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Conserved domains on  [gi|281365807|ref|NP_001163374|]
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sunday driver, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
9-164 8.81e-67

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


:

Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 221.33  E-value: 8.81e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807     9 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 88
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807    89 LEAEDLAEQENKELATRLESVESIVRMLElkhknsLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKM 164
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
867-1118 1.37e-46

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


The actual alignment was detected with superfamily member pfam19056:

Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.21  E-value: 1.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   867 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 944
Cdd:pfam19056   92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   945 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1024
Cdd:pfam19056  172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  1025 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1102
Cdd:pfam19056  250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
                          250
                   ....*....|....*.
gi 281365807  1103 QLSFHGHRDAVKFFVS 1118
Cdd:pfam19056  314 MVSLNAHCGPVKFLVA 329
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
323-391 5.27e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


:

Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.78  E-value: 5.27e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365807   323 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 391
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
54-436 1.32e-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.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 49.33  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    54 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 127
Cdd:pfam05483  205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   128 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 196
Cdd:pfam05483  285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   197 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 275
Cdd:pfam05483  347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   276 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASS--GMGKEVENLIMENNELLATK 341
Cdd:pfam05483  415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHC 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   342 NALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 407
Cdd:pfam05483  495 DKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
                          410       420
                   ....*....|....*....|....*....
gi 281365807   408 DVPLAQRKRFTRVEMAMVLMERNQYKERL 436
Cdd:pfam05483  575 ARSIEYEVLKKEKQMKILENKCNNLKKQI 603
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
9-164 8.81e-67

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 221.33  E-value: 8.81e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807     9 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 88
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807    89 LEAEDLAEQENKELATRLESVESIVRMLElkhknsLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKM 164
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
867-1118 1.37e-46

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.21  E-value: 1.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   867 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 944
Cdd:pfam19056   92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   945 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1024
Cdd:pfam19056  172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  1025 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1102
Cdd:pfam19056  250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
                          250
                   ....*....|....*.
gi 281365807  1103 QLSFHGHRDAVKFFVS 1118
Cdd:pfam19056  314 MVSLNAHCGPVKFLVA 329
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
323-391 5.27e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.78  E-value: 5.27e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365807   323 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 391
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
9-84 6.06e-10

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 56.83  E-value: 6.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807    9 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 84
Cdd:cd14445    18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
54-436 1.32e-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: 49.33  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    54 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 127
Cdd:pfam05483  205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   128 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 196
Cdd:pfam05483  285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   197 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 275
Cdd:pfam05483  347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   276 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASS--GMGKEVENLIMENNELLATK 341
Cdd:pfam05483  415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHC 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   342 NALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 407
Cdd:pfam05483  495 DKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
                          410       420
                   ....*....|....*....|....*....
gi 281365807   408 DVPLAQRKRFTRVEMAMVLMERNQYKERL 436
Cdd:pfam05483  575 ARSIEYEVLKKEKQMKILENKCNNLKKQI 603
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
328-464 1.42e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  328 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 407
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281365807  408 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 464
Cdd:COG4372   142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
299-442 6.01e-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: 47.36  E-value: 6.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   299 NEESEENEIVT--GSWVHPGeYASSGMGKEVENLImennelLATKNALNIVK---DDLIVKVDELTGEVEIVREELNAMQ 373
Cdd:TIGR02168  639 KKLRPGYRIVTldGDLVRPG-GVITGGSAKTNSSI------LERRREIEELEekiEELEEKIAELEKALAELRKELEELE 711
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365807   374 QSRTKLRQRISELEDELKKAKEQVKQQNTEQEEndvpLAQRKRFTRVEMAMVLMERNQYKERLMELQEA 442
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEE 776
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
54-161 6.14e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    54 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 126
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 281365807   127 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 161
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
354-415 3.64e-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: 3.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365807  354 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 415
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
954-1075 1.10e-03

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 43.44  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  954 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1026
Cdd:COG3292   266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 281365807 1027 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1075
Cdd:COG3292   341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
51-150 1.56e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   51 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 128
Cdd:PRK00409  529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
                          90       100
                  ....*....|....*....|..
gi 281365807  129 RLEEREADLKKEYNKLHERYTE 150
Cdd:PRK00409  604 VKAHELIEARKRLNKANEKKEK 625
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
336-443 2.66e-03

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: 41.98  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   336 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 415
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100
                   ....*....|....*....|....*...
gi 281365807   416 RftrvEMAMVLMERNQYKERLMELQEAV 443
Cdd:TIGR02169  758 S----ELKELEARIEELEEDLHKLEEAL 781
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
353-451 8.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  353 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 422
Cdd:PRK02224  335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281365807  423 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 451
Cdd:PRK02224  415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
 
Name Accession Description Interval E-value
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
9-164 8.81e-67

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 221.33  E-value: 8.81e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807     9 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLVTQYEREKSARKQSEQKL 88
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807    89 LEAEDLAEQENKELATRLESVESIVRMLElkhknsLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKM 164
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQRD 150
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
867-1118 1.37e-46

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 175.21  E-value: 1.37e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   867 RDEPAMSSVGPTMWLGAQDGWLYVHSSVGRWHECLHRVLLPD--AVLAIVHVEARVVVALANAQLAVFRRQTDGQWDLNS 944
Cdd:pfam19056   92 RAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLLQHFTPErsPVLCLKHSPQFLFAGLVNGKVAVYARAEDGLWDPEP 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   945 YHLVTLGDrnHSIRCLCVAGERIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAGVWVSIRLDSTLRLYNT 1024
Cdd:pfam19056  172 PKLVKLGV--LPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSSIRLFHT 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  1025 HTFEHKQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWIGTSNGVIISVPLAEVQ--PKSSsdphgqmplccmANA 1102
Cdd:pfam19056  250 ETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPVPRLEgiPKIT------------GKG 313
                          250
                   ....*....|....*.
gi 281365807  1103 QLSFHGHRDAVKFFVS 1118
Cdd:pfam19056  314 MVSLNAHCGPVKFLVA 329
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
323-391 5.27e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.78  E-value: 5.27e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365807   323 MGKEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELK 391
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
9-84 6.06e-10

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


Pssm-ID: 271220 [Multi-domain]  Cd Length: 89  Bit Score: 56.83  E-value: 6.06e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807    9 VQQLAGSIYQEFERMINRYDEDVVKNLMPLLVNVLECLDASYRINQEQDVEVELLREDNEQLvtqyEREKSARKQS 84
Cdd:cd14445    18 VYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRERAQK 89
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
54-436 1.32e-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: 49.33  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    54 QEQDVEVEL---LREDNEQ---LVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHA 127
Cdd:pfam05483  205 QAENARLEMhfkLKEDHEKiqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   128 SRLEEREADLKKEynklherytelfknhvdyMERTKMLMGSTHSQMSTASERMDVS-----------RARLNPVARSSGP 196
Cdd:pfam05483  285 KELIEKKDHLTKE------------------LEDIKMSLQRSMSTQKALEEDLQIAtkticqlteekEAQMEELNKAKAA 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   197 VSYGFASLENsvmldteTICSVgSQSDDSGPPSLQNELDNLSG-TLERGAATDALQQQHHATSPQSPDsspvVPNVPTNV 275
Cdd:pfam05483  347 HSFVVTEFEA-------TTCSL-EELLRTEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVE----LEELKKIL 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   276 G-RSTTKKEQRSDNNLYQELSFQDNE-----ESEENEI------VTGSWVHPGEYASS--GMGKEVENLIMENNELLATK 341
Cdd:pfam05483  415 AeDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIhdleiqLTAIKTSEEHYLKEveDLKTELEKEKLKNIELTAHC 494
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   342 NALNIVKDDLIVKVDELTGEVEIVREELN--------------AMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 407
Cdd:pfam05483  495 DKLLLENKELTQEASDMTLELKKHQEDIInckkqeermlkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
                          410       420
                   ....*....|....*....|....*....
gi 281365807   408 DVPLAQRKRFTRVEMAMVLMERNQYKERL 436
Cdd:pfam05483  575 ARSIEYEVLKKEKQMKILENKCNNLKKQI 603
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
328-464 1.42e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  328 ENLIMENNELLATKNALNIVKDDLivkvDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEEN 407
Cdd:COG4372    66 EELEQARSELEQLEEELEELNEQL----QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281365807  408 DVPLAQRKRftrvemamvlmERNQYKERLMELQEAVRLTEILRASRTVDNLDRKSKQ 464
Cdd:COG4372   142 QSEIAEREE-----------ELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
54-445 2.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   54 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEDLAEQENKELATRLESVESIVRMLELKHKNSLEHASRLEER 133
Cdd:COG4717   142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  134 EADLKKEYNKLHERYTEL-FKNHVDYMERTKMLMGSTHSQMSTASERMDVSRARLNPVARSSGPVSYGFASLENSVMldt 212
Cdd:COG4717   222 LEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA--- 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  213 eticSVGSQSDDSGPPSLQNELDNlsgtlergAATDALQQQHHATSPQSPDSSPVVPNVPTNVgrsttKKEQRSDNNLYQ 292
Cdd:COG4717   299 ----SLGKEAEELQALPALEELEE--------EELEELLAALGLPPDLSPEELLELLDRIEEL-----QELLREAEELEE 361
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  293 ELSFQDNEESEENEIvtgswvhpgEYASSGMGKEVENLIMENNELLATKNALN-------------------IVKDDLIV 353
Cdd:COG4717   362 ELQLEELEQEIAALL---------AEAGVEDEEELRAALEQAEEYQELKEELEeleeqleellgeleelleaLDEEELEE 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  354 KVDELTGEVEIVREELNAMQQSRTKLRQRISELE-----DELKKAKEQVKQQNTEQEEndvplaqrkRFTRVEMAMVLME 428
Cdd:COG4717   433 ELEELEEELEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRELAE---------EWAALKLALELLE 503
                         410       420
                  ....*....|....*....|.
gi 281365807  429 --RNQYKERLME--LQEAVRL 445
Cdd:COG4717   504 eaREEYREERLPpvLERASEY 524
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
299-442 6.01e-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: 47.36  E-value: 6.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   299 NEESEENEIVT--GSWVHPGeYASSGMGKEVENLImennelLATKNALNIVK---DDLIVKVDELTGEVEIVREELNAMQ 373
Cdd:TIGR02168  639 KKLRPGYRIVTldGDLVRPG-GVITGGSAKTNSSI------LERRREIEELEekiEELEEKIAELEKALAELRKELEELE 711
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281365807   374 QSRTKLRQRISELEDELKKAKEQVKQQNTEQEEndvpLAQRKRFTRVEMAMVLMERNQYKERLMELQEA 442
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEE 776
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
54-161 6.14e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 6.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    54 QEQDVEVELLREDNEQLVTQYEREKSARKQSEQKLLEAEdlaeQENKELATRLESVESIVRMLELKHKNSLE-------H 126
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIERLKEtiiknnsE 441
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 281365807   127 ASRLEEREADLKKEYNKLhERYTELFKNHVDYMER 161
Cdd:TIGR04523  442 IKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSR 475
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
349-444 2.40e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  349 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLME 428
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE----ELESLQEE 109
                          90
                  ....*....|....*.
gi 281365807  429 RNQYKERLMELQEAVR 444
Cdd:COG4372   110 AEELQEELEELQKERQ 125
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-447 3.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  354 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENdvpLAQRKRFTRVEMAMVLMERNQYK 433
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLE 365
                          90
                  ....*....|....
gi 281365807  434 ERLMELQEAVRLTE 447
Cdd:COG4913   366 ALLAALGLPLPASA 379
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
354-415 3.64e-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: 3.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281365807  354 KVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 415
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
356-456 4.12e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 43.98  E-value: 4.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   356 DELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRVEMAmvlmernQYKER 435
Cdd:pfam09787   50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELE-------RLQEE 122
                           90       100
                   ....*....|....*....|.
gi 281365807   436 LMELQEAVRLTEILRASRTVD 456
Cdd:pfam09787  123 LRYLEEELRRSKATLQSRIKD 143
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
17-186 4.33e-04

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: 44.46  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    17 YQEFERMINRYDEDVvKNLMPLLVNvLECLDASYRInqeQDVEVELlrednEQLVTQYEREKSARKQSEQKLLEAEDL-- 94
Cdd:pfam06160  232 HLNVDKEIQQLEEQL-EENLALLEN-LELDEAEEAL---EEIEERI-----DQLYDLLEKEVDAKKYVEKNLPEIEDYle 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    95 -AEQENKELATRLESVESIVRMLElkhkNSLEHASRLEEREADLKKEYNKLHER-------YTELfKNHVDYMERTKMLM 166
Cdd:pfam06160  302 hAEEQNKELKEELERVQQSYTLNE----NELERVRGLEKQLEELEKRYDEIVERleekevaYSEL-QEELEEILEQLEEI 376
                          170       180
                   ....*....|....*....|..
gi 281365807   167 GSTHSQM--STASERMDVSRAR 186
Cdd:pfam06160  377 EEEQEEFkeSLQSLRKDELEAR 398
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
954-1075 1.10e-03

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 43.44  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  954 NHSIRCLCVAGE-----RIWAAHRNK-IFIVDPVSLNIVHsLDAHPRKESQVRQMAATGAG-VWVSIRlDSTLRLYNtht 1026
Cdd:COG3292   266 GNSVRSIAEDSDgnlwiRLWIGTYGGgLFRLDPKTGKFKR-YNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD--- 340
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 281365807 1027 fehKQDVDIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWIGTSNGVII 1075
Cdd:COG3292   341 ---PKTGKFTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
51-150 1.56e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   51 RINQEQDV-EVELLREDNEQLVTQYEREKSARKQSEQKLLEAedlAEQE-NKELATRLESVESIVRmlELKHKNSLEHAS 128
Cdd:PRK00409  529 ERELEQKAeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEaQQAIKEAKKEADEIIK--ELRQLQKGGYAS 603
                          90       100
                  ....*....|....*....|..
gi 281365807  129 RLEEREADLKKEYNKLHERYTE 150
Cdd:PRK00409  604 VKAHELIEARKRLNKANEKKEK 625
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
325-406 1.89e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  325 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 404
Cdd:COG1340    22 EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKEL 101

                  ..
gi 281365807  405 EE 406
Cdd:COG1340   102 AE 103
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
953-1075 2.03e-03

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 42.28  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  953 RNHSIRCLCVAGE-RIWAAHRNKIFIVDPVSLNIVHSLDAHPRKESQVRQMAATGAG-VWVSirLDSTLRLYN--THTFE 1028
Cdd:COG3292    79 PSNYIRALLEDSDgRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGnIWVG--TSNGLYRYDpkTGKFK 156
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281365807 1029 HKQDVDIEPYVSKMLGTGKLGfsfvriTALMVSCNRLWIGT-SNGVII 1075
Cdd:COG3292   157 RFTLDGLPSNTITSLAEDADG------NLWVDSDGNLWIGTdGNGLYR 198
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-451 2.05e-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: 42.06  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  333 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLA 412
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 281365807  413 QRKRftrvemAMVLMERNQYKERLM---ELQEAVRLTEILRA 451
Cdd:COG4942   108 ELLR------ALYRLGRQPPLALLLspeDFLDAVRRLQYLKY 143
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
325-400 2.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807  325 KEVENLIMENNELLATKNALNivkddliVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQ 400
Cdd:COG3883    23 KELSELQAELEAAQAELDALQ-------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
328-461 2.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  328 ENLIMENNELLATKNALNIVKDD---LIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQ 404
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281365807  405 EENDVPLAQR-KRFTRVEMAMVLMERNQYKERLMELQEAVRLTEILRASRTVDNLDRK 461
Cdd:COG4372   167 AALEQELQALsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
336-443 2.66e-03

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: 41.98  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   336 ELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRK 415
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100
                   ....*....|....*....|....*...
gi 281365807   416 RftrvEMAMVLMERNQYKERLMELQEAV 443
Cdd:TIGR02169  758 S----ELKELEARIEELEEDLHKLEEAL 781
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
107-179 3.56e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.57  E-value: 3.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281365807   107 ESVESIVRMLELKHKNSLEHASRLEEREADLKKEYNKLHERYTELFKNHVDYMERTKMLMGSTHSQM--STASER 179
Cdd:pfam10168  557 EEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLNSQLpvLSDAER 631
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
342-463 3.99e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.82  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   342 NALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQRKRFTRve 421
Cdd:pfam12718    3 NSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR-- 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 281365807   422 mamvlmeRNQYKERlmELQEAVR----LTEILR-ASRTVDNLDRKSK 463
Cdd:pfam12718   81 -------KIQLLEE--ELEESDKrlkeTTEKLReTDVKAEHLERKVQ 118
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
19-162 4.06e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807   19 EFERMINRYDEDVVKNLmPLLVNvLECLDASYrinqeqdvEVELLREDNEQLVTQYEREKSARKQSEQK---LLEAEDLA 95
Cdd:PRK04778  253 DIEKEIQDLKEQIDENL-ALLEE-LDLDEAEE--------KNEEIQERIDQLYDILEREVKARKYVEKNsdtLPDFLEHA 322
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281365807   96 EQENKELATRLESVesiVRMLELKHkNSLEHASRLEEREADLKKEYNKLHER-------YTELfKNHVDYMERT 162
Cdd:PRK04778  323 KEQNKELKEEIDRV---KQSYTLNE-SELESVRQLEKQLESLEKQYDEITERiaeqeiaYSEL-QEELEEILKQ 391
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
349-414 4.41e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 4.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807  349 DDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQR 414
Cdd:COG3883    26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
325-444 4.43e-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: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  325 KEVENLIMENNELLATKNALNIVKDDLIVKVDELTGEVEIVRE----------------ELNAMQQSRTKLRQRISELED 388
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeeqlgnvrnnkEYEALQKEIESLKRRISDLED 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281365807  389 ELKKAKEQVKQQNTEQEENDVPLAQRKRftrvEMAMVLMERNQYKERLMELQEAVR 444
Cdd:COG1579   111 EILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELE 162
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-181 7.14e-03

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: 40.82  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807     3 EQVVSIVQQLAGSIYQEFERMINRYDEDVVKNLMPLlvnvlecldasyrinqeQDVEVELLREDNEQlvtQYEREKSARK 82
Cdd:TIGR02169  779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL-----------------REIEQKLNRLTLEK---EYLEKEIQEL 838
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807    83 QSEQKLLEA-EDLAEQENKELATRLESVESIVRMLELKHKNslehasrLEEREADLKKEYNKLHERYTELFKNHVDY--- 158
Cdd:TIGR02169  839 QEQRIDLKEqIKSIEKEIENLNGKKEELEEELEELEAALRD-------LESRLGDLKKERDELEAQLRELERKIEELeaq 911
                          170       180
                   ....*....|....*....|...
gi 281365807   159 MERTKMLMGSTHSQMSTASERMD 181
Cdd:TIGR02169  912 IEKKRKRLSELKAKLEALEEELS 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
353-451 8.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281365807  353 VKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTEQEENDVPLAQ-RKRFTRVE---------M 422
Cdd:PRK02224  335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElRERFGDAPvdlgnaedfL 414
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281365807  423 AMVLMERNQYKERLMEL-------QEAVRLTEILRA 451
Cdd:PRK02224  415 EELREERDELREREAELeatlrtaRERVEEAEALLE 450
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
333-403 8.22e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 8.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281365807  333 ENNELLATKNALNIVKDDLIVKVDELTGEVEIVREELNAMQQSRTKLRQRISELEDELKKAKEQVKQQNTE 403
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
 
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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