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Conserved domains on  [gi|807066382|ref|NP_001292909|]
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protein diaphanous homolog 1 isoform 1 [Mus musculus]

Protein Classification

formin homology family protein( domain architecture ID 10273102)

formin homology family protein is a cytoskeletal remodeling protein that may be involved a diverse array of cellular functions including the regulation of actin dynamics as well as the stability and organization of microtubules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
761-1137 8.02e-130

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.19  E-value: 8.02e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   761 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 840
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   841 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 920
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   921 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 1000
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  1001 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1080
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382  1081 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1137
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 2.60e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 216.37  E-value: 2.60e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   351 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 807066382   431 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 88-268 2.44e-43

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 156.32  E-value: 2.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    88 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 160
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   161 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 239
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 807066382   240 GILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-564 1.53e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   429 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382   498 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 564
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
761-1137 8.02e-130

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.19  E-value: 8.02e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   761 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 840
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   841 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 920
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   921 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 1000
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  1001 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1080
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382  1081 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1137
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 762-1199 6.43e-128

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 399.03  E-value: 6.43e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    762 KKVYKPEVQLRRPNWSKFVAEDLSqDCFWTKVKEdrfENNELFAKLTLAFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 841
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    842 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEE-YDDLAESEQFGVVMG 920
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    921 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 1000
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   1001 DTKSADQKMTLLHFLAELCENDHpevlkfpdelahvekasrvsaenlqksldqmkkqiadverdVQNFPAATDEKDKFVE 1080
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   1081 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1160
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 807066382   1161 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1199
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 2.60e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 216.37  E-value: 2.60e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   351 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 807066382   431 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 88-268 2.44e-43

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 156.32  E-value: 2.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    88 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 160
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   161 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 239
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 807066382   240 GILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-564 1.53e-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: 49.67  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   429 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382   498 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 564
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 489-563 1.24e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807066382  489 DSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMA 563
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
46 PHA02562
endonuclease subunit; Provisional
 473-565 7.30e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  473 KVEKSEAKATELEKKLDSELTARHELQVEMKKMeNDFEQKLQDLqgeKDALDSEKQQITA---QKQDLEAEVSKL----- 544
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSKKLLEL---KNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|...
gi 807066382  545 --TGEVAKLSKELEDAKNEMASL 565
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSEL 398
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 455-565 2.96e-03

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: 42.03  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   455 RHLQIDIERLVDQMIDKTKVekSEAKATELEKKldSELTARH-----ELQVEMKKME---NDFEQKLQDLQGEKDALDSE 526
Cdd:pfam15921  544 RNVQTECEALKLQMAEKDKV--IEILRQQIENM--TQLVGQHgrtagAMQVEKAQLEkeiNDRRLELQEFKILKDKKDAK 619

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 807066382   527 KQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
761-1137 8.02e-130

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.19  E-value: 8.02e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   761 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 840
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   841 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 920
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   921 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 1000
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  1001 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1080
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382  1081 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1137
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 762-1199 6.43e-128

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 399.03  E-value: 6.43e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    762 KKVYKPEVQLRRPNWSKFVAEDLSqDCFWTKVKEdrfENNELFAKLTLAFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 841
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    842 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEE-YDDLAESEQFGVVMG 920
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    921 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 1000
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   1001 DTKSADQKMTLLHFLAELCENDHpevlkfpdelahvekasrvsaenlqksldqmkkqiadverdVQNFPAATDEKDKFVE 1080
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   1081 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1160
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 807066382   1161 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1199
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 2.60e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 216.37  E-value: 2.60e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   351 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 807066382   431 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 88-268 2.44e-43

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 156.32  E-value: 2.44e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382    88 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 160
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   161 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 239
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 807066382   240 GILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-564 1.53e-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: 49.67  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   429 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807066382   498 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 564
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 489-563 1.24e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807066382  489 DSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMA 563
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-565 1.41e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  455 RHLQIDIERLVDQMID-KTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDF---EQKLQDLQGEKDALDSEKQQI 530
Cdd:COG1196   235 RELEAELEELEAELEElEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRREL 314

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 807066382  531 TAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-565 1.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  455 RHLQIDIERLVDQM-IDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDF---EQKLQDLQGEKDALDSEKQQI 530
Cdd:COG1196   249 EELEAELEELEAELaELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAEL 328

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 807066382  531 TAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 455-565 1.74e-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: 46.20  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   455 RHLQI-----DIERLVDQMidkTKVEKSEAKATELEKKLDSELTARH----ELQVEMKKMENDFEQ---KLQDLQGEKDA 522
Cdd:TIGR02168  223 RELELallvlRLEELREEL---EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEElqkELYALANEISR 299

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 807066382   523 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 510-565 2.86e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 807066382  510 EQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL 70
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 507-565 4.04e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 4.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 807066382  507 NDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
46 PHA02562
endonuclease subunit; Provisional
 473-565 7.30e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  473 KVEKSEAKATELEKKLDSELTARHELQVEMKKMeNDFEQKLQDLqgeKDALDSEKQQITA---QKQDLEAEVSKL----- 544
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSKKLLEL---KNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|...
gi 807066382  545 --TGEVAKLSKELEDAKNEMASL 565
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSEL 398
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 497-564 9.87e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 9.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807066382  497 ELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 564
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
471-565 1.03e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  471 KTKVEKSEAKATELEKKLDSELTARHELQVEMKKME---NDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGE 547
Cdd:COG4372    72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                          90
                  ....*....|....*...
gi 807066382  548 VAKLSKELEDAKNEMASL 565
Cdd:COG4372   152 LKELEEQLESLQEELAAL 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 473-563 2.62e-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: 42.35  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   473 KVEKSEAKATELEKKLDSELTARHELQ---VEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVA 549
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90
                   ....*....|....
gi 807066382   550 KLSKELEDAKNEMA 563
Cdd:TIGR02168  765 ELEERLEEAEEELA 778
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 455-565 2.96e-03

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: 42.03  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382   455 RHLQIDIERLVDQMIDKTKVekSEAKATELEKKldSELTARH-----ELQVEMKKME---NDFEQKLQDLQGEKDALDSE 526
Cdd:pfam15921  544 RNVQTECEALKLQMAEKDKV--IEILRQQIENM--TQLVGQHgrtagAMQVEKAQLEkeiNDRRLELQEFKILKDKKDAK 619

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 807066382   527 KQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
460-565 3.49e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  460 DIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENdfEQKLQDLQGEKDALDSEKQQITAQKQDLEA 539
Cdd:COG4717   383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEA 460

                          90       100
                  ....*....|....*....|....*...
gi 807066382  540 EVSKL--TGEVAKLSKELEDAKNEMASL 565
Cdd:COG4717   461 ELEQLeeDGELAELLQELEELKAELREL 488
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 473-565 4.46e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  473 KVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQ------KLQDLQG------EKDALDSEKQQITAQKQDLEAE 540
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEvearikKYEEQLGnvrnnkEYEALQKEIESLKRRISDLEDE 111

                          90       100
                  ....*....|....*....|....*
gi 807066382  541 VSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG1579   112 ILELMERIEELEEELAELEAELAEL 136
PRK12704 PRK12704
phosphodiesterase; Provisional
 460-556 6.26e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066382  460 DIERLVDQMIDKTKVE--------KSEAKATELEKK--LDSELTARHElqvEMKKMENDFEQK-------LQDLQGEKDA 522
Cdd:PRK12704   35 EAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHKLRneFEKELRERRN---ELQKLEKRLLQKeenldrkLELLEKREEE 111

                          90       100       110
                  ....*....|....*....|....*....|....
gi 807066382  523 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELE 556
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
Spc24 pfam08286
Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved ...
 523-557 6.54e-03

Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved kinetochore-associated Ndc80 complex and is involved in chromosome segregation


Pssm-ID: 429899 [Multi-domain]  Cd Length: 107  Bit Score: 37.58  E-value: 6.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 807066382   523 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELED 557
Cdd:pfam08286    2 LDNEKFRLAKELNDLESELERLESELAKLKEELEE 36
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 494-565 8.07e-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: 40.13  E-value: 8.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807066382  494 ARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 565
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
 
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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