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Conserved domains on  [gi|22164776|ref|NP_666175|]
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keratin, type II cytoskeletal 79 [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;
138-452 2.31e-140

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 407.38  E-value: 2.31e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   138 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQsQNTGVARsLEPFFENYLSTLRRQLDTKQSERGRLDMELR 217
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   218 NVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVIL 297
Cdd:pfam00038  79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   298 SMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKK 377
Cdd:pfam00038 159 EMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22164776   378 QCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:pfam00038 239 QKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
62-135 2.16e-27

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    62 LYNLGG-KNISVSMA-----------CGASSGRALG-------------------GFGSGAYVGLGASRQTFG------- 103
Cdd:pfam16208  45 LYNLGGsKSISISVAgggsrpgsgfgFGGGGGGGFGggfgggggggfgggggfggGFGGGGYGGGGFGGGGFGgrggfgg 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 22164776   104 PVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRV 135
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
138-452 2.31e-140

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 407.38  E-value: 2.31e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   138 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQsQNTGVARsLEPFFENYLSTLRRQLDTKQSERGRLDMELR 217
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   218 NVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVIL 297
Cdd:pfam00038  79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   298 SMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKK 377
Cdd:pfam00038 159 EMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22164776   378 QCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:pfam00038 239 QKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
62-135 2.16e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    62 LYNLGG-KNISVSMA-----------CGASSGRALG-------------------GFGSGAYVGLGASRQTFG------- 103
Cdd:pfam16208  45 LYNLGGsKSISISVAgggsrpgsgfgFGGGGGGGFGggfgggggggfgggggfggGFGGGGYGGGGFGGGGFGgrggfgg 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 22164776   104 PVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRV 135
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-454 2.23e-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: 53.92  E-value: 2.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    130 PEIQRVRtqerEQIKTLNNKFASFIDKVRflEQQNKVLETKwALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSER 209
Cdd:TIGR02169  674 AELQRLR----ERLEGLKRELSSLQSELR--RIENRLDELS-QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    210 GRLDMELRNVQDNLEDfknkYEDEINkrtALENEFVLLKKDVDAAYmgRMDLHGKVDSLTQEIDFLqqlfEMELSQVQTN 289
Cdd:TIGR02169  747 SSLEQEIENVKSELKE----LEARIE---ELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKL----EEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    290 VSDTNVILSMDNNRNLDLDSIIAEVKAQYELIA--QKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQR 367
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    368 LQGEVDAAKKQCQQLQTAIAEAEQNgemalkdakkkLGDLDTALHQAKEDLARMLREYQDLVSVKlALDMEIATYRKLLE 447
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKR-----------LSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQ 961


                   ....*..
gi 22164776    448 SEESRMS 454
Cdd:TIGR02169  962 RVEEEIR 968
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-426 2.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  199 RRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYmgrmdLHGKVDSLTQEIdflqql 278
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAEL------ 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  279 femelsqvqtnvsdtnvilsmdnnRNLDLDSiiAEVKaqyELIAQKSRAEAEswyqtkyeelqvtagkhgdsLRDTKNEI 358
Cdd:COG4913  678 ------------------------ERLDASS--DDLA---ALEEQLEELEAE--------------------LEELEEEL 708

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  359 AELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNGEMAL---------------------KDAKKKLGDLDTALHQAKED 417
Cdd:COG4913  709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdaverelrENLEERIDALRARLNRAEEE 788


                 ....*....
gi 22164776  418 LARMLREYQ 426
Cdd:COG4913  789 LERAMRAFN 797
46 PHA02562
endonuclease subunit; Provisional
 155-407 2.68e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  155 DKVRFLEQQNKVLETKWALLQEQSQntgvarslepFFENYLSTLRRQLDTKQSergrldmELRNVQDNLEDFKNKYEDEI 234
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK----------TYNKNIEEQRKKNGENIA-------RKQNKYDELVEEAKTIKAEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  235 NKRTALENEFVLLKKDVDAAY----MGRMDLHGKVDSLTQEIDFLQQlfEMELSQVQTNVSDTNVILSmdnnrnlDLDSI 310
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRIT-------KIKDK 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  311 IAEVKAQYELIaqksraeaeswyQTKYEELQVTAGKHGD---SLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQ---- 383
Cdd:PHA02562 308 LKELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQaefv 375

                        250       260
                 ....*....|....*....|....*..
gi 22164776  384 ---TAIAEAEQNgemaLKDAKKKLGDL 407
Cdd:PHA02562 376 dnaEELAKLQDE----LDKIVKTKSEL 398
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
138-452 2.31e-140

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 407.38  E-value: 2.31e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   138 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQsQNTGVARsLEPFFENYLSTLRRQLDTKQSERGRLDMELR 217
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSR-LYSLYEKEIEDLRRQLDTLTVERARLQLELD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   218 NVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVIL 297
Cdd:pfam00038  79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   298 SMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKK 377
Cdd:pfam00038 159 EMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKK 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22164776   378 QCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:pfam00038 239 QKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
62-135 2.16e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    62 LYNLGG-KNISVSMA-----------CGASSGRALG-------------------GFGSGAYVGLGASRQTFG------- 103
Cdd:pfam16208  45 LYNLGGsKSISISVAgggsrpgsgfgFGGGGGGGFGggfgggggggfgggggfggGFGGGGYGGGGFGGGGFGgrggfgg 124

                          90       100       110
                  ....*....|....*....|....*....|..
gi 22164776   104 PVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRV 135
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 130-454 2.23e-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: 53.92  E-value: 2.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    130 PEIQRVRtqerEQIKTLNNKFASFIDKVRflEQQNKVLETKwALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSER 209
Cdd:TIGR02169  674 AELQRLR----ERLEGLKRELSSLQSELR--RIENRLDELS-QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    210 GRLDMELRNVQDNLEDfknkYEDEINkrtALENEFVLLKKDVDAAYmgRMDLHGKVDSLTQEIDFLqqlfEMELSQVQTN 289
Cdd:TIGR02169  747 SSLEQEIENVKSELKE----LEARIE---ELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKL----EEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    290 VSDTNVILSMDNNRNLDLDSIIAEVKAQYELIA--QKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQR 367
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    368 LQGEVDAAKKQCQQLQTAIAEAEQNgemalkdakkkLGDLDTALHQAKEDLARMLREYQDLVSVKlALDMEIATYRKLLE 447
Cdd:TIGR02169  894 LEAQLRELERKIEELEAQIEKKRKR-----------LSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQ 961


                   ....*..
gi 22164776    448 SEESRMS 454
Cdd:TIGR02169  962 RVEEEIR 968
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-434 1.82e-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: 50.83  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776     88 GSGAYVGlGASRQTFGPVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRVRTQERE---QIKTLNNKFASFIDKVRFLEQQN 164
Cdd:TIGR02168  657 PGGVITG-GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    165 KVLETKWALLQEQSQNTGVARSLepfFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEF 244
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTE---LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    245 VLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEmelsqvQTNVSDTNVILSMdNNRNLDLDSIIAEVKAQYELIAQK 324
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIE------ELSEDIESLAAEI-EELEELIEELESELEALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    325 SRAEAESwyQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEaeqNGEMALKDAKKKL 404
Cdd:TIGR02168  886 EEALALL--RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALE 960

                          330       340       350
                   ....*....|....*....|....*....|
gi 22164776    405 GDLDTALHQAKEDLARMLREYQDLVSVKLA 434
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLENKIKELGPVNLA 990
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-425 4.10e-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: 49.67  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    158 RFLEQQNKVLETKWALLqeqsqntgvARSLEpFFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFknkyEDEINKr 237
Cdd:TIGR02168  214 RYKELKAELRELELALL---------VLRLE-ELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSE- 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    238 taLENEFVLLKKDVDAAYmgrmdlhGKVDSLTQEIDFLQQlfemELSQVQTNVSDTNVILSMDNNRNLDLDSIIAEVKAQ 317
Cdd:TIGR02168  279 --LEEEIEELQKELYALA-------NEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEK 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    318 YELIAQK--SRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNG-- 393
Cdd:TIGR02168  346 LEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIee 425

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 22164776    394 ------EMALKDAKKKLGDLDTALHQAKEDLARMLREY 425
Cdd:TIGR02168  426 llkkleEAELKELQAELEELEEELEELQEELERLEEAL 463
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 125-404 9.33e-06

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: 48.48  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   125 NVEIDPEIQrvrtQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNtgvarslepfFENYLSTLRRQLDT 204
Cdd:TIGR04523 358 NSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ----------KDEQIKKLQQEKEL 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   205 KQSERGRL-----------------DMELRNVQDNLEDFKNK-------YEDEINK-RTALEN---EFVLLKKDVDAAYM 256
Cdd:TIGR04523 424 LEKEIERLketiiknnseikdltnqDSVKELIIKNLDNTRESletqlkvLSRSINKiKQNLEQkqkELKSKEKELKKLNE 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   257 GRMDLHGKVDSLTQEIDFL---QQLFEMELSQVQTNVSDTNV-ILSMDNNRNldldsiiaevKAQYELIAQKSRAEAESW 332
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLkekIEKLESEKKEKESKISDLEDeLNKDDFELK----------KENLEKEIDEKNKEIEEL 573

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22164776   333 YQT------KYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIaeaeqngeMALKDAKKKL 404
Cdd:TIGR04523 574 KQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII--------KNIKSKKNKL 643
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-452 1.27e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    354 TKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNgemaLKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKL 433
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750

                           90
                   ....*....|....*....
gi 22164776    434 ALDMEIATYRKLLESEESR 452
Cdd:TIGR02168  751 QLSKELTELEAEIEELEER 769
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-426 2.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  199 RRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYmgrmdLHGKVDSLTQEIdflqql 278
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAEL------ 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  279 femelsqvqtnvsdtnvilsmdnnRNLDLDSiiAEVKaqyELIAQKSRAEAEswyqtkyeelqvtagkhgdsLRDTKNEI 358
Cdd:COG4913  678 ------------------------ERLDASS--DDLA---ALEEQLEELEAE--------------------LEELEEEL 708

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  359 AELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNGEMAL---------------------KDAKKKLGDLDTALHQAKED 417
Cdd:COG4913  709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdaverelrENLEERIDALRARLNRAEEE 788


                 ....*....
gi 22164776  418 LARMLREYQ 426
Cdd:COG4913  789 LERAMRAFN 797
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 201-448 3.40e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 201 QLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQlfe 280
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 281 mELSQVQTNVSDTNVILSMDNNRN-LDLdsiiaevkaqyeLIAQKSRAEAE---SWYQTKYEELQvtagKHGDSLRDTKN 356
Cdd:COG4942  98 -ELEAQKEELAELLRALYRLGRQPpLAL------------LLSPEDFLDAVrrlQYLKYLAPARR----EQAEELRADLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 357 EIAELTRttqrlqgEVDAAKKQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALD 436
Cdd:COG4942 161 ELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233

                       250
                ....*....|..
gi 22164776 437 MEIATYRKLLES 448
Cdd:COG4942 234 AEAAAAAERTPA 245
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 227-450 1.27e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    227 KNKYEDEINKRTALENEFVLLKKDVDAAYmgrMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVILSMDNNRNLD 306
Cdd:pfam15921  592 KAQLEKEINDRRLELQEFKILKDKKDAKI---RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE 668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    307 LDSIIAEvkaqYELIAQKsraeaeswYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQ----------------- 369
Cdd:pfam15921  669 LNSLSED----YEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgmqkqi 736

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    370 ----GEVDAAKKQCQQLQTAIAEAEQNGEMaLKDAKKKLGDLDTALHQAKEDLA---RMLREYQDLVSVKLAlDMEIATY 442
Cdd:pfam15921  737 takrGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVA-NMEVALD 814


                   ....*...
gi 22164776    443 RKLLESEE 450
Cdd:pfam15921  815 KASLQFAE 822
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-452 1.74e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 307 LDSIIAEVKAQYE-LIAQKSRAEAESW-YQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQT 384
Cdd:COG1196 244 LEAELEELEAELEeLEAELAELEAELEeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22164776 385 AIAEAEQNGEMA---LKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:COG1196 324 ELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 208-424 1.76e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.56  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   208 ERGRLDMELRNVQDNLEDFKNKYEDEINKRTALE----------------NEFVLLK-------KDVDAAYMGRMDLHGK 264
Cdd:pfam15905  88 ERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSasvaslekqlleltrvNELLKAKfsedgtqKKMSSLSMELMKLRNK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   265 VDSLTQEIDFLQQLFEMELSQVQTNVSDTNVILSMDNNRNLDLDSIIAEVKAQYE-LIAQKSRAEAESWYQTKYEE---- 339
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEkLLEYITELSCVSEQVEKYKLdiaq 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776   340 LQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAakkQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLA 419
Cdd:pfam15905 248 LEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE---KCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQ 324


                  ....*
gi 22164776   420 RMLRE 424
Cdd:pfam15905 325 KLQQK 329
46 PHA02562
endonuclease subunit; Provisional
 155-407 2.68e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  155 DKVRFLEQQNKVLETKWALLQEQSQntgvarslepFFENYLSTLRRQLDTKQSergrldmELRNVQDNLEDFKNKYEDEI 234
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK----------TYNKNIEEQRKKNGENIA-------RKQNKYDELVEEAKTIKAEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  235 NKRTALENEFVLLKKDVDAAY----MGRMDLHGKVDSLTQEIDFLQQlfEMELSQVQTNVSDTNVILSmdnnrnlDLDSI 310
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRIT-------KIKDK 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  311 IAEVKAQYELIaqksraeaeswyQTKYEELQVTAGKHGD---SLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQ---- 383
Cdd:PHA02562 308 LKELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQaefv 375

                        250       260
                 ....*....|....*....|....*..
gi 22164776  384 ---TAIAEAEQNgemaLKDAKKKLGDL 407
Cdd:PHA02562 376 dnaEELAKLQDE----LDKIVKTKSEL 398
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 326-391 2.71e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.44  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22164776   326 RAEAESWyQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQ 391
Cdd:pfam12718   6 KLEAENA-QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEK 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-442 2.96e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 131 EIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNtgvarslepffenylstLRRQLDTKQSERG 210
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-----------------LEERLEELEEELA 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 211 RLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAymgrmdLHGKVDSLTQEIDFLQQLFEmELSQVQTNV 290
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLE-ALRAAAELA 399

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 291 SDTNVILSMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESwyQTKYEELQvtagkhgDSLRDTKNEIAELTRTTQRLQG 370
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAA-------EEEAELEEEEEALLELLAELLE 470

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22164776 371 EVDAAKKQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARML-REYQDLVSVKLALDMEIATY 442
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAYEAALEAA 543
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 349-426 3.26e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22164776 349 DSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQngemALKDAKKKLGDLDTALHQAKEDLARMLREYQ 426
Cdd:COG3883  23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREELGERARALY 96
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
160-452 4.72e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 160 LEQQNKVLETKWALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTA 239
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 240 LENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFE-------------------MELSQVQTNVSDTNVILSMD 300
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAaleqelqalseaeaeqaldELLKEANRNAEKEEELAEAE 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 301 NNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQ 380
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22164776 381 QLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESR 452
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
302-444 6.95e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 302 NRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQT--KYEELQVTAGKHGDSLRDTKNEIAELTRTT---------QRLQG 370
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLGELEELLEALdeeeleeelEELEE 439

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22164776 371 EVDAAKKQCQQLQTAIAEAEQngEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRK 444
Cdd:COG4717 440 ELEELEEELEELREELAELEA--ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 303-453 7.36e-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: 39.27  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776    303 RNLDLDSIIAEVKAQYELIAQKSRAEAEswYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQL 382
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22164776    383 QTAIAEAEQNGEMALKDAKKKLGDLDTALHQ---AKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRM 453
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
PRK12704 PRK12704
phosphodiesterase; Provisional
 312-425 7.67e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  312 AEVKAQYELIAQKSRAEAEswYQTKYEELQ----------VTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQ 381
Cdd:PRK12704  58 ALLEAKEEIHKLRNEFEKE--LRERRNELQklekrllqkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 22164776  382 LQT-AIAEAEQNGEMALKDAKKKLgdLDTALHQAKEDLARMLREY 425
Cdd:PRK12704 136 LIEeQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLIKEI 178
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 311-454 8.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 8.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776 311 IAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGK--HGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAE 388
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22164776 389 AE---QNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRMS 454
Cdd:COG1196 349 AEeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-277 9.70e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 9.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  112 QEVTVNQSLLTPLNVEIDpeiQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNTGVARsLEPFf 191
Cdd:COG4913  269 ERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-LEQL- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22164776  192 ENYLSTLRRQLDTKQSERGRLDMELRNVQ----DNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDS 267
Cdd:COG4913  344 EREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423

                        170
                 ....*....|
gi 22164776  268 LTQEIDFLQQ 277
Cdd:COG4913  424 LEAEIASLER 433
 
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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