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Conserved domains on  [gi|312836823|ref|NP_001186133|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform 6 [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 2.95e-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: 228.65  E-value: 2.95e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312836823   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 3.51e-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: 3.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836823  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 3.17e-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: 3.17e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823   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 1.21e-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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836823   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 2.95e-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: 228.65  E-value: 2.95e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312836823   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 3.51e-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: 3.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836823  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 3.17e-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: 3.17e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823   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 312836823   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 2.29e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717   319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717   393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                         170
                  ....*....|....*...
gi 312836823  178 KLHQLSGSDQLEATAHSR 195
Cdd:COG4717   461 ELEQLEEDGELAELLQEL 478
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 1.18e-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: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 312836823   140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-535 1.21e-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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836823   482 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:TIGR02168  742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 435-628 2.06e-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: 45.88  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 514
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   515 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 592
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 312836823   593 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 628
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
957-1154 2.76e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  957 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1029
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823 1030 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1102
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836823 1103 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1154
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 3.54e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918  224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312836823  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 6.95e-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: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  405 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 484
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312836823  485 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 519
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 384-514 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  384 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 463
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312836823  464 AEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 514
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-538 2.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  395 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 460
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823  461 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 538
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 394-516 5.11e-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: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   394 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 464
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 312836823   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 5.37e-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: 5.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836823  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 2.95e-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: 228.65  E-value: 2.95e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744    1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312836823   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 3.51e-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: 3.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   940 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 1017
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  1018 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 1097
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836823  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 3.17e-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: 3.17e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823   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 312836823   27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445    21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-195 2.29e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717   319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717   393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460

                         170
                  ....*....|....*...
gi 312836823  178 KLHQLSGSDQLEATAHSR 195
Cdd:COG4717   461 ELEQLEEDGELAELLQEL 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-162 3.58e-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: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   61 LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ---TRVESLESQTRQLELKAKN 137
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRE 313

                          90       100
                  ....*....|....*....|....*
gi 312836823  138 YADQISRLEEREAELKKEYNALHQR 162
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEE 338
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-200 4.84e-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: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   31 IYREFERLIGRYDEevvkelmplVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFED 108
Cdd:COG4913   260 LAERYAAARERLAE---------LEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  109 SQEQ----EKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSG 184
Cdd:COG4913   331 QIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                         170
                  ....*....|....*...
gi 312836823  185 SDQLEA--TAHSRIRKER 200
Cdd:COG4913   411 EAALRDlrRELRELEAEI 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-159 1.16e-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: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196   260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                          90
                  ....*....|....*..
gi 312836823  143 SRLEEREAELKKEYNAL 159
Cdd:COG1196   340 EELEEELEEAEEELEEA 356
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 67-176 1.18e-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: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 312836823   140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523  440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-535 1.21e-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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168  298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEAT 191
Cdd:TIGR02168  376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   192 AHSRIRKERpislgifPLPAGDGLLTPDTQKGGETPGSEQWKFQELsqpRSHTSLKDELSDISQGGSKATTPASTANSDV 271
Cdd:TIGR02168  453 QEELERLEE-------ALEELREELEEAEQALDAAERELAQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGIL 522

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   272 SAIppdtpskednegfvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSG 345
Cdd:TIGR02168  523 GVL---------------SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKG 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   346 YKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIG----------DVDEGADLLGMGREVENLILENTQLL-------- 407
Cdd:TIGR02168  584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVrpggvitg 663

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   408 -ETKNALNVVKNDliAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 481
Cdd:TIGR02168  664 gSAKTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 312836823   482 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:TIGR02168  742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-200 1.82e-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: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312836823  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 2.06e-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: 45.88  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 514
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   515 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 592
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 312836823   593 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 628
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
957-1154 2.76e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  957 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1029
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823 1030 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1102
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836823 1103 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1154
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-178 3.54e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918  224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312836823  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 6.94e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   28 AGSIYREFERLIGRYDEEVVKELM-PLVVAVLENLDsvfAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEF 106
Cdd:COG3206   238 AEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLA---ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312836823  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 6.95e-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: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  405 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 484
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312836823  485 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 519
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-166 7.16e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   59 ENLDSVFAQDQEHQVELELLRDDNEQLitqYEREKALRKHAEEKFIEFEDSQEqEKKDLQTRVESLESQTRQLELKAKNY 138
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADDL---EERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDA 403

                          90       100
                  ....*....|....*....|....*...
gi 312836823  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 7.86e-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: 7.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    55 VAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-------YEREkaLRKHAE---------EKFIEFEDSQEQEKKDLQ 118
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIareaqqnYERE--LVLHAEdikalqalrEELNELKAEIAELKAEAE 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 312836823   119 TRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQR 162
Cdd:pfam07926   82 SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-516 9.65e-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: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  146 EEREAELKKEYNALHQRHTEMIHnyMEHLERTKLHQLSGSDQLEATAHSRIRKERpislgifplpagdglltpdtqkgge 225
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLER--LEEELEELEEALAELEEEEEEEEEALEEAA------------------------- 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  226 tpgSEQWKFQELSQpRSHTSLKDELSDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFVKGTDTSNKSEISKHIEV 305
Cdd:COG1196   449 ---EEEAELEEEEE-ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  306 QVAQETR---NVSTESGENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGD 382
Cdd:COG1196   525 AVAVLIGveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  383 VDEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKA 462
Cdd:COG1196   605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 312836823  463 RAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVR 516
Cdd:COG1196   685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 65-165 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   65 FAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQ 141
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEER 310

                          90       100
                  ....*....|....*....|....
gi 312836823  142 ISRLEEREAELKKEYNALHQRHTE 165
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEE 334
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 384-514 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  384 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 463
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312836823  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 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   53 LVVAVLENLDSVFAQDQEHQVELELlrDDNEQLITQYEREKAlrkhaeekfiefedSQEQEKKDLQTRVESLESQTRQLE 132
Cdd:COG4942     5 LLLALLLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 312836823  133 LKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHL 174
Cdd:COG4942    69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 34-176 1.87e-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: 1.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    34 EFERLIGRYDEEVvKELMPLvvavLENLDsvfaqDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDS---Q 110
Cdd:pfam06160  234 NVDKEIQQLEEQL-EENLAL----LENLE-----LDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYlehA 303

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   111 EQEKKDLQTRVESLeSQTRQL---EL-KAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLER 176
Cdd:pfam06160  304 EEQNKELKEELERV-QQSYTLnenELeRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 435-476 1.90e-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: 1.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836823  435 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 476
Cdd:COG0711    37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 50-159 2.21e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.22  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   50 LMP------LVVAVLENLDSVFAQDQEHQ-VELELLRDDNEQLITQYEREKA---------LRKHAEEKFIEFEDSQEQE 113
Cdd:PRK05771    1 LAPvrmkkvLIVTLKSYKDEVLEALHELGvVHIEDLKEELSNERLRKLRSLLtklsealdkLRSYLPKLNPLREEKKKVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 312836823  114 KKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNAL 159
Cdd:PRK05771   81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-177 2.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   32 YREFERLIGRYDEEVVKELMplvvAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAE--EKFIEFEDs 109
Cdd:COG4717    55 ADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP- 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836823  110 QEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAE---LKKEYNALHQRHTEMIHNYMEHLERT 177
Cdd:COG4717   130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElaeLQEELEELLEQLSLATEEELQDLAEE 200
Filament pfam00038
Intermediate filament protein;
72-194 2.59e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 41.44  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    72 QVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLesqTRQLELKAKNYADQISRLEE- 147
Cdd:pfam00038   74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKNHEEEVRELQAq 150

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312836823   148 -------------REAELKKEYNALHQRHTEMIHNYMEHLE---RTKLHQLsgsdQLEATAHS 194
Cdd:pfam00038  151 vsdtqvnvemdaaRKLDLTSALAEIRAQYEEIAAKNREEAEewyQSKLEEL----QQAAARNG 209
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
395-538 2.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  395 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 460
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823  461 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 538
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
PRK12704 PRK12704
phosphodiesterase; Provisional
 66-190 2.82e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   66 AQDQEHQVELELlRDDNEQLITQYEREKALRKhaeekfiefEDSQEQEKKdLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:PRK12704   51 AEAIKKEALLEA-KEEIHKLRNEFEKELRERR---------NELQKLEKR-LLQKEENLDRKLELLEKREEELEKKEKEL 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 312836823  146 EEREAELKKEYNALHQRHTEmihnymehlERTKLHQLSGSDQLEA 190
Cdd:PRK12704  120 EQKQQELEKKEEELEELIEE---------QLQELERISGLTAEEA 155
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 394-535 2.83e-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: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823  394 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 473
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312836823  474 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 535
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-513 3.38e-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: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   306 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELS-------SAG 376
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   377 SGLIGDVDEGADLLGMGREVENLILENTQLLEtknALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 456
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 312836823   457 EELRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 513
Cdd:TIGR02168  901 EELRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 65-182 3.86e-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: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   65 FAQDQEHqVELELLRDDNE--------QLITQYEREKALRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAK 136
Cdd:COG4026    96 LGHDVEY-VDVELVRKEIKnaiiraglKSLQNIPEYNELREELLELKEKIDEIA-KEKEKLTKENEELESELEELREEYK 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 312836823  137 NYADQISRLEEREAELKKEYNALHQRHTEMIHNymEHLERTKLHQL 182
Cdd:COG4026   174 KLREENSILEEEFDNIKSEYSDLKSRFEELLKK--RLLEVFSLEEL 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 69-200 4.07e-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: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   69 QEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEER 148
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 312836823  149 EAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKER 200
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
66-162 4.90e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135

                          90       100
                  ....*....|....*....|...
gi 312836823  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 5.11e-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: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   394 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 464
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 312836823   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 5.37e-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: 5.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836823  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 6.59e-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: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    74 ELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ----------TRVESLESQTRQLELKAKNYADQIS 143
Cdd:TIGR04523  441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskeKELKKLNEEKKELEEKVKDLTKKIS 520

                           90
                   ....*....|..
gi 312836823   144 RLEEREAELKKE 155
Cdd:TIGR04523  521 SLKEKIEKLESE 532
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 294-472 7.12e-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: 7.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   294 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 368
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   369 fEELSSAGSGLIGDV----DEGADLLGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 443
Cdd:TIGR04523  499 -KKLNEEKKELEEKVkdltKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 312836823   444 AKLKLEDKNRELEEELRKARAEAEDARQK 472
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
 72-154 7.68e-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: 7.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    72 QVELELLRD-DNEQLITQYE------REK-ALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQIS 143
Cdd:pfam05300   66 KIKEELYKRlEQEQAKVQEElarlaeREReAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLA 145

                           90
                   ....*....|.
gi 312836823   144 RLEEREAELKK 154
Cdd:pfam05300  146 RLEEKNAEFYK 156
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 58-158 8.27e-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: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823   58 LENLDSVFAQDQEhqvELELLRDDNEQLitqyEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKN 137
Cdd:COG3883   121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                          90       100
                  ....*....|....*....|.
gi 312836823  138 YADQISRLEEREAELKKEYNA 158
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAA 214
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 23-166 9.68e-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: 9.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    23 RVSGLAGSIyREFERLIGRYDEEVV------KELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-YEREKAL 95
Cdd:pfam07888   74 QRRELESRV-AELKEELRQSREKHEeleekyKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETEL 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    96 RKHAE--EKFIEFEDSQEQEKKDLQTRVESLESQTRQLEL---KAKNYADQ----ISRLEEREAELKKEYNALHQRHTEM 166
Cdd:pfam07888  153 ERMKEraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKEAEN 232
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 60-166 9.74e-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: 9.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836823    60 NLDSVFAQDQEHQVELELLRDDNEQLITQYERE---------------KALRKHAEEKFIEFEDSQEQEKKDLQTrVESL 124
Cdd:TIGR04523  311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQE-IKNL 389

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 312836823   125 ESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:TIGR04523  390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
 
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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