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Conserved domains on  [gi|300623540|emb|CBU83086|]
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unnamed protein product [Homo sapiens]

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

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
79-390 5.99e-145

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 413.93  E-value: 5.99e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   79 NEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNA 158
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  159 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVG-GQVSVEV 237
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  238 DSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300623540  318 AALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
79-390 5.99e-145

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 413.93  E-value: 5.99e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   79 NEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNA 158
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  159 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVG-GQVSVEV 237
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  238 DSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300623540  318 AALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-395 1.27e-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: 60.07  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   130 YYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKE 209
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   210 ELAYL----------------KKNHEEEISTLRGQVGGQVSVEVDSapgtdLAKILSDMRSQYEVMAEQNRKDAEAWfts 273
Cdd:TIGR02168  310 RLANLerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQL--- 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   274 rtEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETE-ARFGAQLAHIQALISGIEAQLGDV 352
Cdd:TIGR02168  382 --ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERL 459
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 300623540   353 RADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLS 395
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
186-385 3.19e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 186 LRRVLDELTLARTDLEMQIEGLKEELAylkkNHEEEISTLRGQVGGqVSVEVDsapGTDLAKILSDMRSQYeVMAEQNRK 265
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEE---AKLLLQQLSELESQL-AEARAELA 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 266 DAEAWFTSRTEELNREVAGHTEQLQMSrsEVTDLRRTLQGLEIELQSQLS-----------MKAALEDTLAETEARFGAQ 334
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRI 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300623540 335 LAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIK---SRLEQEIATYRSLLE 385
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
PRK09039 PRK09039
peptidoglycan -binding protein;
276-389 4.55e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 276 EELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAE------------------------TEARF 331
Cdd:PRK09039  56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAElagagaaaegragelaqeldsekqVSARA 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300623540 332 GAQLAHIQALISGIEAQLGDVRA---DSERQNQEYQ-RLMDIKSRLE-------QEIATYRS--------LLEGQED 389
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAaldASEKRDRESQaKIADLGRRLNvalaqrvQELNRYRSeffgrlreILGDREG 212
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
79-390 5.99e-145

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 413.93  E-value: 5.99e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   79 NEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNA 158
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  159 RLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVG-GQVSVEV 237
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540  238 DSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMK 317
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300623540  318 AALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-395 1.27e-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: 60.07  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   130 YYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKE 209
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   210 ELAYL----------------KKNHEEEISTLRGQVGGQVSVEVDSapgtdLAKILSDMRSQYEVMAEQNRKDAEAWfts 273
Cdd:TIGR02168  310 RLANLerqleeleaqleelesKLDELAEELAELEEKLEELKEELES-----LEAELEELEAELEELESRLEELEEQL--- 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   274 rtEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETE-ARFGAQLAHIQALISGIEAQLGDV 352
Cdd:TIGR02168  382 --ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERL 459
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 300623540   353 RADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLS 395
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-387 3.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   132 TTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEEL 211
Cdd:TIGR02168  719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   212 AYLKKNH---EEEISTLRGQVGGQVS-VEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRT--EELNREVAGH 285
Cdd:TIGR02168  799 KALREALdelRAELTLLNEEAANLRErLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEliEELESELEAL 878
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   286 TEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEarfgAQLAHIQALISGIEAQLGDVRadsERQNQEYQR 365
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQ---ERLSEEYSL 951
                          250       260
                   ....*....|....*....|..
gi 300623540   366 LMDIKSRLEQEIATYRSLLEGQ 387
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRR 973
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
137-378 2.69e-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: 43.13  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   137 LRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKK 216
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   217 NHEEEISTLRgqvggqvsvevdsapgtdlakilsdmRSQYEVMAEQNRKDAeawFTSRTEELNREVAGHTEQLQMSRSEV 296
Cdd:TIGR02169  372 ELEEVDKEFA--------------------------ETRDELKDYREKLEK---LKREINELKRELDRLQEELQRLSEEL 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   297 TDLRRTLQGLEielQSQLSMKAALEDTLAETEArfgaqlahIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQE 376
Cdd:TIGR02169  423 ADLNAAIAGIE---AKINELEEEKEDKALEIKK--------QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491

                   ..
gi 300623540   377 IA 378
Cdd:TIGR02169  492 LA 493
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
186-385 3.19e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 186 LRRVLDELTLARTDLEMQIEGLKEELAylkkNHEEEISTLRGQVGGqVSVEVDsapGTDLAKILSDMRSQYeVMAEQNRK 265
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEE---AKLLLQQLSELESQL-AEARAELA 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 266 DAEAWFTSRTEELNREVAGHTEQLQMSrsEVTDLRRTLQGLEIELQSQLS-----------MKAALEDTLAETEARFGAQ 334
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRI 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300623540 335 LAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIK---SRLEQEIATYRSLLE 385
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
178-388 4.01e-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: 42.75  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   178 SVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEE---EISTLRGQVGgQVSVEVDSapgtdLAKILSDMRS 254
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRD-KLTEEYAE-----LKEELEDLRA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   255 QyevmAEQNRKDAEAWFtsrteelnREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEAR---F 331
Cdd:TIGR02169  372 E----LEEVDKEFAETR--------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineL 439
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300623540   332 GAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQE 388
Cdd:TIGR02169  440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
80-379 4.34e-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: 42.80  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540    80 EKLTMQN----LNDRLASYLDKVRALEAANGEL-------EVKIRDWYQKQGPGpsRDYSHYYTTIQDLRDKILGATIEN 148
Cdd:pfam15921  487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQHLKNEG--DHLRNVQTECEALKLQMAEKDKVI 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   149 SRIVLQIDN-ARLAADDFRTKfETEQALRMSVEADINGLRRVLDELTLART-------DLEMQIEGLKEELAYLKKNHEE 220
Cdd:pfam15921  565 EILRQQIENmTQLVGQHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNAGSE 643
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   221 EISTLRG--QVGGQVSVEVDSAPGTdlakiLSDMRSQYEVMAEQnrkdaeawFTSRTEELNREVAGHTEQLQMSRSEVTD 298
Cdd:pfam15921  644 RLRAVKDikQERDQLLNEVKTSRNE-----LNSLSEDYEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQ 710
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540   299 LRRTLQGLeiELQSQLSMKAALEDTLAETEARfgAQLAHIQALISGIEAQLGDVradserqNQEYQRLMDIKSRLEQEIA 378
Cdd:pfam15921  711 TRNTLKSM--EGSDGHAMKVAMGMQKQITAKR--GQIDALQSKIQFLEEAMTNA-------NKEKHFLKEEKNKLSQELS 779

                   .
gi 300623540   379 T 379
Cdd:pfam15921  780 T 780
PRK09039 PRK09039
peptidoglycan -binding protein;
276-389 4.55e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 276 EELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAE------------------------TEARF 331
Cdd:PRK09039  56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAElagagaaaegragelaqeldsekqVSARA 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300623540 332 GAQLAHIQALISGIEAQLGDVRA---DSERQNQEYQ-RLMDIKSRLE-------QEIATYRS--------LLEGQED 389
Cdd:PRK09039 136 LAQVELLNQQIAALRRQLAALEAaldASEKRDRESQaKIADLGRRLNvalaqrvQELNRYRSeffgrlreILGDREG 212
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
179-390 5.88e-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: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 179 VEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEvdsapgTDLAKILSDMRSQYEV 258
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL------AELARLEQDIARLEER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 259 MAEQNRKDAEAwfTSRTEELNREVAGHTEQLQMSRSEVTDL---RRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQL 335
Cdd:COG1196  311 RRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300623540 336 AHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDH 390
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
154-382 6.48e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 154 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLkknhEEEISTLRGQVGGQV 233
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL----RAELEAQKEELAELL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 234 SVevdsapgtdlakiLSDMRSQYEVMAEQNRKDAEAWFTSRT--EELNREVAGHTEQLQMSRSEVTDLRRtlqgleiELQ 311
Cdd:COG4942  111 RA-------------LYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRA-------ELE 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300623540 312 SQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRS 382
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
154-364 2.51e-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: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 154 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLkknhEEEISTLRGQVGGQV 233
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGERA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 234 -SVEVDSAPGTDLAKIL-----SDMRSQYEVMAEQNRKDAEAwfTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLE 307
Cdd:COG3883   93 rALYRSGGSVSYLDVLLgsesfSDFLDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300623540 308 IELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQ 364
Cdd:COG3883  171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
46 PHA02562
endonuclease subunit; Provisional
137-380 7.82e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 137 LRDKILGATIENSRIVLQIDNA--RLAAddfRTKFETEQalRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYL 214
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIqqQIKT---YNKNIEEQ--RKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 215 KKNHEEEISTLrgqvggqvsvevdSAPGTDLAKILSDMRS--QYEVMAE---------QNRKDAEAWFTSRTEELN---- 279
Cdd:PHA02562 247 VMDIEDPSAAL-------------NKLNTAAAKIKSKIEQfqKVIKMYEkggvcptctQQISEGPDRITKIKDKLKelqh 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300623540 280 --REVAGHTEQLQMSRSEVTDLRRTLQgleiELQSQLSmkaaledTLAETEARFGAQLAHIQALISGIEAQLGDVRADSE 357
Cdd:PHA02562 314 slEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKIS-------TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
                        250       260
                 ....*....|....*....|...
gi 300623540 358 RQNQEYQRLMDIKSRLEQEIATY 380
Cdd:PHA02562 383 KLQDELDKIVKTKSELVKEKYHR 405
 
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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