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Conserved domains on  [gi|755516930|ref|XP_006506343|]
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non-homologous end joining factor IFFO1 isoform X7 [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
230-426 1.96e-16

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 79.96  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  230 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 309
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  310 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ----------------------------RNCEDM--------- 352
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaknreeaeewyqskleelqqaaaRNGDALrsakeeite 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  353 -----------IQMFQQQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQME 421
Cdd:pfam00038 222 lrrtiqsleieLQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301


                  ....*
gi 755516930  422 TCRRL 426
Cdd:pfam00038 302 TYRKL 306
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
230-426 1.96e-16

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 79.96  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  230 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 309
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  310 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ----------------------------RNCEDM--------- 352
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaknreeaeewyqskleelqqaaaRNGDALrsakeeite 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  353 -----------IQMFQQQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQME 421
Cdd:pfam00038 222 lrrtiqsleieLQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301


                  ....*
gi 755516930  422 TCRRL 426
Cdd:pfam00038 302 TYRKL 306
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-409 2.97e-06

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: 50.06  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   230 QIDTITPEIRALYNVLAKVKRERDEYKRRWE------EEYTVRIQ-LQERVTELQEEAQEADACQEELAMKVEQLKAELV 302
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIEeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   303 VFK---GLMSNNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ--RNCEDMIQMFQQQED---SLEKVIKDTESLF 374
Cdd:TIGR02168  800 ALRealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieELSEDIESLAAEIEEleeLIEELESELEALL 879

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 755516930   375 KTREKEyQETIDQIELELATAKNDMNRHLHEYMEM 409
Cdd:TIGR02168  880 NERASL-EEALALLRSELEELSEELRELESKRSEL 913
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-405 3.33e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  230 QIDTITPeIRALYNVLAKVKRERDEYKR-----RWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVF 304
Cdd:COG4913   250 QIELLEP-IRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  305 KGLMSNN----LTELDTKIQEKAMKVDmDICRRIDITAKLCD-------------LAQQRNCEDMIQMFQQQEDSLEKVI 367
Cdd:COG4913   329 EAQIRGNggdrLEQLEREIERLERELE-ERERRRARLEALLAalglplpasaeefAALRAEAAALLEALEEELEALEEAL 407

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 755516930  368 KDTESLFKTREKEYQETIDQIElELATAKNDMNRHLHE 405
Cdd:COG4913   408 AEAEAALRDLRRELRELEAEIA-SLERRKSNIPARLLA 444
46 PHA02562
endonuclease subunit; Provisional
 230-428 3.85e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 230 QIDTITPEIRalyNVLAKVKRERDeYKRRWEEEYTVRIQ-LQERVTELQEEAqeadacqEELAMKVEQLKAELVVFKGLM 308
Cdd:PHA02562 182 QIQTLDMKID---HIQQQIKTYNK-NIEEQRKKNGENIArKQNKYDELVEEA-------KTIKAEIEELTDELLNLVMDI 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 309 ---SNNLTELDTKIQEKAMKvdMDICRRIditAKLcdLAQQRNCEDMIQMFQQQEDSLEKVikdteslfKTREKEYQETI 385
Cdd:PHA02562 251 edpSAALNKLNTAAAKIKSK--IEQFQKV---IKM--YEKGGVCPTCTQQISEGPDRITKI--------KDKLKELQHSL 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755516930 386 DQIElelaTAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLIT 428
Cdd:PHA02562 316 EKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLI 354
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 246-391 6.94e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   246 AKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKA-------ELVVFKGL---MSNNLTEL 315
Cdd:smart00787 126 ARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDrkdaleeELRQLKQLedeLEDCDPTE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   316 DTKIQEKAMKVDMDICRRIDitaKLCDLAQQRN-CEDMIQMFQQQEDSLEKVIKDTESLFKTR-------EKEYQETIDQ 387
Cdd:smart00787 206 LDRAKEKLKKLLQEIMIKVK---KLEELEEELQeLESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKL 282


                   ....
gi 755516930   388 IELE 391
Cdd:smart00787 283 LQSL 286
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
230-426 1.96e-16

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 79.96  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  230 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 309
Cdd:pfam00038  62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  310 NNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ----------------------------RNCEDM--------- 352
Cdd:pfam00038 142 EEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQyeeiaaknreeaeewyqskleelqqaaaRNGDALrsakeeite 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  353 -----------IQMFQQQEDSLEKVIKDTESLFKTREKEYQETIDQIELELATAKNDMNRHLHEYMEMCSMKRGLDVQME 421
Cdd:pfam00038 222 lrrtiqsleieLQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301


                  ....*
gi 755516930  422 TCRRL 426
Cdd:pfam00038 302 TYRKL 306
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-409 2.97e-06

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: 50.06  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   230 QIDTITPEIRALYNVLAKVKRERDEYKRRWE------EEYTVRIQ-LQERVTELQEEAQEADACQEELAMKVEQLKAELV 302
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAqlskelTELEAEIEeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   303 VFK---GLMSNNLTELDTKIQEKAMKVDMDICRRIDITAKLCDLAQQ--RNCEDMIQMFQQQED---SLEKVIKDTESLF 374
Cdd:TIGR02168  800 ALRealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieELSEDIESLAAEIEEleeLIEELESELEALL 879

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 755516930   375 KTREKEyQETIDQIELELATAKNDMNRHLHEYMEM 409
Cdd:TIGR02168  880 NERASL-EEALALLRSELEELSEELRELESKRSEL 913
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-405 3.33e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  230 QIDTITPeIRALYNVLAKVKRERDEYKR-----RWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVF 304
Cdd:COG4913   250 QIELLEP-IRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  305 KGLMSNN----LTELDTKIQEKAMKVDmDICRRIDITAKLCD-------------LAQQRNCEDMIQMFQQQEDSLEKVI 367
Cdd:COG4913   329 EAQIRGNggdrLEQLEREIERLERELE-ERERRRARLEALLAalglplpasaeefAALRAEAAALLEALEEELEALEEAL 407

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 755516930  368 KDTESLFKTREKEYQETIDQIElELATAKNDMNRHLHE 405
Cdd:COG4913   408 AEAEAALRDLRRELRELEAEIA-SLERRKSNIPARLLA 444
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 265-426 3.63e-05

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: 46.25  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  265 VRIQLQERVTELQEEAQEADACQEE----------LAMKVEQLKAELVVFK---GLMSNNLTEL--DTKIQEKAMKVDMD 329
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKgsaenkqlnaYEIKVNKLELELASAKqkfEEIIDNYQKEieDKKISEEKLLEEVE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  330 ICRRI-DITAKL---CDLAQQRNCEDMIQMFQQQEDSLEKVIKDTES---LFKTREKEYQETIDQIELELATAKNdmnrh 402
Cdd:pfam05483 679 KAKAIaDEAVKLqkeIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSAKAALEIELSNIKA----- 753

                         170       180
                  ....*....|....*....|....
gi 755516930  403 lheymEMCSMKRGLDVQMETCRRL 426
Cdd:pfam05483 754 -----ELLSLKKQLEIEKEEKEKL 772
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 230-405 7.32e-05

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: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 230 QIDTitpEIRALYNVLAKVKRERDEYKRRWEEeytvriqLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLMS 309
Cdd:COG1579   14 ELDS---ELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 310 N--NLTELDTKIQEkamkvdmdicrrIDITAKlcdlaQQRNCEDMIQMFQQQEDSLEKVIKDTESLFKTREKEYQETIDQ 387
Cdd:COG1579   84 NvrNNKEYEALQKE------------IESLKR-----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146

                        170
                 ....*....|....*...
gi 755516930 388 IELELATAKNDMNRHLHE 405
Cdd:COG1579  147 LDEELAELEAELEELEAE 164
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 229-396 1.09e-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: 45.06  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   229 VQIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELvvfkglm 308
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI------- 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   309 sNNLTELDTKIQEKAMKVDMDICR-RIDITAKLCDLAQ-QRNCEDMIQMFQQQEDSLEKVIKDTES----LFKTREK--E 380
Cdd:TIGR02169  402 -NELKRELDRLQEELQRLSEELADlNAAIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLSKyeqeLYDLKEEydR 480

                          170
                   ....*....|....*.
gi 755516930   381 YQETIDQIELELATAK 396
Cdd:TIGR02169  481 VEKELSKLQRELAEAE 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-402 6.59e-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: 6.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   230 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKglms 309
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE---- 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   310 NNLTELDTKIQEKAMKVDmDICRRIDITAklcdlAQQRNCEDMIQMFQQQEDSLEKVIKDTE-SLFKTREKEYQETIDQI 388
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVA-QLELQIASLN-----NEIERLEARLERLEDRRERLQQEIEELLkKLEEAELKELQAELEEL 445

                          170
                   ....*....|....
gi 755516930   389 ELELATAKNDMNRH 402
Cdd:TIGR02168  446 EEELEELQEELERL 459
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 223-409 1.25e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.38  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  223 HPDGVGVQIDTITPEIRALYNVLAKVKRERDEYKRRWEEeytvriqLQERVTELQEEAQEAdacQEELamkvEQLKA--- 299
Cdd:pfam06160 257 ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPE-------IEDYLEHAEEQNKEL---KEEL----ERVQQsyt 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930  300 ----ELVVFKGL------MSNNLTELDTKIQEKAMkvdmdicRRIDITAKLcdlaqqrncEDMIQMFQQQEDSLEKVIKD 369
Cdd:pfam06160 323 lnenELERVRGLekqleeLEKRYDEIVERLEEKEV-------AYSELQEEL---------EEILEQLEEIEEEQEEFKES 386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755516930  370 TESLFKTrEKEYQETIDQIELELATAKNDM-NRHL----HEYMEM 409
Cdd:pfam06160 387 LQSLRKD-ELEAREKLDEFKLELREIKRLVeKSNLpglpESYLDY 430
46 PHA02562
endonuclease subunit; Provisional
 230-428 3.85e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 230 QIDTITPEIRalyNVLAKVKRERDeYKRRWEEEYTVRIQ-LQERVTELQEEAqeadacqEELAMKVEQLKAELVVFKGLM 308
Cdd:PHA02562 182 QIQTLDMKID---HIQQQIKTYNK-NIEEQRKKNGENIArKQNKYDELVEEA-------KTIKAEIEELTDELLNLVMDI 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 309 ---SNNLTELDTKIQEKAMKvdMDICRRIditAKLcdLAQQRNCEDMIQMFQQQEDSLEKVikdteslfKTREKEYQETI 385
Cdd:PHA02562 251 edpSAALNKLNTAAAKIKSK--IEQFQKV---IKM--YEKGGVCPTCTQQISEGPDRITKI--------KDKLKELQHSL 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755516930 386 DQIElelaTAKNDMNRHLHEYMEMCSMKRGLDVQMETCRRLIT 428
Cdd:PHA02562 316 EKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLI 354
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
230-398 4.32e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 230 QIDTITPEIRALYNVLAKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAElvvfkglms 309
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR--------- 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 310 nnltelDTKIQEkamkvdmdicrriditaklcDLAQQRNCedmIQMFQQQEDSLEKVIKDTESlfktREKEYQETIDQIE 389
Cdd:PRK02224 323 ------DEELRD--------------------RLEECRVA---AQAHNEEAESLREDADDLEE----RAEELREEAAELE 369


                 ....*....
gi 755516930 390 LELATAKND 398
Cdd:PRK02224 370 SELEEAREA 378
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 246-391 6.94e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   246 AKVKRERDEYKRRWEEEYTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKA-------ELVVFKGL---MSNNLTEL 315
Cdd:smart00787 126 ARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDrkdaleeELRQLKQLedeLEDCDPTE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   316 DTKIQEKAMKVDMDICRRIDitaKLCDLAQQRN-CEDMIQMFQQQEDSLEKVIKDTESLFKTR-------EKEYQETIDQ 387
Cdd:smart00787 206 LDRAKEKLKKLLQEIMIKVK---KLEELEEELQeLESKIEDLTNKKSELNTEIAEAEKKLEQCrgftfkeIEKLKEQLKL 282


                   ....
gi 755516930   388 IELE 391
Cdd:smart00787 283 LQSL 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-405 7.61e-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: 38.88  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   244 VLAKVKRERDEYKRRWEEEYTvriQLQERVTELQEEAQEADACQEELAMKVEQLKAELVVFKGLM---SNNLTELDTKIQ 320
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELK---EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930   321 EKAMKVDMDICRRIDITAKLCDLAQQRNC-EDMIQMFQQQEDSLEKVIKDTESLFKTREKEYQE---TIDQIELELATAK 396
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDElAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLR 385


                   ....*....
gi 755516930   397 NDMNRHLHE 405
Cdd:TIGR02168  386 SKVAQLELQ 394
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
230-429 9.05e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.97  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 230 QIDTITPEIRALYNVLAKVKRERDEYKRR---WEEE----YTVRIQLQERVTELQEEAQEADACQEELAMKVEQLKAELV 302
Cdd:COG1340    2 KTDELSSSLEELEEKIEELREEIEELKEKrdeLNEElkelAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755516930 303 VFKglmsNNLTELDTKIQEKAMKVDMDICRRIDITAKlcdlaqQRNCEDMIQMFQqqedslekvikdTESLFKTREKEYQ 382
Cdd:COG1340   82 ELN----EKLNELREELDELRKELAELNKAGGSIDKL------RKEIERLEWRQQ------------TEVLSPEEEKELV 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755516930 383 ETIDQIELELATAKnDMNRHLHEYMEMCSMKRGLDVQMETCRRLITQ 429
Cdd:COG1340  140 EKIKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKE 185
 
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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