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Conserved domains on  [gi|70887772|ref|NP_081845|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform 1 [Mus musculus]

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 ...
 24-178 2.78e-69

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: 229.04  E-value: 2.78e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887772    104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 940-1158 3.40e-41

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: 159.41  E-value: 3.40e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887772   1098 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1158
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 392-460 3.11e-25

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: 100.08  E-value: 3.11e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887772    392 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 460
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-535 1.14e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887772    482 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:TIGR02168  742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
 
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 ...
 24-178 2.78e-69

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: 229.04  E-value: 2.78e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887772    104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 940-1158 3.40e-41

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 159.41  E-value: 3.40e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887772   1098 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1158
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 392-460 3.11e-25

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: 100.08  E-value: 3.11e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887772    392 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 460
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 27-96 1.11e-09

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: 56.45  E-value: 1.11e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445   21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 1.99e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717  319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717  393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                        170
                 ....*....|....*...
gi 70887772  178 KLHQLSGSDQLEATAHSR 195
Cdd:COG4717  461 ELEQLEEDGELAELLQEL 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-535 1.14e-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: 46.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887772    482 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:TIGR02168  742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 1.33e-04

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: 46.55  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 70887772    140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 435-628 2.27e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 514
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    515 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 592
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 70887772    593 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 628
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
957-1154 2.73e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  957 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1029
Cdd:COG3292  186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772 1030 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1102
Cdd:COG3292  263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 70887772 1103 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1154
Cdd:COG3292  341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 3.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918  224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887772   109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
405-519 6.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  405 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 484
Cdd:COG4913  266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 70887772  485 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 519
Cdd:COG4913  344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 384-514 1.14e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  384 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 463
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 70887772  464 AEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 514
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
388-538 2.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   388 DLLGMGREVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNR 453
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIR 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   454 ELEEELRKARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQE 532
Cdd:PRK03918  263 ELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELE 334


                  ....*.
gi 70887772   533 KKRSSI 538
Cdd:PRK03918  335 EKEERL 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 394-516 4.93e-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: 41.20  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    394 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 464
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 70887772    465 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 516
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 435-476 5.26e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 5.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 70887772  435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 476
Cdd:cd06503   36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
 
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 ...
 24-178 2.78e-69

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: 229.04  E-value: 2.78e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887772    104 IEFEDSQEQEKKDLQTRVESLESQTRQLElkaknyADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTK 178
Cdd:pfam09744   81 EEIEDQWEQETKDLLSQVESLEEENRRLE------ADHVSRLEEKEAELKKEYSKLHERETEVLRKLKEVVDRQR 149
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 940-1158 3.40e-41

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 159.41  E-value: 3.40e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887772   1098 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1158
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 392-460 3.11e-25

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: 100.08  E-value: 3.11e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887772    392 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 460
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
RILP-like cd14445
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
 27-96 1.11e-09

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: 56.45  E-value: 1.11e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445   21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 1.99e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717  319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717  393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                        170
                 ....*....|....*...
gi 70887772  178 KLHQLSGSDQLEATAHSR 195
Cdd:COG4717  461 ELEQLEEDGELAELLQEL 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-162 3.31e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   61 LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ---TRVESLESQTRQLELKAKN 137
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRE 313

                         90       100
                 ....*....|....*....|....*
gi 70887772  138 YADQISRLEEREAELKKEYNALHQR 162
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEE 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-200 4.39e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   31 IYREFERLIGRYDEevvkelmplVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFED 108
Cdd:COG4913  260 LAERYAAARERLAE---------LEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  109 SQEQ----EKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSG 184
Cdd:COG4913  331 QIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                        170
                 ....*....|....*...
gi 70887772  185 SDQLEA--TAHSRIRKER 200
Cdd:COG4913  411 EAALRDlrRELRELEAEI 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-159 1.10e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90
                 ....*....|....*..
gi 70887772  143 SRLEEREAELKKEYNAL 159
Cdd:COG1196  340 EELEEELEEAEEELEEA 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-535 1.14e-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: 46.59  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887772    482 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:TIGR02168  742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 1.33e-04

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: 46.55  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 70887772    140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-200 1.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887772  146 EEREAELKKEYNALHQRHTEMIHNYMEHLE--------RTKLHQLSGSDQLEATAHSRIRKER 200
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEELLEalraaaelAAQLEELEEAEEALLERLERLEEEL 423
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 435-628 2.27e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 514
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    515 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 592
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 70887772    593 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 628
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
957-1154 2.73e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  957 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1029
Cdd:COG3292  186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772 1030 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1102
Cdd:COG3292  263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 70887772 1103 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1154
Cdd:COG3292  341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 3.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918  224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 70887772   109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
28-166 5.99e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   28 AGSIYREFERLIGRYDEEVVKELM-PLVVAVLENLDsvfAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEF 106
Cdd:COG3206  238 AEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLA---ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887772  107 EDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLE--EREAELKKE-YNALHQRHTEM 166
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElYESLLQRLEEA 377
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
405-519 6.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  405 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 484
Cdd:COG4913  266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 70887772  485 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 519
Cdd:COG4913  344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-166 7.32e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    59 ENLDSVFAQDQEHQVELELLRDDNEQLitqYEREKALRKHAEEKFIEFEDSQEqEKKDLQTRVESLESQTRQLELKAKNY 138
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADDL---EERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDA 403

                          90       100
                  ....*....|....*....|....*...
gi 70887772   139 ADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAEL 431
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 55-162 8.01e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 40.70  E-value: 8.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     55 VAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-------YEREkaLRKHAE---------EKFIEFEDSQEQEKKDLQ 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIareaqqnYERE--LVLHAEdikalqalrEELNELKAEIAELKAEAE 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 70887772    119 TRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQR 162
Cdd:pfam07926   82 SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-516 9.31e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  146 EEREAELKKEYNALHQRHTEMIHnyMEHLERTKLHQLSGSDQLEATAHSRIRKERpislgifplpagdglltpdtqkgge 225
Cdd:COG1196  396 AELAAQLEELEEAEEALLERLER--LEEELEELEEALAELEEEEEEEEEALEEAA------------------------- 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  226 tpgSEQWKFQELSQpRSHTSLKDELSDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFVKGTDTSNKSEISKHIEV 305
Cdd:COG1196  449 ---EEEAELEEEEE-ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  306 QVAQETR---NVSTESGENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGD 382
Cdd:COG1196  525 AVAVLIGveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  383 VDEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKA 462
Cdd:COG1196  605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 70887772  463 RAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVR 516
Cdd:COG1196  685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 65-165 9.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   65 FAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQ 141
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEER 310

                         90       100
                 ....*....|....*....|....
gi 70887772  142 ISRLEEREAELKKEYNALHQRHTE 165
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEE 334
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 384-514 1.14e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  384 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 463
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 70887772  464 AEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 514
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 53-174 1.51e-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: 42.44  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   53 LVVAVLENLDSVFAQDQEHQVELELlrDDNEQLITQYEREKAlrkhaeekfiefedSQEQEKKDLQTRVESLESQTRQLE 132
Cdd:COG4942    5 LLLALLLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALA 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 70887772  133 LKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHL 174
Cdd:COG4942   69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 435-476 1.83e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.16  E-value: 1.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 70887772  435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 476
Cdd:COG0711   37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 34-176 1.93e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     34 EFERLIGRYDEEVvKELMPLvvavLENLDsvfaqDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDS---Q 110
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLAL----LENLE-----LDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYlehA 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    111 EQEKKDLQTRVESLeSQTRQL---EL-KAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLER 176
Cdd:pfam06160  304 EEQNKELKEELERV-QQSYTLnenELeRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-177 2.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   32 YREFERLIGRYDEEVVKELMplvvAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAE--EKFIEFEDs 109
Cdd:COG4717   55 ADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP- 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887772  110 QEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAE---LKKEYNALHQRHTEMIHNYMEHLERT 177
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElaeLQEELEELLEQLSLATEEELQDLAEE 200
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 50-159 2.19e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    50 LMP------LVVAVLENLDSVFAQDQEHQ-VELELLRDDNEQLITQYEREKA---------LRKHAEEKFIEFEDSQEQE 113
Cdd:PRK05771    1 LAPvrmkkvLIVTLKSYKDEVLEALHELGvVHIEDLKEELSNERLRKLRSLLtklsealdkLRSYLPKLNPLREEKKKVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 70887772   114 KKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNAL 159
Cdd:PRK05771   81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
Filament pfam00038
Intermediate filament protein;
72-194 2.56e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     72 QVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLesqTRQLELKAKNYADQISRLEE- 147
Cdd:pfam00038   74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKNHEEEVRELQAq 150

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887772    148 -------------REAELKKEYNALHQRHTEMIHNYMEHLE---RTKLHQLsgsdQLEATAHS 194
Cdd:pfam00038  151 vsdtqvnvemdaaRKLDLTSALAEIRAQYEEIAAKNREEAEewyQSKLEEL----QQAAARNG 209
PRK12704 PRK12704
phosphodiesterase; Provisional
 66-190 2.65e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    66 AQDQEHQVELELlRDDNEQLITQYEREKALRKhaeekfiefEDSQEQEKKdLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:PRK12704   51 AEAIKKEALLEA-KEEIHKLRNEFEKELRERR---------NELQKLEKR-LLQKEENLDRKLELLEKREEELEKKEKEL 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 70887772   146 EEREAELKKEYNALHQRHTEmihnymehlERTKLHQLSGSDQLEA 190
Cdd:PRK12704  120 EQKQQELEKKEEELEELIEE---------QLQELERISGLTAEEA 155
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 394-535 2.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  394 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 473
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887772  474 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
388-538 2.82e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   388 DLLGMGREVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNR 453
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIR 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   454 ELEEELRKARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQE 532
Cdd:PRK03918  263 ELEERIEELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELE 334


                  ....*.
gi 70887772   533 KKRSSI 538
Cdd:PRK03918  335 EKEERL 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-513 3.31e-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: 41.97  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    306 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELS-------SAG 376
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    377 SGLIGDVDEGADLLGMGREVENLILENTQLLEtknALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 456
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 70887772    457 EELRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 513
Cdd:TIGR02168  901 EELRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-200 3.96e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   69 QEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEER 148
Cdd:COG1196  277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 70887772  149 EAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKER 200
Cdd:COG1196  357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 65-182 3.99e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   65 FAQDQEHqVELELLRDDNE--------QLITQYEREKALRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAK 136
Cdd:COG4026   96 LGHDVEY-VDVELVRKEIKnaiiraglKSLQNIPEYNELREELLELKEKIDEIA-KEKEKLTKENEELESELEELREEYK 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 70887772  137 NYADQISRLEEREAELKKEYNALHQRHTEMIHNymEHLERTKLHQL 182
Cdd:COG4026  174 KLREENSILEEEFDNIKSEYSDLKSRFEELLKK--RLLEVFSLEEL 217
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
66-162 4.76e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372   57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135

                         90       100
                 ....*....|....*....|...
gi 70887772  140 DQISRLEEREAELKKEYNALHQR 162
Cdd:COG4372  136 AQIAELQSEIAEREEELKELEEQ 158
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 394-516 4.93e-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: 41.20  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    394 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 464
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 70887772    465 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 516
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 435-476 5.26e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 5.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 70887772  435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 476
Cdd:cd06503   36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 74-155 7.28e-03

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: 40.77  E-value: 7.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     74 ELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ----------TRVESLESQTRQLELKAKNYADQIS 143
Cdd:TIGR04523  441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskeKELKKLNEEKKELEEKVKDLTKKIS 520

                           90
                   ....*....|..
gi 70887772    144 RLEEREAELKKE 155
Cdd:TIGR04523  521 SLKEKIEKLESE 532
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 72-154 8.26e-03

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 38.91  E-value: 8.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     72 QVELELLRD-DNEQLITQYE------REK-ALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQIS 143
Cdd:pfam05300   66 KIKEELYKRlEQEQAKVQEElarlaeREReAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLA 145

                           90
                   ....*....|.
gi 70887772    144 RLEEREAELKK 154
Cdd:pfam05300  146 RLEEKNAEFYK 156
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 58-158 8.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   58 LENLDSVFAQDQEhqvELELLRDDNEQLitqyEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKN 137
Cdd:COG3883  121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                         90       100
                 ....*....|....*....|.
gi 70887772  138 YADQISRLEEREAELKKEYNA 158
Cdd:COG3883  194 AEAQLAELEAELAAAEAAAAA 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 294-472 8.41e-03

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: 40.39  E-value: 8.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    294 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 368
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772    369 fEELSSAGSGLIGDV----DEGADLLGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 443
Cdd:TIGR04523  499 -KKLNEEKKELEEKVkdltKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 70887772    444 AKLKLEDKNRELEEELRKARAEAEDARQK 472
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
56-162 9.34e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772   56 AVLENLDSVFAQDQEHQVELELLRDDNEQLITQYERekaLRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKA 135
Cdd:COG4717  139 AELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                         90       100
                 ....*....|....*....|....*..
gi 70887772  136 KNYADQISRLEEREAELKKEYNALHQR 162
Cdd:COG4717  216 EEAQEELEELEEELEQLENELEAAALE 242
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 23-166 9.66e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.26  E-value: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     23 RVSGLAGSIyREFERLIGRYDEEVV------KELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-YEREKAL 95
Cdd:pfam07888   74 QRRELESRV-AELKEELRQSREKHEeleekyKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETEL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772     96 RKHAE--EKFIEFEDSQEQEKKDLQTRVESLESQTRQLEL---KAKNYADQ----ISRLEEREAELKKEYNALHQRHTEM 166
Cdd:pfam07888  153 ERMKEraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKEAEN 232
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 430-514 9.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  430 EKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDipTAQRKRFTRV--EMARVLMERNQYKER 507
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELlaELARLEQDIARLEER 310


                 ....*..
gi 70887772  508 LMELQEA 514
Cdd:COG1196  311 RRELEER 317
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 420-514 9.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887772  420 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLM 499
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         90
                 ....*....|....*
gi 70887772  500 ERNQYKERLMELQEA 514
Cdd:COG1196  324 ELAELEEELEELEEE 338
 
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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