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Conserved domains on  [gi|6681183|ref|NP_031884|]
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protein diaphanous homolog 1 isoform 2 [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;
752-1128 4.57e-130

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.57  E-value: 4.57e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     752 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 831
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     832 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 911
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     912 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 991
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     992 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1071
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183    1072 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1128
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 265-455 2.03e-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: 216.76  E-value: 2.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     265 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 341
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     342 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 421
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 6681183     422 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 455
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 79-259 2.24e-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: 2.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      79 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 151
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     152 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 230
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 6681183     231 GILLLVRAMDPAVPNMMIDAAKLLSALCI 259
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 420-555 1.48e-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: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     420 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 488
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183     489 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 555
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
752-1128 4.57e-130

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.57  E-value: 4.57e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     752 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 831
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     832 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 911
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     912 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 991
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     992 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1071
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183    1072 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1128
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 753-1190 2.83e-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: 399.80  E-value: 2.83e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      753 KKVYKPEVQLRRPNWSKFVAEDLSqDCFWTKVKEdrfENNELFAKLTLAFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 832
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      833 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEE-YDDLAESEQFGVVMG 911
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      912 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 991
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      992 DTKSADQKMTLLHFLAELCENDHpevlkfpdelahvekasrvsaenlqksldqmkkqiadverdVQNFPAATDEKDKFVE 1071
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     1072 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1151
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 6681183     1152 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1190
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 265-455 2.03e-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: 216.76  E-value: 2.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     265 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 341
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     342 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 421
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 6681183     422 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 455
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 79-259 2.24e-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: 2.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      79 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 151
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     152 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 230
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 6681183     231 GILLLVRAMDPAVPNMMIDAAKLLSALCI 259
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 420-555 1.48e-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: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     420 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 488
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183     489 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 555
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 480-554 1.22e-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: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681183   480 DSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMA 554
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
46 PHA02562
endonuclease subunit; Provisional
 464-556 7.12e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183    464 KVEKSEAKATELEKKLDSELTARHELQVEMKKMeNDFEQKLQDLqgeKDALDSEKQQITA---QKQDLEAEVSKL----- 535
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSKKLLEL---KNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|...
gi 6681183    536 --TGEVAKLSKELEDAKNEMASL 556
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSEL 398
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 446-556 2.99e-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: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     446 RHLQIDIERLVDQMIDKTKVekSEAKATELEKKldSELTARH-----ELQVEMKKME---NDFEQKLQDLQGEKDALDSE 517
Cdd:pfam15921  544 RNVQTECEALKLQMAEKDKV--IEILRQQIENM--TQLVGQHgrtagAMQVEKAQLEkeiNDRRLELQEFKILKDKKDAK 619

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 6681183     518 KQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
752-1128 4.57e-130

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 403.57  E-value: 4.57e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     752 PKKVYKPEVQLRRPNWSKfVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 831
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDK-VRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     832 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMG 911
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     912 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 991
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     992 DTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVE 1071
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183    1072 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMF 1128
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 753-1190 2.83e-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: 399.80  E-value: 2.83e-128
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      753 KKVYKPEVQLRRPNWSKFVAEDLSqDCFWTKVKEdrfENNELFAKLTLAFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 832
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      833 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEE-YDDLAESEQFGVVMG 911
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      912 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLR 991
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      992 DTKSADQKMTLLHFLAELCENDHpevlkfpdelahvekasrvsaenlqksldqmkkqiadverdVQNFPAATDEKDKFVE 1071
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     1072 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1151
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 6681183     1152 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1190
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 265-455 2.03e-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: 216.76  E-value: 2.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     265 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGTS--IALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQEL 341
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSENdnVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     342 REIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 421
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 6681183     422 YKLIEECVSQIVLHKNGTDPDFKCR-HLQIDIERL 455
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 79-259 2.24e-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: 2.24e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183      79 SDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHT--SKAGMNQKESSR-----SAMMYIQELRSglrDMH 151
Cdd:pfam06371    5 DENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKD---DSI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     152 LLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEETSGNYDsrNQHEIIRCLKAFMNNKFGIKTMLETEE 230
Cdd:pfam06371   82 SSKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQEEEDLD--REYEILKCLKALMNNKFGLDHVLGHPS 159

                          170       180
                   ....*....|....*....|....*....
gi 6681183     231 GILLLVRAMDPAVPNMMIDAAKLLSALCI 259
Cdd:pfam06371  160 SIDLLVQSLDSERLKTRKLVLELLTALCL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 420-555 1.48e-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: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     420 QYYKLIEECVSQIVLHKngtdpdFKCRHLQIDIERLVDQM--------IDKTKVEKSEAKATELEKKLDS---ELTARHE 488
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681183     489 LQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 555
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 480-554 1.22e-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: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681183   480 DSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMA 554
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 446-556 1.28e-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: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183   446 RHLQIDIERLVDQMID-KTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDF---EQKLQDLQGEKDALDSEKQQI 521
Cdd:COG1196  235 RELEAELEELEAELEElEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRREL 314

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6681183   522 TAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 446-556 1.32e-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: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183   446 RHLQIDIERLVDQM-IDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDF---EQKLQDLQGEKDALDSEKQQI 521
Cdd:COG1196  249 EELEAELEELEAELaELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAEL 328

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 6681183   522 TAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:COG1196  329 EEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 446-556 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     446 RHLQI-----DIERLVDQMidkTKVEKSEAKATELEKKLDSELTARH----ELQVEMKKMENDFEQ---KLQDLQGEKDA 513
Cdd:TIGR02168  223 RELELallvlRLEELREEL---EELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEElqkELYALANEISR 299

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 6681183     514 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 501-556 2.79e-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: 2.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681183   501 EQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL 70
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 498-556 4.01e-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: 4.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6681183   498 NDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
46 PHA02562
endonuclease subunit; Provisional
 464-556 7.12e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183    464 KVEKSEAKATELEKKLDSELTARHELQVEMKKMeNDFEQKLQDLqgeKDALDSEKQQITA---QKQDLEAEVSKL----- 535
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSKKLLEL---KNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|...
gi 6681183    536 --TGEVAKLSKELEDAKNEMASL 556
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSEL 398
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 488-555 9.62e-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: 9.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6681183   488 ELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMAS 555
Cdd:COG3883  140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
462-556 9.63e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 9.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183   462 KTKVEKSEAKATELEKKLDSELTARHELQVEMKKME---NDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGE 538
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                         90
                 ....*....|....*...
gi 6681183   539 VAKLSKELEDAKNEMASL 556
Cdd:COG4372  152 LKELEEQLESLQEELAAL 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 464-554 2.45e-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: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     464 KVEKSEAKATELEKKLDSELTARHELQ---VEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVA 540
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90
                   ....*....|....
gi 6681183     541 KLSKELEDAKNEMA 554
Cdd:TIGR02168  765 ELEERLEEAEEELA 778
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 446-556 2.99e-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: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183     446 RHLQIDIERLVDQMIDKTKVekSEAKATELEKKldSELTARH-----ELQVEMKKME---NDFEQKLQDLQGEKDALDSE 517
Cdd:pfam15921  544 RNVQTECEALKLQMAEKDKV--IEILRQQIENM--TQLVGQHgrtagAMQVEKAQLEkeiNDRRLELQEFKILKDKKDAK 619

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 6681183     518 KQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
451-556 3.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183   451 DIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENdfEQKLQDLQGEKDALDSEKQQITAQKQDLEA 530
Cdd:COG4717  383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEA 460

                         90       100
                 ....*....|....*....|....*...
gi 6681183   531 EVSKL--TGEVAKLSKELEDAKNEMASL 556
Cdd:COG4717  461 ELEQLeeDGELAELLQELEELKAELREL 488
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 464-556 4.15e-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: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183   464 KVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQ------KLQDLQG------EKDALDSEKQQITAQKQDLEAE 531
Cdd:COG1579   32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEvearikKYEEQLGnvrnnkEYEALQKEIESLKRRISDLEDE 111

                         90       100
                 ....*....|....*....|....*
gi 6681183   532 VSKLTGEVAKLSKELEDAKNEMASL 556
Cdd:COG1579  112 ILELMERIEELEEELAELEAELAEL 136
PRK12704 PRK12704
phosphodiesterase; Provisional
 451-547 6.00e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681183    451 DIERLVDQMIDKTKVE--------KSEAKATELEKK--LDSELTARHElqvEMKKMENDFEQK-------LQDLQGEKDA 513
Cdd:PRK12704   35 EAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHKLRneFEKELRERRN---ELQKLEKRLLQKeenldrkLELLEKREEE 111

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6681183    514 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELE 547
Cdd:PRK12704  112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
Spc24 pfam08286
Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved ...
 514-548 6.37e-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: 6.37e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 6681183     514 LDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELED 548
Cdd:pfam08286    2 LDNEKFRLAKELNDLESELERLESELAKLKEELEE 36
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 485-556 8.01e-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: 8.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6681183   485 ARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASL 556
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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