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Conserved domains on  [gi|1958657467|ref|XP_038941537|]
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keratin, type I cytoskeletal 17 isoform X2 [Rattus norvegicus]

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;
25-312 2.31e-126

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 365.01  E-value: 2.31e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  25 TANTELEVKIRDWYQKQAPGPARDYSAYYQTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEAD 104
Cdd:pfam00038  25 QQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEND 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 105 INGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMDAAPGVDLSRILSEMRDQYEKMAE 183
Cdd:pfam00038 105 LVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMDAARKLDLTSALAEIRAQYEEIAA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 184 KNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGL 263
Cdd:pfam00038 185 KNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQEL 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958657467 264 IGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 312
Cdd:pfam00038 265 ISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
25-312 2.31e-126

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 365.01  E-value: 2.31e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  25 TANTELEVKIRDWYQKQAPGPARDYSAYYQTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEAD 104
Cdd:pfam00038  25 QQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEND 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 105 INGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMDAAPGVDLSRILSEMRDQYEKMAE 183
Cdd:pfam00038 105 LVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMDAARKLDLTSALAEIRAQYEEIAA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 184 KNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGL 263
Cdd:pfam00038 185 KNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQEL 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958657467 264 IGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 312
Cdd:pfam00038 265 ISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-307 1.47e-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: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  101 VEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEK 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  181 MAEKNRKDAEDWFF------SKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYC 254
Cdd:TIGR02168  762 EIEELEERLEEAEEelaeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958657467  255 V---QLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 307
Cdd:TIGR02168  842 DleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
92-300 1.20e-06

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: 49.76  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  92 ETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKK---NHEEEMNALRGQVGgEINVEMDAapgvdLS 168
Cdd:COG4942    24 EAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKEIAE-----LR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 169 RILSEMRDQYEKMAEK----NRKDAEDWFFSKTE--ELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASL 242
Cdd:COG4942    97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958657467 243 EGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 300
Cdd:COG4942   177 EALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
25-312 2.31e-126

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 365.01  E-value: 2.31e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  25 TANTELEVKIRDWYQKQAPGPARDYSAYYQTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEAD 104
Cdd:pfam00038  25 QQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEND 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 105 INGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMDAAPGVDLSRILSEMRDQYEKMAE 183
Cdd:pfam00038 105 LVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMDAARKLDLTSALAEIRAQYEEIAA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 184 KNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGL 263
Cdd:pfam00038 185 KNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQEL 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958657467 264 IGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 312
Cdd:pfam00038 265 ISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-307 1.47e-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: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  101 VEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEK 180
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  181 MAEKNRKDAEDWFF------SKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYC 254
Cdd:TIGR02168  762 EIEELEERLEEAEEelaeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958657467  255 V---QLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 307
Cdd:TIGR02168  842 DleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
54-301 2.98e-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: 52.37  E-value: 2.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467   54 QTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEEL 133
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  134 AYL---KKNHEEEMNALRGQVGG-EINVEMDAAPGVDLSRILSEMRDQYEKMAEK---NRKDAEDWFFSkTEELNREVAT 206
Cdd:TIGR02168  771 EEAeeeLAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAANLRERlesLERRIAATERR-LEDLEEQIEE 849
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  207 NSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQgligSVEEQLAQLRCEMEQQNQEYK 286
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR----ELESKRSELRRELEELREKLA 925
                          250
                   ....*....|....*
gi 1958657467  287 ILLDVKTRLEQEIAT 301
Cdd:TIGR02168  926 QLELRLEGLEVRIDN 940
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
89-307 3.17e-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: 52.37  E-value: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467   89 TKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHE-----------------EEMNALRGQV 151
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqleeleskldelaEELAELEEKL 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  152 gGEINVEMDAapgvdLSRILSEMRDQYEKMAEKNRKDAEDWffsktEELNREVATNSELVQSGKSEISELRRTMQALEIE 231
Cdd:TIGR02168  347 -EELKEELES-----LEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958657467  232 LQSQLSMKASLEGSLAETEnrycvqLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 307
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
92-300 1.20e-06

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: 49.76  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  92 ETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKK---NHEEEMNALRGQVGgEINVEMDAapgvdLS 168
Cdd:COG4942    24 EAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKEIAE-----LR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 169 RILSEMRDQYEKMAEK----NRKDAEDWFFSKTE--ELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASL 242
Cdd:COG4942    97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958657467 243 EGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 300
Cdd:COG4942   177 EALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-307 3.11e-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: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 108 LRRVLDELTLARADLEMQIENLKEELAylkkNHEEEMNALRGQVGGeINVEMDAApgvDLSRILSEMRDQYEKmAEKNRK 187
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 188 DAEDWFFSKTEELNREVATNSELVQSgkSEISELRRTMQALEIELQSQLS--------------MKASLEGSLAETENRY 253
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytpnhpdvialraQIAALRAQLQQEAQRI 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958657467 254 cvqLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVK---TRLEQEIATYRRLLE 307
Cdd:COG3206   315 ---LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
119-316 3.72e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 45.50  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 119 RADLEMQIENLKEELAYLKKNHEEEMN-ALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAE------- 190
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIeLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 191 --DWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRY------CVQLSQIQG 262
Cdd:pfam05557  84 ylEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAseaeqlRQNLEKQQS 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958657467 263 LIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQeIATYRRLLEGEDAHLTQY 316
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELERLREHNKHL 216
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-311 2.41e-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: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  54 QTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADI--------------NGLRRVLDELTLAR 119
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleqdiarleerrRELEERLEELEEEL 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 120 ADLEMQIENLKEELAYLKKNHEEEMNALRgqvggeinvemdaapgvDLSRILSEMRDQYEKMAEKNRKDAEDWffsktEE 199
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELE-----------------EAEAELAEAEEALLEAEAELAEAEEEL-----EE 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 200 LNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEME 279
Cdd:COG1196   384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE----EEEEEEEALEEAAEEEAELEEEEE 459
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958657467 280 QQNQEYKILLDVKTRLEQEIATYRRLLEGEDA 311
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAA 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
76-281 2.23e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  76 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG--- 152
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRaly 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 153 -----GEINVEMDAAPGVDLSRILsemrdQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQA 227
Cdd:COG4942   115 rlgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958657467 228 LEIELQSQLSMKASLEGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQ 281
Cdd:COG4942   190 LEALKAERQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAA 239
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
100-284 2.62e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 100 SVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKN---HEEEMNALRGQVGGEINVE-MDAAPGVDLSRILSEmr 175
Cdd:COG3883    34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGS-- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 176 dqyekmaeknrKDAEDwFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENrycv 255
Cdd:COG3883   112 -----------ESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---- 175
                         170       180
                  ....*....|....*....|....*....
gi 1958657467 256 QLSQIQGLIGSVEEQLAQLRCEMEQQNQE 284
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
74-335 5.91e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.55  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467  74 LLQIDNARLAADDFRTKFETEQALRMSVEADINglrrvLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGG 153
Cdd:pfam05483 159 LLKETCARSAEKTKKYEYEREETRQVYMDLNNN-----IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 154 EINVEMDAAPGV------------DLSRILSEMRDQYEKMAEKNRKDAEDW--FFSKTEELNREVATNSELVQSGKSEIS 219
Cdd:pfam05483 234 EINDKEKQVSLLliqitekenkmkDLTFLLEESRDKANQLEEKTKLQDENLkeLIEKKDHLTKELEDIKMSLQRSMSTQK 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657467 220 ELRRTMQAL---------EIELQSQLSMKASLEGSLAETENRYCV-----QLSQIQGLIGSVEEQLAQLRCEMEQQNQEY 285
Cdd:pfam05483 314 ALEEDLQIAtkticqlteEKEAQMEELNKAKAAHSFVVTEFEATTcsleeLLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958657467 286 KILLDVKTRLEQEIATYRRLLeGEDAHLTQYKpkepvttRQVRTIVEEVQ 335
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKIL-AEDEKLLDEK-------KQFEKIAEELK 435
 
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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