|
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 |
9.73e-70 |
|
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: 230.19 E-value: 9.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878980 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. |
952-1172 |
7.18e-41 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 158.26 E-value: 7.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 952 PNEQDLVREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1025
Cdd:pfam19056 80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 1026 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1105
Cdd:pfam19056 160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878980 1106 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1172
Cdd:pfam19056 238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
406-458 |
1.41e-19 |
|
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: 83.90 E-value: 1.41e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 406 MGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQA 458
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAA 53
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
27-96 |
1.09e-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: 1.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-195 |
2.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717 319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717 393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460
|
170
....*....|....*...
gi 1622878980 178 KLHQLSGSDQLESTAHSR 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 |
6.24e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622878980 140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-178 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918 224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878980 109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
971-1168 |
2.79e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 45.37 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 971 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1043
Cdd:COG3292 186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 1044 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1116
Cdd:COG3292 263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 1117 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1168
Cdd:COG3292 341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
66-363 |
2.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 140 DQISRLEEREAELKKEYNALH------QRHTEMIHNYMEHLERTKLHQlsGSDQLESTAHSRIRKERPISLGIFPLPAgD 213
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIES-L 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 214 GLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIptdtp 293
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA----- 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 294 LKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGS 363
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
|
|
|
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 |
9.73e-70 |
|
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: 230.19 E-value: 9.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878980 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. |
952-1172 |
7.18e-41 |
|
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
Pssm-ID: 465964 Cd Length: 487 Bit Score: 158.26 E-value: 7.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 952 PNEQDLVREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1025
Cdd:pfam19056 80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 1026 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1105
Cdd:pfam19056 160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878980 1106 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1172
Cdd:pfam19056 238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
406-458 |
1.41e-19 |
|
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: 83.90 E-value: 1.41e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 406 MGREVENLILENTQLLETKNALNIVKNDLIAKVDELTCEKDVLQGELEAVKQA 458
Cdd:pfam16471 1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAA 53
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
27-96 |
1.09e-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: 1.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-195 |
2.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717 319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717 393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460
|
170
....*....|....*...
gi 1622878980 178 KLHQLSGSDQLESTAHSR 195
Cdd:COG4717 461 ELEQLEEDGELAELLQEL 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-162 |
3.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 61 LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ---TRVESLESQTRQLELKAKN 137
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRE 313
|
90 100
....*....|....*....|....*
gi 1622878980 138 YADQISRLEEREAELKKEYNALHQR 162
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEE 338
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-176 |
6.24e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622878980 140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-159 |
9.60e-05 |
|
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: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90
....*....|....*..
gi 1622878980 143 SRLEEREAELKKEYNAL 159
Cdd:COG1196 340 EELEEELEEAEEELEEA 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-176 |
9.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 31 IYREFERLIGRYDEevvkelmplVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFED 108
Cdd:COG4913 260 LAERYAAARERLAE---------LEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622878980 109 SQEQ----EKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLER 176
Cdd:COG4913 331 QIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-178 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918 224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622878980 109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
971-1168 |
2.79e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 45.37 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 971 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1043
Cdd:COG3292 186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 1044 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1116
Cdd:COG3292 263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 1117 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1168
Cdd:COG3292 341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-200 |
3.22e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 146 EEREAELKKEYNALHQRHTEMIHNYMEHLE--------RTKLHQLSGSDQLESTAHSRIRKER 200
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEalraaaelAAQLEELEEAEEALLERLERLEEEL 423
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-166 |
5.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 59 ENLDSVFAQDQEHQVELELLRDDNEQLitqYEREKALRKHAEEKFIEFEDSQEqEKKDLQTRVESLESQTRQLELKAKNY 138
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDL---EERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDA 403
|
90 100
....*....|....*....|....*...
gi 1622878980 139 ADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAEL 431
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
28-166 |
8.12e-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: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 28 AGSIYREFERLIGRYDEEVVKELM-PLVVAVLENLDsvfAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEF 106
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLA---ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622878980 107 EDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLE--EREAELKKE-YNALHQRHTEM 166
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElYESLLQRLEEA 377
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-165 |
8.83e-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: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 65 FAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQ 141
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEER 310
|
90 100
....*....|....*....|....
gi 1622878980 142 ISRLEEREAELKKEYNALHQRHTE 165
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEE 334
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-192 |
9.13e-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: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQ-----------------EQEKKDLQTRVESLESQT 128
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaeaeeeleelaeelleaLRAAAELAAQLEELEEAE 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622878980 129 RQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLESTA 192
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
34-199 |
1.32e-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: 42.92 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 34 EFERLIGRYDEEVvKELMPLvvavLENLDsvfaqDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDS---Q 110
Cdd:pfam06160 234 NVDKEIQQLEEQL-EENLAL----LENLE-----LDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYlehA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 111 EQEKKDLQTRVESLeSQTRQL---EL-KAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYME---HLERTKLHQLS 183
Cdd:pfam06160 304 EEQNKELKEELERV-QQSYTLnenELeRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEileQLEEIEEEQEE 382
|
170
....*....|....*.
gi 1622878980 184 GSDQLEStahsrIRKE 199
Cdd:pfam06160 383 FKESLQS-----LRKD 393
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
53-174 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 53 LVVAVLENLDSVFAQDQEHQVELELlrDDNEQLITQYEREKAlrkhaeekfiefedSQEQEKKDLQTRVESLESQTRQLE 132
Cdd:COG4942 5 LLLALLLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622878980 133 LKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHL 174
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-177 |
1.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 32 YREFERLIGRYDEEVVKELMplvvAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAE--EKFIEFEDs 109
Cdd:COG4717 55 ADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP- 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622878980 110 QEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAE---LKKEYNALHQRHTEMIHNYMEHLERT 177
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAElaeLQEELEELLEQLSLATEEELQDLAEE 200
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
50-159 |
2.24e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 50 LMP------LVVAVLENLDSVFAQDQEHQ-VELELLRDDNEQLITQYEREKA---------LRKHAEEKFIEFEDSQEQE 113
Cdd:PRK05771 1 LAPvrmkkvLIVTLKSYKDEVLEALHELGvVHIEDLKEELSNERLRKLRSLLtklsealdkLRSYLPKLNPLREEKKKVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622878980 114 KKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNAL 159
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
55-165 |
2.82e-03 |
|
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: 39.16 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 55 VAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-------YEREkaLRKHAEekfiefeDSQEQEKkdLQTRVESLESQ 127
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIareaqqnYERE--LVLHAE-------DIKALQA--LREELNELKAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622878980 128 TRQLELKAKNYADQISRLE----EREAELKKEYNALHQRHTE 165
Cdd:pfam07926 73 IAELKAEAESAKAELEESEesweEQKKELEKELSELEKRIED 114
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
66-363 |
2.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 140 DQISRLEEREAELKKEYNALH------QRHTEMIHNYMEHLERTKLHQlsGSDQLESTAHSRIRKERPISLGIFPLPAgD 213
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEeqleslQEELAALEQELQALSEAEAEQ--ALDELLKEANRNAEKEEELAEAEKLIES-L 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 214 GLLTPDAQKGGETPGSEQWKFQELSQPRSHTSLKVSNSPEPQKAVEQEDELSDVSQGGSKATTPASTANSDVATIptdtp 293
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA----- 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 294 LKEENEGFVKVTDAPNKSEISKHIEVQVAQETRNVSTGSAENEEKSEVQAIIESTPELDMDKDLSGYKGS 363
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
65-182 |
2.89e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 65 FAQDQEHqVELELLRDDNE--------QLITQYEREKALRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAK 136
Cdd:COG4026 96 LGHDVEY-VDVELVRKEIKnaiiraglKSLQNIPEYNELREELLELKEKIDEIA-KEKEKLTKENEELESELEELREEYK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622878980 137 NYADQISRLEEREAELKKEYNALHQRHTEMIHNymEHLERTKLHQL 182
Cdd:COG4026 174 KLREENSILEEEFDNIKSEYSDLKSRFEELLKK--RLLEVFSLEEL 217
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
66-176 |
3.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELlRDDNEQLITQYEREKALRKhaeekfiefEDSQEQEKKdLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:PRK12704 51 AEAIKKEALLEA-KEEIHKLRNEFEKELRERR---------NELQKLEKR-LLQKEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110
....*....|....*....|....*....|.
gi 1622878980 146 EEREAELKKEYNALHQRHTEMIhnymEHLER 176
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQL----QELER 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-200 |
3.09e-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: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168 298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQ-LEST 191
Cdd:TIGR02168 376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEeLEEL 452
|
....*....
gi 1622878980 192 AHSRIRKER 200
Cdd:TIGR02168 453 QEELERLEE 461
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
72-193 |
3.44e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 72 QVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLesqTRQLELKAKNYADQISRLEE- 147
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKNHEEEVRELQAq 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622878980 148 -------------REAELKKEYNALHQRHTEMIHNYMEHLE---RTKLHQL-----SGSDQLESTAH 193
Cdd:pfam00038 151 vsdtqvnvemdaaRKLDLTSALAEIRAQYEEIAAKNREEAEewyQSKLEELqqaaaRNGDALRSAKE 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
74-155 |
4.44e-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: 41.54 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 74 ELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ----------TRVESLESQTRQLELKAKNYADQIS 143
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskeKELKKLNEEKKELEEKVKDLTKKIS 520
|
90
....*....|..
gi 1622878980 144 RLEEREAELKKE 155
Cdd:TIGR04523 521 SLKEKIEKLESE 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-167 |
5.01e-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: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 69 QEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEER 148
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90
....*....|....*....
gi 1622878980 149 EAELKKEYNALHQRHTEMI 167
Cdd:COG1196 357 EAELAEAEEALLEAEAELA 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
60-166 |
5.92e-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: 41.16 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 60 NLDSVFAQDQEHQVELELLRDDNEQLITQYERE---------------KALRKHAEEKFIEFEDSQEQEKKDLQTrVESL 124
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQE-IKNL 389
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622878980 125 ESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
23-166 |
7.01e-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: 40.65 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 23 RVSGLAGSIyREFERLIGRYDEEVV------KELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-YEREKAL 95
Cdd:pfam07888 74 QRRELESRV-AELKEELRQSREKHEeleekyKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 96 RKHAE--EKFIEFEDSQEQEKKDLQTRVESLESQTRQLEL---KAKNYADQ----ISRLEEREAELKKEYNALHQRHTEM 166
Cdd:pfam07888 153 ERMKEraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKEAEN 232
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
72-154 |
7.07e-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: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 72 QVELELLRD-DNEQLITQYE------REK-ALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQIS 143
Cdd:pfam05300 66 KIKEELYKRlEQEQAKVQEElarlaeREReAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLA 145
|
90
....*....|.
gi 1622878980 144 RLEEREAELKK 154
Cdd:pfam05300 146 RLEEKNAEFYK 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-200 |
8.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLElkakNYADQISRL 145
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL----EALRAAAEL 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622878980 146 EEREAELKKEYNALHQRHTEmihnyMEHLERTKLHQLSGSDQLESTAHSRIRKER 200
Cdd:COG1196 399 AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
56-162 |
8.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 56 AVLENLDSVFAQDQEHQVELELLRDDNEQLITQYERekaLRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKA 135
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
90 100
....*....|....*....|....*..
gi 1622878980 136 KNYADQISRLEEREAELKKEYNALHQR 162
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
66-155 |
9.36e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.90 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622878980 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLesqtRQLELKAKNYADQISR- 144
Cdd:pfam13868 238 QQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE----KQIEEREEQRAAEREEe 313
|
90
....*....|.
gi 1622878980 145 LEEREAELKKE 155
Cdd:pfam13868 314 LEEGERLREEE 324
|
|
|