|
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 |
3.30e-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: 3.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975810 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. |
957-1177 |
3.62e-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: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 957 PNEQDLAREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1030
Cdd:pfam19056 80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 1031 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1110
Cdd:pfam19056 160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975810 1111 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1177
Cdd:pfam19056 238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
411-479 |
3.06e-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: 3.06e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975810 411 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 479
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 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-195 |
2.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717 319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717 393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460
|
170
....*....|....*...
gi 568975810 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 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439
|
90 100 110
....*....|....*....|....*....|....*..
gi 568975810 140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
454-647 |
2.30e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 454 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 533
Cdd:pfam17380 290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 534 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 611
Cdd:pfam17380 359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434
|
170 180 190
....*....|....*....|....*....|....*...
gi 568975810 612 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 647
Cdd:pfam17380 435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
976-1173 |
2.80e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 45.37 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 976 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1048
Cdd:COG3292 186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 1049 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1121
Cdd:COG3292 263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568975810 1122 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1173
Cdd:COG3292 341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-178 |
3.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918 224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975810 109 SQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEERE---AELKKEYNALHQRHT--EMIHNYMEHLERTK 178
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELEKRLEELEERHElyEEAKAKKEELERLK 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-538 |
7.00e-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: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 424 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 503
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
|
90 100 110
....*....|....*....|....*....|....*.
gi 568975810 504 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 538
Cdd:COG4913 344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-533 |
1.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 411 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 490
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568975810 491 KAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 533
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
414-557 |
2.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 414 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 479
Cdd:PRK03918 190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975810 480 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 557
Cdd:PRK03918 270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
454-495 |
5.40e-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: 5.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568975810 454 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 495
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 |
3.30e-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: 3.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 24 VSGLAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKF 103
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975810 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. |
957-1177 |
3.62e-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: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 957 PNEQDLAREEAQK----MSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIF 1030
Cdd:pfam19056 80 PEEPEPEEEEAVRaertAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 1031 HRGVDGQWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVS 1110
Cdd:pfam19056 160 ARAEDGLWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMA 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975810 1111 IRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1177
Cdd:pfam19056 238 FSSGSSIRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
|
|
| JIP_LZII |
pfam16471 |
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ... |
411-479 |
3.06e-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: 3.06e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975810 411 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 479
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 |
1.13e-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: 1.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 27 LAGSIYREFERLIGRYDEEVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLitqyEREKALR 96
Cdd:cd14445 21 IASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRL----ELEKRER 86
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-195 |
2.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 33 REFERLIGRY--DEEVVKELMPLVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQY--EREKALRKHAEekfief 106
Cdd:COG4717 319 EELEELLAALglPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAgvEDEEELRAALE------ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 107 edsQEQEKKDLQTRVESLESQTRQLELKAKNYAD---------QISRLEEREAELKKEYNALHQRHTEMihnymehleRT 177
Cdd:COG4717 393 ---QAEEYQELKEELEELEEQLEELLGELEELLEaldeeeleeELEELEEELEELEEELEELREELAEL---------EA 460
|
170
....*....|....*...
gi 568975810 178 KLHQLSGSDQLEATAHSR 195
Cdd:COG4717 461 ELEQLEEDGELAELLQEL 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
61-162 |
3.52e-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: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 61 LDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ---TRVESLESQTRQLELKAKN 137
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRE 313
|
90 100
....*....|....*....|....*
gi 568975810 138 YADQISRLEEREAELKKEYNALHQR 162
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-200 |
4.75e-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: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 31 IYREFERLIGRYDEevvkelmplVVAVLENLDSVFAQ--DQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFED 108
Cdd:COG4913 260 LAERYAAARERLAE---------LEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 109 SQEQ----EKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSG 184
Cdd:COG4913 331 QIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
170
....*....|....*...
gi 568975810 185 SDQLEA--TAHSRIRKER 200
Cdd:COG4913 411 EAALRDlrRELRELEAEI 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-159 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90
....*....|....*..
gi 568975810 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 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 67 QDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFiefeDSQEQEKKDLQTRVESLESQTRQLE-----LKAKNY--A 139
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEkeierLKETIIknN 439
|
90 100 110
....*....|....*....|....*....|....*..
gi 568975810 140 DQISRLEEREAELKKEYNALHQRhTEMIHNYMEHLER 176
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSR 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-200 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975810 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 ... |
454-647 |
2.30e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 454 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 533
Cdd:pfam17380 290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 534 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 611
Cdd:pfam17380 359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434
|
170 180 190
....*....|....*....|....*....|....*...
gi 568975810 612 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 647
Cdd:pfam17380 435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
976-1173 |
2.80e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 45.37 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 976 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 1048
Cdd:COG3292 186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 1049 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 1121
Cdd:COG3292 263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568975810 1122 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1173
Cdd:COG3292 341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-178 |
3.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 33 REFERLIGRYDE--EVVKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEE--KFIEFED 108
Cdd:PRK03918 224 EKLEKEVKELEElkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYE 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975810 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 |
6.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 28 AGSIYREFERLIGRYDEEVVKELM-PLVVAVLENLDsvfAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEF 106
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLA---ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975810 107 EDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLE--EREAELKKE-YNALHQRHTEM 166
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARElYESLLQRLEEA 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-538 |
7.00e-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: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 424 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 503
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343
|
90 100 110
....*....|....*....|....*....|....*.
gi 568975810 504 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 538
Cdd:COG4913 344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
59-166 |
7.15e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 59 ENLDSVFAQDQEHQVELELLRDDNEQLitqYEREKALRKHAEEKFIEFEDSQEqEKKDLQTRVESLESQTRQLELKAKNY 138
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDL---EERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDA 403
|
90 100
....*....|....*....|....*...
gi 568975810 139 ADQISRLEEREAELKKEYNALHQRHTEM 166
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAEL 431
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
55-162 |
8.13e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.70 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 55 VAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-------YEREkaLRKHAE---------EKFIEFEDSQEQEKKDLQ 118
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIareaqqnYERE--LVLHAEdikalqalrEELNELKAEIAELKAEAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568975810 119 TRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQR 162
Cdd:pfam07926 82 SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
65-165 |
1.02e-03 |
|
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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 65 FAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQ 141
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEER 310
|
90 100
....*....|....*....|....
gi 568975810 142 ISRLEEREAELKKEYNALHQRHTE 165
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEE 334
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-554 |
1.15e-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: 43.51 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLESQTRQLELKAKNYADQI 142
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEeklEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 143 SRLEEREAELKKEYNALHQRhtemIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKER-PISLGIFPLPAGDGLLTPDTQ 221
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 222 KGGETPGSEQWKFQELSQPRSHTSLKVSHSPEPLKAVE-QEDELSDISQGGSKATTPASTANSDVSAIppdtpskedneg 300
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLErLQENLEGFSEGVKALLKNQSGLSGILGVL------------ 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 301 fvkGTDTSNKSEISKHIEVqVAQETRNVSTESGENEEKSEVQAIIEST------PELDmdkDLSGYKGSSTPTKGIENKA 374
Cdd:TIGR02168 526 ---SELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNElgrvtfLPLD---SIKGTEIQGNDREILKNIE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 375 FDRNTESLFEELSSAGSGLIG----------DVDEGADL---LDHNF----------------FGMGREVENLILENTQl 425
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELakkLRPGYrivtldgdlvrpggviTGGSAKTNSSILERRR- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 426 letknalnvvkndliaKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI----- 500
Cdd:TIGR02168 678 ----------------EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleae 741
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568975810 501 --PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 554
Cdd:TIGR02168 742 veQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
411-533 |
1.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 411 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 490
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568975810 491 KAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 533
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
53-174 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 53 LVVAVLENLDSVFAQDQEHQVELELlrDDNEQLITQYEREKAlrkhaeekfiefedSQEQEKKDLQTRVESLESQTRQLE 132
Cdd:COG4942 5 LLLALLLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELA--------------ALKKEEKALLKQLAALERRIAALA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568975810 133 LKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHL 174
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
320-532 |
1.75e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 320 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAgSGLIGDV 397
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANL 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 398 DEGADLLDHNFFGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE 477
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568975810 478 LRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 532
Cdd:TIGR02168 903 LRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
454-495 |
1.86e-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: 1.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568975810 454 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 495
Cdd:COG0711 37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
34-176 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 34 EFERLIGRYDEEVvKELMPLvvavLENLDsvfaqDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDS---Q 110
Cdd:pfam06160 234 NVDKEIQQLEEQL-EENLAL----LENLE-----LDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYlehA 303
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 111 EQEKKDLQTRVESLeSQTRQL---EL-KAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLER 176
Cdd:pfam06160 304 EEQNKELKEELERV-QQSYTLnenELeRVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-192 |
2.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDL---QTRVESLESQTRQLELKAKNYADQI 142
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLERL 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568975810 143 SRLEE-------REAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATA 192
Cdd:COG1196 417 ERLEEeleeleeALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
50-159 |
2.25e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 50 LMP------LVVAVLENLDSVFAQDQEHQ-VELELLRDDNEQLITQYEREKA---------LRKHAEEKFIEFEDSQEQE 113
Cdd:PRK05771 1 LAPvrmkkvLIVTLKSYKDEVLEALHELGvVHIEDLKEELSNERLRKLRSLLtklsealdkLRSYLPKLNPLREEKKKVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568975810 114 KKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNAL 159
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
32-177 |
2.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 32 YREFERLIGRYDEEVVKELMplvvAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAE--EKFIEFEDs 109
Cdd:COG4717 55 ADELFKPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLP- 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975810 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 568975810 72 QVELELLRDDNEQLITQYEREKALRKHAEEKFIEFE---DSQEQEKKDLQTRVESLesqTRQLELKAKNYADQISRLEE- 147
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRkdlDEATLARVDLEAKIESL---KEELAFLKKNHEEEVRELQAq 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975810 148 -------------REAELKKEYNALHQRHTEMIHNYMEHLE---RTKLHQLsgsdQLEATAHS 194
Cdd:pfam00038 151 vsdtqvnvemdaaRKLDLTSALAEIRAQYEEIAAKNREEAEewyQSKLEEL----QQAAARNG 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
414-557 |
2.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 414 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 479
Cdd:PRK03918 190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975810 480 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 557
Cdd:PRK03918 270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
66-190 |
2.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELlRDDNEQLITQYEREKALRKhaeekfiefEDSQEQEKKdLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:PRK12704 51 AEAIKKEALLEA-KEEIHKLRNEFEKELRERR---------NELQKLEKR-LLQKEENLDRKLELLEKREEELEKKEKEL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568975810 146 EEREAELKKEYNALHQRHTEmihnymehlERTKLHQLSGSDQLEA 190
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEE---------QLQELERISGLTAEEA 155
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-200 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRL 145
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568975810 146 EEREAELKKEYNALHQRHTEMIHnyMEHLERTKLHQLSGSDQLEATAHSRIRKER 200
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLER--LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
413-554 |
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 568975810 413 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 492
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975810 493 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 554
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
57-644 |
3.41e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 57 VLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEfeDSQEQEKKD--LQTRVESLESQTRQLELK 134
Cdd:pfam02463 270 VLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE--SEKEKKKAEkeLKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 135 AKNYA------DQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLE------------RTKLHQLSGSD----QLEATA 192
Cdd:pfam02463 348 EIKREaeeeeeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeelelkseeekeAQLLLELARQLedllKEEKKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 193 HSRIRKERPISLGIFPLPAGDGLLTPDTQKGGETPGSEQWKFQELSQPRSH-TSLKVSHSPEPLKAVEQEDELSDISQGG 271
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQlVKLQEQLELLLSRQKLEERSQKESKARS 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 272 SKATTPASTANSDVSAIPPDTPSKEDNE----------GFVKGTDTSNKSEISKHIEVQVAQETRNVSTESGENEEKSEV 341
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDLGvavenykvaiSTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 342 QAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGS-----GLIGDVDEGADLLDHNFFGMGREVE 416
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesakAKESGLRKGVSLEEGLAEKSEVKAS 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 417 NLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQG--ELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKD 494
Cdd:pfam02463 668 LSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQreKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 495 DDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQE---AVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNA 571
Cdd:pfam02463 748 EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkvEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE 827
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975810 572 TKKPEPPVNLKynaptsHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKE 644
Cdd:pfam02463 828 EKIKEEELEEL------ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-195 |
3.46e-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: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 33 REFERLIGRYDEEVvKELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEq 112
Cdd:TIGR02168 298 SRLEQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 113 ekkDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATA 192
Cdd:TIGR02168 376 ---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
...
gi 568975810 193 HSR 195
Cdd:TIGR02168 453 QEE 455
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
65-182 |
3.92e-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: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 65 FAQDQEHqVELELLRDDNE--------QLITQYEREKALRKHAEEKFIEFEDSQeQEKKDLQTRVESLESQTRQLELKAK 136
Cdd:COG4026 96 LGHDVEY-VDVELVRKEIKnaiiraglKSLQNIPEYNELREELLELKEKIDEIA-KEKEKLTKENEELESELEELREEYK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568975810 137 NYADQISRLEEREAELKKEYNALHQRHTEMIHNymEHLERTKLHQL 182
Cdd:COG4026 174 KLREENSILEEEFDNIKSEYSDLKSRFEELLKK--RLLEVFSLEEL 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-200 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 69 QEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQISRLEER 148
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568975810 149 EAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSRIRKER 200
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
66-162 |
4.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 66 AQDQEHQVELELLRDDNEQLITQyEREKALRKHAEEKFIEFEDSQEQ------EKKDLQTRVESLESQTRQLELKAKNYA 139
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQAELAQAQEEleslqeEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100
....*....|....*....|...
gi 568975810 140 DQISRLEEREAELKKEYNALHQR 162
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQ 158
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
454-495 |
5.40e-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: 5.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568975810 454 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 495
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 |
6.53e-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: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 74 ELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQEQEKKDLQ----------TRVESLESQTRQLELKAKNYADQIS 143
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEqkqkelkskeKELKKLNEEKKELEEKVKDLTKKIS 520
|
90
....*....|..
gi 568975810 144 RLEEREAELKKE 155
Cdd:TIGR04523 521 SLKEKIEKLESE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
58-158 |
7.64e-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: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 58 LENLDSVFAQDQEhqvELELLRDDNEQLitqyEREKALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKN 137
Cdd:COG3883 121 LSALSKIADADAD---LLEELKADKAEL----EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
90 100
....*....|....*....|.
gi 568975810 138 YADQISRLEEREAELKKEYNA 158
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAA 214
|
|
| MIC19_MIC25 |
pfam05300 |
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ... |
72-154 |
8.56e-03 |
|
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Pssm-ID: 461615 [Multi-domain] Cd Length: 173 Bit Score: 38.91 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 72 QVELELLRD-DNEQLITQYE------REK-ALRKHAEEKFIEFEDSQEQEKKDLQTRVESLESQTRQLELKAKNYADQIS 143
Cdd:pfam05300 66 KIKEELYKRlEQEQAKVQEElarlaeREReAAQESLTRAILRERASTEDERLKAQQLAKQLEEKEAELKKQDAFYKEQLA 145
|
90
....*....|.
gi 568975810 144 RLEEREAELKK 154
Cdd:pfam05300 146 RLEEKNAEFYK 156
|
|
| 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 568975810 60 NLDSVFAQDQEHQVELELLRDDNEQLITQYERE---------------KALRKHAEEKFIEFEDSQEQEKKDLQTrVESL 124
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnsesenSEKQRELEEKQNEIEKLKKENQSYKQE-IKNL 389
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568975810 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 |
9.84e-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: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 23 RVSGLAGSIyREFERLIGRYDEEVV------KELMPLVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQ-YEREKAL 95
Cdd:pfam07888 74 QRRELESRV-AELKEELRQSREKHEeleekyKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975810 96 RKHAE--EKFIEFEDSQEQEKKDLQTRVESLESQTRQLEL---KAKNYADQ----ISRLEEREAELKKEYNALHQRHTEM 166
Cdd:pfam07888 153 ERMKEraKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKefqELRNSLAQrdtqVLQLQDTITTLTQKLTTAHRKEAEN 232
|
|
| |
