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Conserved domains on  [gi|530399828|ref|XP_005268733|]
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keratin, type II cytoskeletal 80 isoform X1 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
28-428 1.36e-75

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 240.21  E-value: 1.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   28 DPFAAFLlSQVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRI 106
Cdd:pfam00038  11 DRLASYI-DKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  107 RYEDEISKRTDMEFTFVQLKKvacpacprgsflmgpgpsfppdillsfmpnqspqrlksqdqqtdreippspsssffeal 186
Cdd:pfam00038  90 KYEDELNLRTSAENDLVGLRK----------------------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  187 sqissgitptltqeaapqptpalgpsipsptthhccqpqDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQV 266
Cdd:pfam00038 111 ---------------------------------------DLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQV 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  267 KDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRS 346
Cdd:pfam00038 152 SDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEI 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  347 QILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEE 426
Cdd:pfam00038 232 ELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311


                  ..
gi 530399828  427 GR 428
Cdd:pfam00038 312 CR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
28-428 1.36e-75

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 240.21  E-value: 1.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   28 DPFAAFLlSQVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRI 106
Cdd:pfam00038  11 DRLASYI-DKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  107 RYEDEISKRTDMEFTFVQLKKvacpacprgsflmgpgpsfppdillsfmpnqspqrlksqdqqtdreippspsssffeal 186
Cdd:pfam00038  90 KYEDELNLRTSAENDLVGLRK----------------------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  187 sqissgitptltqeaapqptpalgpsipsptthhccqpqDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQV 266
Cdd:pfam00038 111 ---------------------------------------DLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQV 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  267 KDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRS 346
Cdd:pfam00038 152 SDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEI 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  347 QILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEE 426
Cdd:pfam00038 232 ELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311


                  ..
gi 530399828  427 GR 428
Cdd:pfam00038 312 CR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 234-430 3.12e-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: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   234 RTELETKLKSLESFVELMktiyeQELKDLAAQVKDVSVTVgmdsrchidLSGIVEEVKAQYDAvaarsLEEAEAYSRSQL 313
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-----ERYKELKAELRELELAL---------LVLRLEELREELEE-----LQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   314 EEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAK---TKLAQLEAALQQA 390
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleAQLEELESKLDEL 335

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 530399828   391 KQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 430
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
256-439 5.96e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 256 EQELKDLAAQVKDVSVTVGMDSrchidLSGIVEEVKAQYDAVAARsLEEAEAySRSQLEEQAARSAEYGSSLQSS----- 330
Cdd:COG3206  195 EAALEEFRQKNGLVDLSEEAKL-----LLQQLSELESQLAEARAE-LAEAEA-RLAALRAQLGSGPDALPELLQSpviqq 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 331 -RSEIADLNVR--------------IQKLRSQILSVKShclKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMA 395
Cdd:COG3206  268 lRAQLAELEAElaelsarytpnhpdVIALRAQIAALRA---QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530399828 396 RQLRKYQELMNVKLALDIEIATYRKLVE-----GEEGRMDSPSATVVSA 439
Cdd:COG3206  345 ELPELEAELRRLEREVEVARELYESLLQrleeaRLAEALTVGNVRVIDP 393
PRK09039 PRK09039
peptidoglycan -binding protein;
256-396 2.48e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 256 EQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAA-RS-LEEAEAYSRSQLEEQAARSAEYGSSL------ 327
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAeRSrLQALLAELAGAGAAAEGRAGELAQELdsekqv 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530399828 328 -QSSRSEIADLNVRIQKLRSQILSvkshclkLEENIKTAEEQGelafQDAKTKLA----QLEAALQQAKQDMAR 396
Cdd:PRK09039 132 sARALAQVELLNQQIAALRRQLAA-------LEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 261-422 3.88e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.28  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 261 DLAAQVKDVSVTVGMDSRchIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAArsaeygsslqssrsEIADLNVR 340
Cdd:cd22656   73 SLAGDIYNYAQNAGGTID--SYYAEILELIDDLADATDDEELEEAKKTIKALLDDLLK--------------EAKKYQDK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 341 IQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQD-----AKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLA-LDIE 414
Cdd:cd22656  137 AAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAdDEAK 216


                 ....*...
gi 530399828 415 IATYRKLV 422
Cdd:cd22656  217 LAAALRLI 224
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
28-428 1.36e-75

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 240.21  E-value: 1.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   28 DPFAAFLlSQVQALEQRNQLLETRWSFLQGQDSA-IFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRI 106
Cdd:pfam00038  11 DRLASYI-DKVRFLEQQNKLLETKISELRQKKGAePSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  107 RYEDEISKRTDMEFTFVQLKKvacpacprgsflmgpgpsfppdillsfmpnqspqrlksqdqqtdreippspsssffeal 186
Cdd:pfam00038  90 KYEDELNLRTSAENDLVGLRK----------------------------------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  187 sqissgitptltqeaapqptpalgpsipsptthhccqpqDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQV 266
Cdd:pfam00038 111 ---------------------------------------DLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQV 151

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  267 KDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRS 346
Cdd:pfam00038 152 SDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEI 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  347 QILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEE 426
Cdd:pfam00038 232 ELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311


                  ..
gi 530399828  427 GR 428
Cdd:pfam00038 312 CR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 234-430 3.12e-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: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   234 RTELETKLKSLESFVELMktiyeQELKDLAAQVKDVSVTVgmdsrchidLSGIVEEVKAQYDAvaarsLEEAEAYSRSQL 313
Cdd:TIGR02168  195 LNELERQLKSLERQAEKA-----ERYKELKAELRELELAL---------LVLRLEELREELEE-----LQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   314 EEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAK---TKLAQLEAALQQA 390
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleAQLEELESKLDEL 335

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 530399828   391 KQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 430
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
256-439 5.96e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 256 EQELKDLAAQVKDVSVTVGMDSrchidLSGIVEEVKAQYDAVAARsLEEAEAySRSQLEEQAARSAEYGSSLQSS----- 330
Cdd:COG3206  195 EAALEEFRQKNGLVDLSEEAKL-----LLQQLSELESQLAEARAE-LAEAEA-RLAALRAQLGSGPDALPELLQSpviqq 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 331 -RSEIADLNVR--------------IQKLRSQILSVKShclKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMA 395
Cdd:COG3206  268 lRAQLAELEAElaelsarytpnhpdVIALRAQIAALRA---QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530399828 396 RQLRKYQELMNVKLALDIEIATYRKLVE-----GEEGRMDSPSATVVSA 439
Cdd:COG3206  345 ELPELEAELRRLEREVEVARELYESLLQrleeaRLAEALTVGNVRVIDP 393
PRK09039 PRK09039
peptidoglycan -binding protein;
256-396 2.48e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 256 EQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAA-RS-LEEAEAYSRSQLEEQAARSAEYGSSL------ 327
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAeRSrLQALLAELAGAGAAAEGRAGELAQELdsekqv 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530399828 328 -QSSRSEIADLNVRIQKLRSQILSvkshclkLEENIKTAEEQGelafQDAKTKLA----QLEAALQQAKQDMAR 396
Cdd:PRK09039 132 sARALAQVELLNQQIAALRRQLAA-------LEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 296-402 5.27e-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: 42.06  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 296 AVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQgelaFQD 375
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAE 87

                         90       100
                 ....*....|....*....|....*..
gi 530399828 376 AKTKLAQLEAALQQAKQDMARQLRKYQ 402
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALY 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 288-431 8.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 288 EEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEY-------GSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEE 360
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELeaelaelEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530399828 361 NIKTAEE---QGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMDS 431
Cdd:COG1196  303 DIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 234-406 8.05e-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: 42.35  E-value: 8.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   234 RTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSV---TVGMDSRCHIDLSGIVEEVKAQYDAVAAR--SLEEAEAY 308
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaEVEQLEERIAQLSKELTELEAEIEELEERleEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   309 SRSQLEEQAARSAEYGSSLQSSRSEIADLN--------------VRIQKLRSQILSVKSHCLKLEENIKTAEEQGE---L 371
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaanlrERLESLERRIAATERRLEDLEEQIEELSEDIEslaA 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 530399828   372 AFQDAKTKLAQLEAALQ-------QAKQDMARQLRKYQELMN 406
Cdd:TIGR02168  860 EIEELEELIEELESELEallneraSLEEALALLRSELEELSE 901
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
368-439 8.13e-04

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 41.70  E-value: 8.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530399828 368 QGELAFQDAKTKLAQLEAALQQAKQDMARqlrkYQELMNVKLALDIEIATYRKLVEGEEGRMDSPSATVVSA 439
Cdd:PRK11556 122 PFKVALAQAQGQLAKDQATLANARRDLAR----YQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASA 189
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 287-426 8.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 287 VEEVKAQYDAVAAR--SLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKT 364
Cdd:COG1196  283 LEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530399828 365 AEEQG---ELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEE 426
Cdd:COG1196  363 AEEALleaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 234-430 8.86e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 8.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 234 RTELETKLKSLE-------SFVELMKTIYEQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAARSLEEAE 306
Cdd:COG1196  195 LGELERQLEPLErqaekaeRYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 307 AYSRSQLEEQAARSAEYG---------SSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENI-------KTAEEQ-- 368
Cdd:COG1196  275 ELEELELELEEAQAEEYEllaelarleQDIARLEERRRELEERLEELEEELAELEEELEELEEELeeleeelEEAEEEle 354

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530399828 369 -GELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 430
Cdd:COG1196  355 eAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-403 1.39e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 307 AYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQgelafqdaktkLAQLEAA 386
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-----------IAEAEAE 80

                         90
                 ....*....|....*..
gi 530399828 387 LQQAKQDMARQLRKYQE 403
Cdd:COG3883   81 IEERREELGERARALYR 97
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-417 1.73e-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: 41.21  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   236 ELETKLKSLESFVELMKTI---YEQELKDLAAQVkdvsvtvgmdsrchidlsgiveevkAQYDAVAARSLEEAEAYSRsQ 312
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSiaeKERELEDAEERL-------------------------AKLEAEIDKLLAEIEELER-E 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   313 LEEQAARSAEYGSSLQSSRSEIADLNVRIQKL--RSQILSVKSHCLKlEENIKTAEEQGELAFQDAK--TKLAQLEAALQ 388
Cdd:TIGR02169  345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVdkEFAETRDELKDYR-EKLEKLKREINELKRELDRlqEELQRLSEELA 423

                          170       180
                   ....*....|....*....|....*....
gi 530399828   389 QAKQDMARQLRKYQELMNVKLALDIEIAT 417
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIKK 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 289-423 3.43e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   289 EVKAQYDAVAARsLEEAEAYSRSQLEEQAARSAEYGSS-LQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIK--TA 365
Cdd:TIGR02169  208 EKAERYQALLKE-KREYEGYELLKEKEALERQKEAIERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlGE 286

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530399828   366 EEQGELafqdaKTKLAQLEAALQQAK----------QDMARQLRKYQELMNVKLA----LDIEIATYRKLVE 423
Cdd:TIGR02169  287 EEQLRV-----KEKIGELEAEIASLErsiaekerelEDAEERLAKLEAEIDKLLAeieeLEREIEEERKRRD 353
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 261-422 3.88e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.28  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 261 DLAAQVKDVSVTVGMDSRchIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAArsaeygsslqssrsEIADLNVR 340
Cdd:cd22656   73 SLAGDIYNYAQNAGGTID--SYYAEILELIDDLADATDDEELEEAKKTIKALLDDLLK--------------EAKKYQDK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 341 IQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQD-----AKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLA-LDIE 414
Cdd:cd22656  137 AAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDeggaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIAdDEAK 216


                 ....*...
gi 530399828 415 IATYRKLV 422
Cdd:cd22656  217 LAAALRLI 224
PRK11281 PRK11281
mechanosensitive channel MscK;
288-395 3.93e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828  288 EEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEygsSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEE 367
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLD---KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 530399828  368 Q--GELAFQDAKTKLAQLEAALQQAKQDMA 395
Cdd:PRK11281  116 EtlSTLSLRQLESRLAQTLDQLQNAQNDLA 145
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
256-396 4.43e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 39.26  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 256 EQELKDLAAQ----VKDVSVTVG-----------MDSRchiDLSGIVEEVKAQYD-AVAARSLEEAEAYSRSQLEEQAAR 319
Cdd:COG1566   42 EARVVTVAAKvsgrVTEVLVKEGdrvkkgqvlarLDPT---DLQAALAQAEAQLAaAEAQLARLEAELGAEAEIAAAEAQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 320 SAEYGSSLQSSRSEIAdlnvRIQKL--------------RSQILSVKSHCLKLEENIKTAEEQGELAFQ--DAKTKLAQL 383
Cdd:COG1566  119 LAAAQAQLDLAQRELE----RYQALykkgavsqqeldeaRAALDAAQAQLEAAQAQLAQAQAGLREEEElaAAQAQVAQA 194

                        170
                 ....*....|...
gi 530399828 384 EAALQQAKQDMAR 396
Cdd:COG1566  195 EAALAQAELNLAR 207
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-410 4.71e-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: 39.65  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   235 TELETKLKSLESFVELMKTIY---EQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDavaarSLEEAEAYSRS 311
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-----ELEELIEELES 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828   312 QLEE------------QAARSAEY--GSSLQSSRSEIADLNVRIQKLRSQILSVKSHC----LKLEENIKTAEEQGELAF 373
Cdd:TIGR02168  874 ELEAllnerasleealALLRSELEelSEELRELESKRSELRRELEELREKLAQLELRLegleVRIDNLQERLSEEYSLTL 953

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 530399828   374 QDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLA 410
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 303-386 6.47e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 39.00  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 303 EEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVK-----------------SHCLKLEENIKTA 365
Cdd:PRK10636 534 KENNANSAQARKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEeklgdselydqsrkaelTACLQQQASAKSG 613

                         90       100
                 ....*....|....*....|.
gi 530399828 366 EEQGELAFQDAKTKLAQLEAA 386
Cdd:PRK10636 614 LEECEMAWLEAQEQLEQMLLE 634
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-430 6.90e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 286 IVEEVKAQYD------AVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHclklE 359
Cdd:COG1196  194 ILGELERQLEplerqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE----L 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530399828 360 ENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMD 430
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 302-423 7.71e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 302 LEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKS----HCLKLE-ENIKTAEEQGELAFQDA 376
Cdd:COG1579   36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyEALQKEiESLKRRISDLEDEILEL 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530399828 377 KTKLAQLEAALQQAKQDMARQLRKYQELmnvKLALDIEIATYRKLVE 423
Cdd:COG1579  116 MERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-423 8.05e-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: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399828 296 AVAARSLEEAEAY---SRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELA 372
Cdd:COG1196  347 EEAEEELEEAEAElaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530399828 373 FQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVE 423
Cdd:COG1196  427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
 
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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