|
Name |
Accession |
Description |
Interval |
E-value |
| CC149 |
pfam09789 |
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ... |
1-283 |
1.49e-120 |
|
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.
Pssm-ID: 462902 [Multi-domain] Cd Length: 314 Bit Score: 355.49 E-value: 1.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 1 MANQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789 31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 81 G---DEEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622939062 237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-195 |
8.85e-07 |
|
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: 51.60 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGD--NKLLRMTIAKQRLGDEEIgvrhfaahEREDLVQQLERAKE 107
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaaNLRERLESLERRIAATER--------RLEDLEEQIEELSE 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 108 QIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
....*...
gi 1622939062 188 KYKNALER 195
Cdd:TIGR02168 933 GLEVRIDN 940
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
29-195 |
3.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEeigvRHFAAHEREDLVQQLERAKEQ 108
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 109 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:COG4717 155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230
|
....*...
gi 1622939062 188 KYKNALER 195
Cdd:COG4717 231 QLENELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-195 |
4.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGdnklLRMTIAK-QRLGDEEIGVRHfAAHEREDLVQQLER---- 104
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE----RREALQRlAEYSWDEIDVAS-AEREIAELEAELERldas 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 105 ------AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNH---ILSGHENRIIDVDALCMENRYLQERL--- 172
Cdd:COG4913 684 sddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERFAAALGdav 763
|
170 180
....*....|....*....|....*...
gi 1622939062 173 -----KQLHEEVNLLKSNIAKYKNALER 195
Cdd:COG4913 764 erelrENLEERIDALRARLNRAEEELER 791
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
4-187 |
6.52e-06 |
|
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: 48.35 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 4 QLRERHQSLKKKYREMIDGDPSLPPEKRKqanLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDnkLLRMTIAKQRLGde 83
Cdd:pfam07888 91 QSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETE--LERMKERAKKAG-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 84 eiGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCM 163
Cdd:pfam07888 164 --AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA----HRKEAENEALLE 237
|
170 180
....*....|....*....|....
gi 1622939062 164 ENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELS 261
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-284 |
2.20e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRII----DVDALCM 163
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELArleqDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 164 ENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgVLSAKQVQDLLSEDHGCSLPATpQSISDLKS 243
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE-EELEELAE 386
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622939062 244 LATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
30-188 |
4.54e-05 |
|
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: 46.00 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLgevqgdnkllrmtiakqRLGDEEIGvrhfaaheredLVQQLErakEQI 109
Cdd:pfam06160 290 EKNLPEIEDYLEHAEEQNKELKEELERVQQSY-----------------TLNENELE-----------RVRGLE---KQL 338
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939062 110 ESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAK 188
Cdd:pfam06160 339 EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-284 |
1.53e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKK------KYREMIDGdpslppEKRKQANLAQL-LRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI 75
Cdd:COG1196 196 GELERQLEPLERqaekaeRYRELKEE------LKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 76 AKQRLGDEEigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRI 155
Cdd:COG1196 270 EELRLELEE------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 156 IDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLS--AKQVQDLLSEDHgcslpa 233
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEelEEAEEALLERLE------ 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622939062 234 tpQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196 418 --RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-198 |
1.96e-04 |
|
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: 43.60 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGD-----NKLLRMTIAK 77
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 78 QRLG------------DEEIGVRHFA-----AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERL 140
Cdd:COG4942 114 YRLGrqpplalllspeDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622939062 141 NQELNHILSGHENRIidvdalcmenRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 198
Cdd:COG4942 194 KAERQKLLARLEKEL----------AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-195 |
3.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 2 ANQLRERHQSLKKKYREMIDGDPSLPPEKRKQAnlAQLLRDSQDRNKhlgEEIKELQQRLGEvqgdnkllrmtiAKQRLG 81
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELR---AELARLEAELER------------LEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 82 DeeigvrhfAAHEREDLVQQLERAK-EQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDA 160
Cdd:COG4913 320 A--------LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*
gi 1622939062 161 LCMEnryLQERLKQLHEEVNLLKSNIAKYKNALER 195
Cdd:COG4913 392 LLEA---LEEELEALEEALAEAEAALRDLRRELRE 423
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-284 |
7.44e-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: 42.31 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgd 82
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN--- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 83 EEIgvrhfaaherEDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELnhilsghENRIIDVDALC 162
Cdd:TIGR04523 440 SEI----------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 163 MENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSEDHgcslpatpQSISDLK 242
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN--------KEIEELK 574
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622939062 243 SLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
91-284 |
7.83e-04 |
|
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: 41.67 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIidvdalcmenRYLQE 170
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQEL----------AALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 171 RLKQLHEEVNLLKSNIAKYKNALERRkNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcSLPATPQSISDLKSLATALLE 250
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRA 157
|
170 180 190
....*....|....*....|....*....|....
gi 1622939062 251 TIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALE 191
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-285 |
8.35e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI--AKQRLGDEEIGVRHF------AAHEREDLVQQ 101
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLeaeveqLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 102 LERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHenriidvDALCMENRYLQERLKQLHEEVNL 181
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-------DELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 182 LKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQ--DLLSE--DHGCSLPATPQSISDLKSLATALLETIHEKNM 257
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieELESEleALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260
....*....|....*....|....*...
gi 1622939062 258 VIQHQRQTNKILGNRVAELEKKLRTLEV 285
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-284 |
9.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 99 VQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsgheNRIIDVDALCMENRYLQERLKQLHEE 178
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 179 VNLLKSNIAKYKNALERRKNSKGQgkssssaltgvlsAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMV 258
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE-------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180
....*....|....*....|....*.
gi 1622939062 259 IQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
27-198 |
1.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 27 PPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeeigvrhfaaHEREDLVQQLERAK 106
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------------SELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 107 EQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNI 186
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170
....*....|..
gi 1622939062 187 AKYKNALERRKN 198
Cdd:COG4372 167 AALEQELQALSE 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
52-313 |
1.12e-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: 41.29 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 52 EEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeeiGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 131
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 132 SYQDKVERLNQELNHIL---------------------SGHENRIIDVDALcmeNRYLQERLKQLHEEVNLLKSNIAKYK 190
Cdd:COG4942 94 ELRAELEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYL---APARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 191 NALERRKNSKGQGKSSSSALTgvlSAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIheKNMVIQHQRQTNKILG 270
Cdd:COG4942 171 AERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622939062 271 NRVAELEKKLRtlevsglWSLPGlsyNVSVGFGRGKDTILFSD 313
Cdd:COG4942 246 AGFAALKGKLP-------WPVSG---RVVRRFGERDGGGGRNK 278
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
46-184 |
1.22e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 46 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEEIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 113
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939062 114 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 184
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
29-124 |
1.50e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEEIGV--RHFAAHERE--DLVQQLER 104
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLlkQKLEEHLEKlhEAQSELQK 381
|
90 100
....*....|....*....|....
gi 1622939062 105 AKEQIESLEHDLQAS----VDELQ 124
Cdd:pfam05622 382 KKEQIEELEPKQDSNlaqkIDELQ 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-286 |
1.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 96 EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQL 175
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 176 HEEVNLLKSNIAKyknaLERRKNSKGQGKSSSSALTGVLsAKQVQDLLSEdhgcsLPATPQSISDLKSLATALLETIHE- 254
Cdd:TIGR02168 315 ERQLEELEAQLEE----LESKLDELAEELAELEEKLEEL-KEELESLEAE-----LEELEAELEELESRLEELEEQLETl 384
|
170 180 190
....*....|....*....|....*....|..
gi 1622939062 255 KNMVIQHQRQTNKIlGNRVAELEKKLRTLEVS 286
Cdd:TIGR02168 385 RSKVAQLELQIASL-NNEIERLEARLERLEDR 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-140 |
2.34e-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: 40.81 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 2 ANQLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLG 81
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEE 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939062 82 DEEigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERL 140
Cdd:TIGR02168 449 LEE------LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
4-288 |
2.68e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 4 QLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDE 83
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLK---KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 84 EIGVRHFAAHERedlVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDK---VERLNQELNhilsghenRIIDVDA 160
Cdd:pfam05557 136 ELQERLDLLKAK---ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELA--------RIPELEK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 161 LCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSEDHGCSLPaTPQSISd 240
Cdd:pfam05557 205 ELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLR-SPEDLS- 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622939062 241 lkslatalletihekNMVIQHQrQTNKILGNRVAELEKKLRTLEVSGL 288
Cdd:pfam05557 283 ---------------RRIEQLQ-QREIVLKEENSSLTSSARQLEKARR 314
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-148 |
2.85e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKKKYREMidgdpslppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGD 82
Cdd:TIGR02169 850 KSIEKEIENLNGKKEEL----------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 83 EEIGVRHFAAHER---------------------EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLN 141
Cdd:TIGR02169 920 SELKAKLEALEEElseiedpkgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
....*..
gi 1622939062 142 QELNHIL 148
Cdd:TIGR02169 1000 EERKAIL 1006
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
31-195 |
3.09e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 31 RKQANLAQllRDSQDRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEEIGVRHFAAHE--REDLVQQLER 104
Cdd:PRK04863 506 REQRHLAE--QLQQLRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 105 AKEQIESLEH---DLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNL 181
Cdd:PRK04863 577 ARERRMALRQqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDE 649
|
170
....*....|....
gi 1622939062 182 LKSNIAKYKNALER 195
Cdd:PRK04863 650 LAARKQALDEEIER 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-225 |
3.89e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKKKYREmidgdpslppEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgd 82
Cdd:COG1196 277 EELELELEEAQAEEYE----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 83 EEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQdvkEERSSYQDKVERLNQELNHILSGHENRIIDVDALC 162
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622939062 163 MENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGV--LSAKQVQDLLSE 225
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEaaLLEAALAELLEE 485
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-198 |
4.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 3 NQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRdsqdRNKHLGEEIKELQQRLGEVQGDNKLLrmtiaKQRLGD 82
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKL-----EEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 83 EEigvrhfaaHEREDLVQQLERAKEQIESLEhDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRIIDVD 159
Cdd:PRK03918 264 LE--------ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLeeeINGIEERIKELE 334
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622939062 160 ALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 198
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
8-284 |
6.29e-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: 39.23 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 8 RHQSLKKKYREMIdgdpsLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLGDEEIGV 87
Cdd:TIGR04523 193 KNKLLKLELLLSN-----LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT--TEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 88 RHfaahEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEErssyqdKVERLNQELNHILSGHENRIIDVDALCMENRY 167
Cdd:TIGR04523 266 KK----QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 168 ----LQERLKQLHEEVNLLKSNIAKYKNALERRKNskgqgkssssaltgvlsakQVQDLLSEDHGCSlpatpQSISDLKS 243
Cdd:TIGR04523 336 iisqLNEQISQLKKELTNSESENSEKQRELEEKQN-------------------EIEKLKKENQSYK-----QEIKNLES 391
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622939062 244 LATALletihekNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:TIGR04523 392 QINDL-------ESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
|
| TraB_PrgY_gumN |
pfam01963 |
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ... |
23-172 |
6.34e-03 |
|
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.
Pssm-ID: 426534 Cd Length: 262 Bit Score: 38.49 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 23 DPSLPPEKRKQANLAQLLRDSQDRN--KHLGEE-IKELQQRLGEVQ-GDNKLLRM------------TIAKQRLGDEEIG 86
Cdd:pfam01963 47 DLSRYTDPATQAALPKLGLLPDGKTlsDLLSPElYARLQKALAKRGlPLAALDRMkpwlaalllslaELAKQKAGLDPDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 87 V-RHFA--AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLnqeLNHILSGHENRIIDVDALCM 163
Cdd:pfam01963 127 VdRYLAktAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLDELEKGEDLLETL---VEAWAEGDLEALELEAELKE 203
|
....*....
gi 1622939062 164 ENRYLQERL 172
Cdd:pfam01963 204 AYPELYEVL 212
|
|
|