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Conserved domains on  [gi|55956899|ref|NP_000217|]
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keratin, type I cytoskeletal 9 [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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
152-464 7.30e-119

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.77  E-value: 7.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   152 NEKSTMQELNSRLASYLDKVQALEEANNDLENKIQDWYDKKGPAaIQKNYSPYYNTIDDLKDQIVDLTVGNNKTLLDIDN 231
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   232 TRMTLDDFRIKFEMEQNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNS-GDVNVE 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   311 INVAPGKDLTKTLNDMRQEYEQLIAKNRKDIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSK 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55956899   391 KAALEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQED 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
152-464 7.30e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.77  E-value: 7.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   152 NEKSTMQELNSRLASYLDKVQALEEANNDLENKIQDWYDKKGPAaIQKNYSPYYNTIDDLKDQIVDLTVGNNKTLLDIDN 231
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   232 TRMTLDDFRIKFEMEQNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNS-GDVNVE 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   311 INVAPGKDLTKTLNDMRQEYEQLIAKNRKDIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSK 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55956899   391 KAALEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQED 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
250-430 1.11e-06

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: 51.99  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    250 RQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMAL----KKNHKEEMSQLTGQnSGDVNVEI-----NVAPGKDLT 320
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEK-IGELEAEIaslerSIAEKEREL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    321 KTLNDMRQEYEQLIAKNRKDIEnQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLED 400
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 55956899    401 TKN----------RYCGQLQMIQEQISNLEAQITDVRQEI 430
Cdd:TIGR02169  397 LKReinelkreldRLQEELQRLSEELADLNAAIAGIEAKI 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
255-431 3.74e-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: 49.38  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 255 ADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLtgQNSGDVNVEINVAPGKDLTKTLndMRQEYEQLI 334
Cdd:COG4942  69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAV--RRLQYLKYL 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 335 AKNRKDIENQYETQITQIEHEVsssgQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLEDTKNRYCGQLQMIQE 414
Cdd:COG4942 145 APARREQAEELRADLAELAALR----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
                       170
                ....*....|....*..
gi 55956899 415 QISNLEAQITDVRQEIE 431
Cdd:COG4942 221 EAEELEALIARLEAEAA 237
46 PHA02562
endonuclease subunit; Provisional
257-455 2.64e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  257 INGLRQVLDNLTMEKSDLEMQ---YETLQEELMALKKN-----------HKEEMSQLTGQNSgDVNVEIN--VAPGKDLT 320
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQiktYNKNIEEQRKKNGEniarkqnkydeLVEEAKTIKAEIE-ELTDELLnlVMDIEDPS 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  321 KTLNDMRQEYEQLIAK--NRKDIENQYET---------QITQIEHEVSS---SGQEVQSSAKEVTQLRHGVQELEIELQS 386
Cdd:PHA02562 255 AALNKLNTAAAKIKSKieQFQKVIKMYEKggvcptctqQISEGPDRITKikdKLKELQHSLEKLDTAIDELEEIMDEFNE 334
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55956899  387 QLSKKAALEKSLEDTKN---RYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYH 455
Cdd:PHA02562 335 QSKKLLELKNKISTNKQsliTLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
152-464 7.30e-119

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.77  E-value: 7.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   152 NEKSTMQELNSRLASYLDKVQALEEANNDLENKIQDWYDKKGPAaIQKNYSPYYNTIDDLKDQIVDLTVGNNKTLLDIDN 231
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   232 TRMTLDDFRIKFEMEQNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNS-GDVNVE 310
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   311 INVAPGKDLTKTLNDMRQEYEQLIAKNRKDIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSK 390
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55956899   391 KAALEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQED 464
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
250-430 1.11e-06

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: 51.99  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    250 RQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMAL----KKNHKEEMSQLTGQnSGDVNVEI-----NVAPGKDLT 320
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEK-IGELEAEIaslerSIAEKEREL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    321 KTLNDMRQEYEQLIAKNRKDIEnQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLED 400
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 55956899    401 TKN----------RYCGQLQMIQEQISNLEAQITDVRQEI 430
Cdd:TIGR02169  397 LKReinelkreldRLQEELQRLSEELADLNAAIAGIEAKI 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
255-431 3.74e-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: 49.38  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 255 ADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLtgQNSGDVNVEINVAPGKDLTKTLndMRQEYEQLI 334
Cdd:COG4942  69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAV--RRLQYLKYL 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 335 AKNRKDIENQYETQITQIEHEVsssgQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLEDTKNRYCGQLQMIQE 414
Cdd:COG4942 145 APARREQAEELRADLAELAALR----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
                       170
                ....*....|....*..
gi 55956899 415 QISNLEAQITDVRQEIE 431
Cdd:COG4942 221 EAEELEALIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
253-470 1.17e-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: 48.51  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    253 VDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNSGDVNVEINVAPGKDLTKTLNDMRQEYEQ 332
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    333 LIAKNRKDIENQyETQITQIEhevsssgQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLEDTKNRYCGQLQMI 412
Cdd:TIGR02168  359 ELEELEAELEEL-ESRLEELE-------EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 55956899    413 QE-QISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQEDFESSGA 470
Cdd:TIGR02168  431 EEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
318-467 8.45e-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: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    318 DLTKTLNDMRQEYEQLIAKNRK--DIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALE 395
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    396 ----------KSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQEDF 465
Cdd:TIGR02168  775 eelaeaeaeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854

                   ..
gi 55956899    466 ES 467
Cdd:TIGR02168  855 ES 856
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
245-431 1.08e-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: 44.15  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 245 MEQNLR-----QGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLtgqnsgdvnveinvapgkdl 319
Cdd:COG1579   2 MPEDLRalldlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI-------------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 320 tKTLNDMRQEYEQLIAKNRKDIEN-QYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSL 398
Cdd:COG1579  62 -KRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
                       170       180       190
                ....*....|....*....|....*....|...
gi 55956899 399 EDTKNRYCGQLQMIQEQISNLEAQITDVRQEIE 431
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIP 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-415 1.88e-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: 44.66  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    155 STMQELNSRLASYLDKVQALEEANNDLENKIQDwydkkgpaaIQKNYSPYYNTIDDLKDQIV-------DLTVGNNKTLL 227
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEE---------LQKELYALANEISRLEQQKQilrerlaNLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    228 DIDNTRMTLDDFRIKFEMEQNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNSgdv 307
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN--- 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    308 NVEINVAPGKDLTKTLNDMRQEYEQLIAK----NRKDIENQYET---QITQIEHEVSSSGQEVQSSAKEVTQLRHGVQEL 380
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKleeaELKELQAELEEleeELEELQEELERLEEALEELREELEEAEQALDAA 480
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 55956899    381 EIELQSQLSKKAALEKSLEDTKNRYCGQLQMIQEQ 415
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
46 PHA02562
endonuclease subunit; Provisional
257-455 2.64e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  257 INGLRQVLDNLTMEKSDLEMQ---YETLQEELMALKKN-----------HKEEMSQLTGQNSgDVNVEIN--VAPGKDLT 320
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQiktYNKNIEEQRKKNGEniarkqnkydeLVEEAKTIKAEIE-ELTDELLnlVMDIEDPS 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  321 KTLNDMRQEYEQLIAK--NRKDIENQYET---------QITQIEHEVSS---SGQEVQSSAKEVTQLRHGVQELEIELQS 386
Cdd:PHA02562 255 AALNKLNTAAAKIKSKieQFQKVIKMYEKggvcptctqQISEGPDRITKikdKLKELQHSLEKLDTAIDELEEIMDEFNE 334
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55956899  387 QLSKKAALEKSLEDTKN---RYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYH 455
Cdd:PHA02562 335 QSKKLLELKNKISTNKQsliTLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
199-428 1.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  199 KNYSPYYNTIDDLKDQIvdltvgnnKTLLDIDNTRMTLDDFRIKFEMEQNLRQGVDADING-----LRQVLDNLTMEKSD 273
Cdd:COG4913  235 DDLERAHEALEDAREQI--------ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELAR 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  274 LEMQYETLQEELmalkKNHKEEMSQLTGQ--NSGDVNVEinvapgkDLTKTLNDMRQEYEQliaknRKDIENQYETQITQ 351
Cdd:COG4913  307 LEAELERLEARL----DALREELDELEAQirGNGGDRLE-------QLEREIERLERELEE-----RERRRARLEALLAA 370
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55956899  352 IEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAAleksledtknrycgQLQMIQEQISNLEAQITDVRQ 428
Cdd:COG4913  371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA--------------ALRDLRRELRELEAEIASLER 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
247-460 1.56e-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: 41.29  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 247 QNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNSgdvNVEINVAPGKDLTKTLNDM 326
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQ 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 327 RQEYEQLIAKNRKDIENQYETQITQiehevSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLEDTKNRYC 406
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 55956899 407 GQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEG 460
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
247-438 1.93e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 247 QNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKN----------HKEEMSQLTG---QNSGDVNVEINV 313
Cdd:COG3883  29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaeaeieeRREELGERARalyRSGGSVSYLDVL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899 314 APGKDLTKTLNdmRQEYEQLIAKNRKDIENQYETQITQIEHEvsssGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAA 393
Cdd:COG3883 109 LGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 55956899 394 LEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYS 438
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
PRK12704 PRK12704
phosphodiesterase; Provisional
317-431 2.17e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899  317 KDLTKTLNDMRQEYEQLIAKNRKDIENQYETQITQIEHEVSSSGQEVQssaKEVTQLRHGVQELEIELQ---SQLSKKAA 393
Cdd:PRK12704  27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLqkeENLDRKLE 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 55956899  394 L----EKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIE 431
Cdd:PRK12704 104 LlekrEEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
154-431 3.73e-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: 40.43  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    154 KSTMQELNSRLASYLDKVQALEEANNDLENKIQDWYDKKgpAAIQKNYSPYYNTIDDLKDQIVDLtvgnNKTLLDIDNTR 233
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI--SALRKDLARLEAEVEQLEERIAQL----SKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    234 MTLDDFRIKFEME----QNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEEL-------------MALKKNHKEEM 296
Cdd:TIGR02168  764 EELEERLEEAEEElaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlrerleslerrIAATERRLEDL 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    297 SQLTGQNSGDVnvEINVAPGKDLTKTLNDMRQEYEQLiaknrKDIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHG 376
Cdd:TIGR02168  844 EEQIEELSEDI--ESLAAEIEELEELIEELESELEAL-----LNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55956899    377 VQELEIELQSQLSKKAALEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIE 431
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
265-436 5.44e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 39.66  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   265 DNLTMEKSDLEMQYETLQEELMALKKN--HKEEMSQLTGqnsgdvnveiNVAPGKDLTKTLNDmrqeyeqLIAKNRK--- 339
Cdd:pfam13166 324 EDIESEAEVLNSQLDGLRRALEAKRKDpfKSIELDSVDA----------KIESINDLVASINE-------LIAKHNEitd 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899   340 DIENQYETQITQIEhevsssgqevqssakevtqlRHGVQELEIELQSQLSKKAALEK---SLEDTKNRYCGQLQMIQEQI 416
Cdd:pfam13166 387 NFEEEKNKAKKKLR--------------------LHLVEEFKSEIDEYKDKYAGLEKainSLEKEIKNLEAEIKKLREEI 446
                         170       180
                  ....*....|....*....|
gi 55956899   417 SNLEAQITDVRQEIECQNQE 436
Cdd:pfam13166 447 KELEAQLRDHKPGADEINKL 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
327-468 6.88e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55956899    327 RQEYEQLIAKNRKDIENQyETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKsledtknryc 406
Cdd:TIGR02168  672 ILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---------- 740
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55956899    407 gQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQEDFESS 468
Cdd:TIGR02168  741 -EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
 
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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