALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSLRATAEN 206
Cdd:pfam07888  40 LQERAELLQAQEAANRQRE----KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   207 EFVALKKDVDCAYLRKSDLEANAEALTQ-----ETDfLRRMYDEETRI------------------------LHSHISD- 256
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQrvlerETE-LERMKERAKKAgaqrkeeeaerkqlqaklqqteeeLRSLSKEf 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   257 ---------------------TSIVVKMD--NSRDLNMDCVVAEIKAQYD--------------DIAS----RSRAEAE- 294
Cdd:pfam07888 195 qelrnslaqrdtqvlqlqdtiTTLTQKLTtaHRKEAENEALLEELRSLQErlnaserkveglgeELSSmaaqRDRTQAEl 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   295 --------------SWYRTKCEEIKATVIRHGETLRRT----REEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ 356
Cdd:pfam07888 275 hqarlqaaqltlqlADASLALREGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDC 354

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 74315985   357 GEAALADARCKLAELEGALQKAKQDMACLLKEYQEVM 393
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
PTZ00121 PTZ00121
MAEBL; Provisional
 159-381 8.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   159 IEALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSlraTAENEFVALKkdvdcayLRKSDLEANAEALTQETDF 238
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR---KAEEERKAEE-------ARKAEDAKKAEAVKKAEEA 1235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   239 LRrmyDEETRILHSHISDTSIVVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAEswyRTKCEEI-KATVIRHGETLRR 317
Cdd:PTZ00121 1236 KK---DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74315985   318 TREEinelNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQD 381
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-381 9.04e-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: 41.67  E-value: 9.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 170 EADSGRLAAELNHAQESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRI 249
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 250 L---------HSHISDTSIVVKMDNSRDlnmdcvvAEIKAQYDDIASRSRAEaeswyrtkceeikatvirHGETLRRTRE 320
Cdd:COG4942 106 LaellralyrLGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELRADLA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74315985 321 EINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQD 381
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
313-397 9.71e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 9.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 313 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALAdarcKLAELEGALQKAKQDMACLLKEYQEV 392
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE----ELKELEEQLESLQEELAALEQELQAL 176


                ....*
gi 74315985 393 MNSKL 397
Cdd:COG4372 177 SEAEA 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 105-332 1.34e-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: 41.58  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    105 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRkccesnmeplfegyIEALRREAECVEADSGRLAAELNHAQ 184
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------------LESLERRIAATERRLEDLEEQIEELS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    185 ESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQEtdfLRRMYDEETRILHSHISDTSIVVKMD 264
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE---LRELESKRSELRRELEELREKLAQLE 928

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74315985    265 NsrdlnmdcVVAEIKAQYDDIASRSRAEaeswYRTKCEEIKATVIRHGETLRRTREEINELNRMIQRL 332
Cdd:TIGR02168  929 L--------RLEGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
PRK11281 PRK11281
mechanosensitive channel MscK;
276-383 1.49e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   276 AEIKAQYDDIASRSRAEAESwyrtkceeiKATVIRHGETLR------RTREEINELNRMIQRLTAEIENAKCQNTKLEAA 349
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 74315985   350 VTQSEQQ--GEAALADARCKLAELEGALQKAKQDMA 383
Cdd:PRK11281  110 NDEETREtlSTLSLRQLESRLAQTLDQLQNAQNDLA 145
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 160-411 2.08e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    160 EALRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFL 239
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    240 RRMYDEetriLHSHISDtsivvkmdnsrdlnMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTR 319
Cdd:TIGR02169  757 KSELKE----LEARIEE--------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    320 EEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGE----------AALADARCKLAELEGALQKAKQDMACLLKEY 389
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQL 898

                          250       260
                   ....*....|....*....|..
gi 74315985    390 QEVMNSKLGLDVEITTYRRLLE 411
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLS 920
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 103-416 2.94e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    103 KHEEKEQIKCLNSKFAAFIDKVRFLEQQNKLLE-TKWQFYQNRKCCESNMEPLFEGYIEALR----------REAECVEA 171
Cdd:TIGR00606  243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKsRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELV 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    172 DSGRLAAELNhaQESMEGYKKRYEEEVslrataENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILH 251
Cdd:TIGR00606  323 DCQRELEKLN--KERRLLNQEKTELLV------EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    252 SHisdtsIVVKMDNSRDLNMdcvvaeikaqyddiASRSRAEAESWYRTKCEEIKatvirhgetlrRTREEINELNRMIQr 331
Cdd:TIGR00606  395 FH-----TLVIERQEDEAKT--------------AAQLCADLQSKERLKQEQAD-----------EIRDEKKGLGRTIE- 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985    332 LTAEIENAKCQNTKLeaaVTQSEQQGEAALADarckLAELEGALQKAKQDMA---------CLLKEYQEVMNSKLGLDve 402
Cdd:TIGR00606  444 LKKEILEKKQEELKF---VIKELQQLEGSSDR----ILELDQELRKAERELSkaeknslteTLKKEVKSLQNEKADLD-- 514

                          330
                   ....*....|....
gi 74315985    403 iTTYRRLLEGEEQR 416
Cdd:TIGR00606  515 -RKLRKLDQEMEQL 527
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
275-381 4.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 275 VAEIKAQYDDIASRSRAEAESWYRtkcEEIKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNT--KLEAAV-T 351
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDE---EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELeE 480

                        90       100       110
                ....*....|....*....|....*....|..
gi 74315985 352 QSEQQGEAALADARCKLAE--LEGALQKAKQD 381
Cdd:COG4717 481 LKAELRELAEEWAALKLALelLEEAREEYREE 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-417 4.80e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 274 VVAEIKAQYDDIAsRSRAEAESW--YRTKCEEIKATVI-----RHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKL 346
Cdd:COG1196 194 ILGELERQLEPLE-RQAEKAERYreLKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74315985 347 EAAVTQSEQQGEAALADarckLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEITTYRRLLEGEEQRL 417
Cdd:COG1196 273 RLELEELELELEEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 285-391 5.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 5.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985 285 IASRSRAEAESWYRTKCEEIKATVirhgETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQgeaalada 364
Cdd:COG3883   6 LAAPTPAFADPQIQAKQKELSELQ----AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------- 73

                        90       100
                ....*....|....*....|....*..
gi 74315985 365 rckLAELEGALQKAKQDMACLLKEYQE 391
Cdd:COG3883  74 ---IAEAEAEIEERREELGERARALYR 97
mukB PRK04863
chromosome partition protein MukB;
175-362 6.14e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   175 RLAAELNHAQESMEGYKKRYEEEVSLRATAENEFVALKkDVDC--AYLRKSD----LEANA---EALTQETDFLRRMYDE 245
Cdd:PRK04863  925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQrrAHFSYEDaaemLAKNSdlnEKLRQRLEQAEQERTR 1003

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   246 ETRILHSHISD----TSIVVKMDNSRDLNMDcVVAEIKAQYDDIASRSRAEAESWYRTKCEEIkatvirHGEtLRRTREE 321
Cdd:PRK04863 1004 AREQLRQAQAQlaqyNQVLASLKSSYDAKRQ-MLQELKQELQDLGVPADSGAEERARARRDEL------HAR-LSANRSR 1075

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 74315985   322 INELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALA 362
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 288-413 7.69e-03

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 38.16  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74315985   288 RSRAEAESWyrtkcEEIKATVIRHGETLRRTREE--------------INELNRMIQRltAEIENAKCQNTKLEAAVTQS 353
Cdd:pfam14992  44 RSLAEDEER-----EELNFTIMEKEDALQELELEtaklekkneilvksVMELQRKLSR--KSDKNTGLEQETLKQMLEEL 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74315985   354 E---QQGEAALADARCKLAELEGALQKAKQ---DMACLLKEYQEVMNsKLGLDVEIttyrRLLEGE 413
Cdd:pfam14992 117 KvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILR-KMEEEKET----RLLEKE 177
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 313-391 9.85e-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: 38.21  E-value: 9.85e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74315985 313 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQgeaaLADARCKLAELEGALQKAKQDMACLLKEYQE 391
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAE 94
 
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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