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Conserved domains on  [gi|6680606|ref|NP_032497|]
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keratin, type I cytoskeletal 19 isoform 1 [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 11981676)

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-393 4.54e-151

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 429.73  E-value: 4.54e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPSRDYNHYFKTIEDLRDKILGATIDNSKIVLQIDNA 161
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    162 RLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVG-GQVSVEV 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    241 DSTPGVDLAKILSEMRSQYEIMAEKNRKDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680606    321 AALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-393 4.54e-151

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 429.73  E-value: 4.54e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPSRDYNHYFKTIEDLRDKILGATIDNSKIVLQIDNA 161
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    162 RLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVG-GQVSVEV 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    241 DSTPGVDLAKILSEMRSQYEIMAEKNRKDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680606    321 AALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-399 1.91e-09

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: 59.69  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     137 IEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAY 216
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     217 L---KKNHEEEITALRSQVGG-QVSVEVDSTPGVDLAKILSEMRSQY---EIMAEKNRKDAEATYlARIEELNTQVAVHS 289
Cdd:TIGR02168  773 AeeeLAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATE-RRLEDLEEQIEELS 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     290 EQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQIQSVisgfEAQLSDVRADIERQNQEYKQL 369
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQL 927
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 6680606     370 MDIKSRLEQEIAT--------YRSLLEGQEAHYNNLPT 399
Cdd:TIGR02168  928 ELRLEGLEVRIDNlqerlseeYSLTLEEAEALENKIED 965
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
189-388 1.93e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  189 LRRVLDELTLARTDLEMQIESLKEELAylkkNHEEEITALRSQVGGqVSVEVDSTpgvDLAKILSEMRSQYEiMAEKNRK 268
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLA-EARAELA 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  269 DAEAtylaRIEELNTQVAVHSEQIQ--ISKTEVTDLRRTLQGLEIELQSQLS-----------MKAALEGTLAETEARYG 335
Cdd:COG3206 237 EAEA----RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQ 312
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680606  336 VQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIK---SRLEQEIATYRSLLE 388
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
46 PHA02562
endonuclease subunit; Provisional
135-383 1.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   135 KTIEDL-------------RDKILGATIDNSKIVLQIDNA--RLAAddfRTKFETEhaLRLSVEADINGLRRVLDELTLA 199
Cdd:PHA02562 154 KLVEDLldisvlsemdklnKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEE--QRKKNGENIARKQNKYDELVEE 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   200 RTDLEMQIESLKEELAYLKKNHEEEITALR--SQVGGQVSVEVDStpgvdLAKIL-------------SEMRSQYEIMAE 264
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ-----FQKVIkmyekggvcptctQQISEGPDRITK 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   265 KNRKDAEATYlaRIEELNTQVavhsEQIQISKTEVTDLRRTLQgleiELQSQLSmkaALEGTLAETEArygvQLSQIQSV 344
Cdd:PHA02562 304 IKDKLKELQH--SLEKLDTAI----DELEEIMDEFNEQSKKLL----ELKNKIS---TNKQSLITLVD----KAKKVKAA 366
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 6680606   345 ISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATY 383
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-393 4.54e-151

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 429.73  E-value: 4.54e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     82 NEKITMQNLNDRLASYLDKVRALEQANGELEVKIRDWYQKQGPGPSRDYNHYFKTIEDLRDKILGATIDNSKIVLQIDNA 161
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    162 RLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVG-GQVSVEV 240
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    241 DSTPGVDLAKILSEMRSQYEIMAEKNRKDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMK 320
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680606    321 AALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAH 393
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-399 1.91e-09

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: 59.69  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     137 IEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAY 216
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     217 L---KKNHEEEITALRSQVGG-QVSVEVDSTPGVDLAKILSEMRSQY---EIMAEKNRKDAEATYlARIEELNTQVAVHS 289
Cdd:TIGR02168  773 AeeeLAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATE-RRLEDLEEQIEELS 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     290 EQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQIQSVisgfEAQLSDVRADIERQNQEYKQL 369
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLAQL 927
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 6680606     370 MDIKSRLEQEIAT--------YRSLLEGQEAHYNNLPT 399
Cdd:TIGR02168  928 ELRLEGLEVRIDNlqerlseeYSLTLEEAEALENKIED 965
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-388 2.00e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     190 RRVLDELTLARTDLEMQIESLKEELAYLKKNHEE-----------------EITALRSQVG------GQVSVEVDSTpGV 246
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkeleelsrQISALRKDLArleaevEQLEERIAQL-SK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     247 DLAKILSEMRSQYEIMAEKNRKDAEAtyLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGT 326
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680606     327 LAETEARYGV---QLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:TIGR02168  833 IAATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-397 2.41e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 2.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     137 IEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAY 216
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     217 L----------------KKNHEEEITALRSQVGGQVSVEVDStpgvdLAKILSEMRSQYEIMAEKNR-KDAEATYLAR-I 278
Cdd:TIGR02168  314 LerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEeLEEQLETLRSkV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     279 EELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLsmKAALEGTLAETEArygvQLSQIQSVISGFEAQLSDVRAD 358
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQA----ELEELEEELEELQEELERLEEA 462
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 6680606     359 IERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
189-388 1.93e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  189 LRRVLDELTLARTDLEMQIESLKEELAylkkNHEEEITALRSQVGGqVSVEVDSTpgvDLAKILSEMRSQYEiMAEKNRK 268
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLA-EARAELA 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  269 DAEAtylaRIEELNTQVAVHSEQIQ--ISKTEVTDLRRTLQGLEIELQSQLS-----------MKAALEGTLAETEARYG 335
Cdd:COG3206 237 EAEA----RLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQ 312
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680606  336 VQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIK---SRLEQEIATYRSLLE 388
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
251-392 2.72e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  251 ILSEMRSQY--------------EIMAEKNRKDAEAtYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQ 316
Cdd:COG1196 194 ILGELERQLeplerqaekaeryrELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6680606  317 LSMKAALEGTLAETEARY---GVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEA 392
Cdd:COG1196 273 RLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
157-385 3.21e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 3.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  157 QIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVggqv 236
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL---- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  237 svevdstpgvdlaKILSEMRSQYEIMAEKNRKDAEATY--LARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQ 314
Cdd:COG4942 111 -------------RALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680606  315 SQLSMKAALEGTLAEtearygvQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRS 385
Cdd:COG4942 178 ALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
140-393 6.89e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 6.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     140 LRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKK 219
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     220 NHEEEITALRSQVGGQVSVEvdstpgVDLAKILSEMrsqYEIMAEKNRKDAEATYL-ARIEELNTQVAVHSEQIQISKTE 298
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYR------EKLEKLKREI---NELKRELDRLQEELQRLsEELADLNAAIAGIEAKINELEEE 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     299 VTDLRRTLQGLEIELQSQLSMKAALEGT---LAETEARYGVQLSQIQSVISGFEAQLSDVRadiERQNQEYKQLMDIKSR 375
Cdd:TIGR02169  443 KEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASE---ERVRGGRAVEEVLKAS 519
                          250
                   ....*....|....*...
gi 6680606     376 LEQEIATYRSLLEGQEAH 393
Cdd:TIGR02169  520 IQGVHGTVAQLGSVGERY 537
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-385 8.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 8.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   159 DNARLAADDFRTKF--ETEHALRLSVEA----DINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRsqv 232
Cdd:COG4913  173 DSFSAYLARLRRRLgiGSEKALRLLHKTqsfkPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDARE--- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   233 ggQVsvevdstpgvdlaKILSEMRSQYE----IMAEKNRKDAEATYL-------------ARIEELNTQVAVHSEQIQIS 295
Cdd:COG4913  250 --QI-------------ELLEPIRELAEryaaARERLAELEYLRAALrlwfaqrrlelleAELEELRAELARLEAELERL 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   296 KTEVTDLRRTLQGLEI-----------ELQSQLSMK------------------AALEGTLAETEARYGVQLSQIQSVIS 346
Cdd:COG4913  315 EARLDALREELDELEAqirgnggdrleQLEREIERLereleererrrarleallAALGLPLPASAEEFAALRAEAAALLE 394
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 6680606   347 GFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRS 385
Cdd:COG4913  395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-388 1.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   272 ATYLARIEELNTQVAVHSEQIQISKTE---VTDLRRTLQGLEiELQSQLSMKAALEGTLAETEARYGvQLSQIQSVISGF 348
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAEldaLQERREALQRLA-EYSWDEIDVASAEREIAELEAELE-RLDASSDDLAAL 690
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 6680606   349 EAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:COG4913  691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
207-392 1.59e-04

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: 43.90  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     207 IESLKEELAYLKKNhEEEITALRSQVGGQVSvevdstpgvDLAKILSEMRSQYEIMAEKNRKDAEatylaRIEELntqva 286
Cdd:TIGR02169  683 LEGLKRELSSLQSE-LRRIENRLDELSQELS---------DASRKIGEIEKEIEQLEQEEEKLKE-----RLEEL----- 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     287 vhSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQ-LSQIQSVISGFEAQLSDVRADIERQNQE 365
Cdd:TIGR02169  743 --EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQK 820
                          170       180       190
                   ....*....|....*....|....*....|
gi 6680606     366 YKQLMDIKSRLEQEIAT---YRSLLEGQEA 392
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQElqeQRIDLKEQIK 850
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
157-378 1.65e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  157 QIDNARLAADDFRTKfeteHALrLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKnheeeitalrsqvggQV 236
Cdd:COG3206 190 ELEEAEAALEEFRQK----NGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA---------------QL 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  237 SVEVDSTPGVDLAKILSEMRSQYeIMAEKNRKDAEATYLAR---IEELNTQVAVHSEQIQisktevTDLRRTLQGLEIEL 313
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQL-AELEAELAELSARYTPNhpdVIALRAQIAALRAQLQ------QEAQRILASLEAEL 322
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680606  314 QSQLSMKAALEGTLAETEARYGvQLSQIQsvisgfeAQLSDVRADIERQNQEYKQLMdikSRLEQ 378
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA-ELPELE-------AELRRLEREVEVARELYESLL---QRLEE 376
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
89-397 2.66e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606      89 NLNDRLASYLDKVRALEQA-NGELEVKIRDWYQKQGPGPSRDynHYFKTIEDLRDKI--LGATID--NSKIVLQIDNARL 163
Cdd:pfam15921  374 NLDDQLQKLLADLHKREKElSLEKEQNKRLWDRDTGNSITID--HLRRELDDRNMEVqrLEALLKamKSECQGQMERQMA 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     164 AADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHE------EEITALRSQVGGQVS 237
Cdd:pfam15921  452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnAEITKLRSRVDLKLQ 531
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     238 -VEVDSTPGVDLAKILSEMRSQYEIMAEKNRkdAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQ 316
Cdd:pfam15921  532 eLQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     317 LSMKAALEGTLAETEARYG-VQLSQIQSVISGFEaQLSDVRaDIErqnQEYKQLMDiksrleqEIATYRSLLEGQEAHYN 395
Cdd:pfam15921  610 KILKDKKDAKIRELEARVSdLELEKVKLVNAGSE-RLRAVK-DIK---QERDQLLN-------EVKTSRNELNSLSEDYE 677

                   ..
gi 6680606     396 NL 397
Cdd:pfam15921  678 VL 679
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
182-392 3.28e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  182 VEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEITALRSQVGgqvsvevdstpgvDLAKILSEM-RSQYE 260
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-------------EEYELLAELaRLEQD 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  261 IMAEKNRKDAEAtylARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELqsqlsmkAALEGTLAETEARYGV---Q 337
Cdd:COG1196 304 IARLEERRRELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEEL-------EEAEAELAEAEEALLEaeaE 373
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6680606  338 LSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEA 392
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-394 3.60e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  135 KTIEDLRDKILGATIDNSKIVLQIDNARLAADDFRTKFETEHALRLSVEADI--------------NGLRRVLDELTLAR 200
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleqdiarleerrRELEERLEELEEEL 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  201 TDLEMQIESLKEELAYLKKNHEEEITALRSQvggQVSVEvdstpgvDLAKILSEMRSQYE--IMAEKNRKDAEATYLARI 278
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEA---EAELA-------EAEEALLEAEAELAeaEEELEELAEELLEALRAA 395
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  279 EELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYGVQLSQiqsvisgfEAQLSDVRAD 358
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--------EEALLELLAE 467
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 6680606  359 IERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHY 394
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
157-354 5.99e-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: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     157 QIDNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKN---HEEEITALRSQVG 233
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLE 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     234 G-QVSVEVDSTPGVDLAKILSEMRSQyEIMAEKNRKDAEatylarIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIE 312
Cdd:TIGR02168  411 RlEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEE------LEELQEELERLEEALEELREELEEAEQALDAAERE 483
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 6680606     313 LQSQLSMKAALEGTL--AETEARYGVQLSQIQSVISGFEAQLSD 354
Cdd:TIGR02168  484 LAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVLSE 527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
159-368 9.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   159 DNARLAADDFRTKFETEHALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKN------------------ 220
Cdd:COG4913  585 GNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidva 664
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   221 -HEEEITALRSQVGgqvsvEVDSTPGVdlakiLSEMRSQYEImAEKNRKDAEatylARIEELNTQVAVHSEQIQISKTEV 299
Cdd:COG4913  665 sAEREIAELEAELE-----RLDASSDD-----LAALEEQLEE-LEAELEELE----EELDELKGEIGRLEKELEQAEEEL 729
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680606   300 TDLRRTLQGLEIELQSQLSmkAALEGTLAE--TEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQ 368
Cdd:COG4913  730 DELQDRLEAAEDLARLELR--ALLEERFAAalGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
246-397 9.94e-04

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: 40.29  E-value: 9.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  246 VDLAKILSEMRSqyeimAEKNRKDAEAtylaRIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQsqlsmkaaleg 325
Cdd:COG1579  10 LDLQELDSELDR-----LEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----------- 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680606  326 TLAETEARYGVQLSQIQSV--ISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:COG1579  70 EVEARIKKYEEQLGNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
46 PHA02562
endonuclease subunit; Provisional
135-383 1.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   135 KTIEDL-------------RDKILGATIDNSKIVLQIDNA--RLAAddfRTKFETEhaLRLSVEADINGLRRVLDELTLA 199
Cdd:PHA02562 154 KLVEDLldisvlsemdklnKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEE--QRKKNGENIARKQNKYDELVEE 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   200 RTDLEMQIESLKEELAYLKKNHEEEITALR--SQVGGQVSVEVDStpgvdLAKIL-------------SEMRSQYEIMAE 264
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNklNTAAAKIKSKIEQ-----FQKVIkmyekggvcptctQQISEGPDRITK 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   265 KNRKDAEATYlaRIEELNTQVavhsEQIQISKTEVTDLRRTLQgleiELQSQLSmkaALEGTLAETEArygvQLSQIQSV 344
Cdd:PHA02562 304 IKDKLKELQH--SLEKLDTAI----DELEEIMDEFNEQSKKLL----ELKNKIS---TNKQSLITLVD----KAKKVKAA 366
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 6680606   345 ISGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATY 383
Cdd:PHA02562 367 IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
235-392 1.53e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.22  E-value: 1.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  235 QVSVEVDSTPGV----------DLAKILSEM---RSQYEI--MAEKNRKDAeatyLARIEElntQVAVHSEQIQISKTEV 299
Cdd:COG3524 128 RVKVEYDSTSGIitlevrafdpEDAQAIAEAllaESEELVnqLSERAREDA----VRFAEE---EVERAEERLRDAREAL 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  300 TDLRRTLQGL--EIELQSQLSMKAALEGTLAETEArygvQLSQIQSVISGFEAQLSDVRADIErqnqeykqlmdiksRLE 377
Cdd:COG3524 201 LAFRNRNGILdpEATAEALLQLIATLEGQLAELEA----ELAALRSYLSPNSPQVRQLRRRIA--------------ALE 262
                       170
                ....*....|....*
gi 6680606  378 QEIATYRSLLEGQEA 392
Cdd:COG3524 263 KQIAAERARLTGASG 277
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
177-388 1.95e-03

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: 40.26  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    177 ALRLSVEADINGLRRVLDELTLARTDLEMQIESLKEELAYLKKNHEEEitalrsqvggqvsvevdstpgvdLAKILSEMR 256
Cdd:pfam07888  52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-----------------------EEKYKELSA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    257 SQYEIMAEKNR-KDAEATYLARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLEIELQSQLSMKAALEGTLAETEARYG 335
Cdd:pfam07888 109 SSEELSEEKDAlLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680606    336 VQLSQIQSVISGFEAQLSDV---RADIERQNQEYKQLMDIKSRLEQEIATYRSLLE 388
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVlqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQE 244
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
193-360 3.21e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.40  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    193 LDELTLARTDLEMQIESLKEELaylKKNHEEEITALRSQVGGQVS-VEVDSTPGVD-----LAKILSEMRSQYEIMAEKN 266
Cdd:pfam01442   6 LDELSTYAEELQEQLGPVAQEL---VDRLEKETEALRERLQKDLEeVRAKLEPYLEelqakLGQNVEELRQRLEPYTEEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    267 RKDAEAtylaRIEELNTQVAVHSEQIQ-ISKTEVTDLRRTLQGLEIELQSQLSMKA-ALEGTLAETEARYGVQLSQ-IQS 343
Cdd:pfam01442  83 RKRLNA----DAEELQEKLAPYGEELReRLEQNVDALRARLAPYAEELRQKLAERLeELKESLAPYAEEVQAQLSQrLQE 158
                         170
                  ....*....|....*..
gi 6680606    344 VISGFEAQLSDVRADIE 360
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
276-397 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: 39.27  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606     276 ARIEELNTQVAVHSEQIQISKTEVTDLRRTLQGLE----------IELQSQLSMKAALEGTLAETEARYGVQLSQIQSVI 345
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 6680606     346 SGFEAQLSDVRADIERQNQEYKQLMDIKSRLEQEIATYRSLLEGQEAHYNNL 397
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
75-388 5.53e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 38.79  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606   75 SDGLLSGNEKITMQNLNDRLASYLDKVRALEQANGELE--VKIRDWYQKQGPGPSRDY--------NHYFKTIEDLRDKI 144
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEklVEQNTDLRLEKLGENAESskrlnenaNNLIKQFENTKEKI 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  145 LGATIDNS-KIVLQIDNARLAADDFRTKFEtehALRLSVEADINGLRRvldELTLARTDLEMQIESLKEELAYLKknhEE 223
Cdd:COG5185 299 AEYTKSIDiKKATESLEEQLAAAEAEQELE---ESKRETETGIQNLTA---EIEQGQESLTENLEAIKEEIENIV---GE 369
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  224 EITALRSQVGGQVSVEVDSTPgvdlAKILSEMRSQ--YEIMAEKNRKDAEATYLARIEELNTQV----AVHSEQIQISKT 297
Cdd:COG5185 370 VELSKSSEELDSFKDTIESTK----ESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIeqatSSNEEVSKLLNE 445
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606  298 EVTDLRRTLQGLEIELQSQLSMKA-ALEGTLAETEARYGVQLSQIQSVISGFEAQLSDVRADIERQNQEYKQLMDIKSRL 376
Cdd:COG5185 446 LISELNKVMREADEESQSRLEEAYdEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAES 525
                       330
                ....*....|..
gi 6680606  377 EQEIATYRSLLE 388
Cdd:COG5185 526 LKDFMRARGYAH 537
Rabaptin pfam03528
Rabaptin;
247-391 5.70e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 38.93  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680606    247 DLAKILSE-MRSQYEIMAEKNRKDAE--ATYLARIEELNTQVAVhseqIQISKTEVTDLRRTLQGLEIELQSQLSMKAAL 323
Cdd:pfam03528  12 ELEKENAEfYRLKQQLEAEFNQKRAKfkELYLAKEEDLKRQNAV----LQEAQVELDALQNQLALARAEMENIKAVATVS 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6680606    324 EGTlaETEARYGVQlSQIQSVISGFEAQLSDVRADIERQ-----NQEYKQLMDIKSRLEQEIATY-RSLLEGQE 391
Cdd:pfam03528  88 ENT--KQEAIDEVK-SQWQEEVASLQAIMKETVREYEVQfhrrlEQERAQWNQYRESAEREIADLrRRLSEGQE 158
 
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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