|
Name |
Accession |
Description |
Interval |
E-value |
| CC149 |
pfam09789 |
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ... |
26-338 |
2.71e-140 |
|
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: 407.10 E-value: 2.71e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHL 105
Cdd:pfam09789 1 KRKLQSKVEALLILSKELEKCRQERDQYKLMAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 106 GEEIKELQQRLGEVQGDNKLLRMTIAKQRLG---DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVK 182
Cdd:pfam09789 81 RLEVEELRQKLNEAQGDIKLLREQIARQRLGgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 183 EERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSS 262
Cdd:pfam09789 161 TERDAYKCKAHRLNHELNYILGGDESRIVDIDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299473762 263 SALTGVLSAKQVQDLLsedHGCSLPATPQ-SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 338
Cdd:pfam09789 241 SSGGLVISAKQVKELL---ESGSLSNTPQaTISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-250 |
1.21e-08 |
|
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: 57.76 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKkyrELIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLG 106
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE---RLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 107 EEIKELQQRLgevqgdnKLLRMTIAKQRLGDEAIGVRHFAAHER-EDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:TIGR02168 803 EALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299473762 186 SSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
26-242 |
4.66e-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: 49.12 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELdtcQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKqanLAQLLRDSQDRNKHL 105
Cdd:pfam07888 61 KERYKRDREQWERQRREL---ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIREL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 106 GEEIKELQQRLGEVQGDnkLLRMTIAKQRlgdeAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:pfam07888 135 EEDIKTLTQRVLERETE--LERMKERAKK----AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 299473762 186 SSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:pfam07888 209 LQLQDTITTLTQKLTTA----HRKEAENEALLEELRSLQERLNASERKVEGLGEELS 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-253 |
5.19e-06 |
|
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: 48.61 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDSQDRNKHL 105
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------EQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 106 GEEIKELQQRLGEV------QGDNKLLRMTIAKQRLGDEAIGVRHFAA--HEREDLVQQLERAKEQIESLEHDLQASVDE 177
Cdd:COG4942 96 RAELEAQKEELAELlralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 299473762 178 LQDVKEERSSYQDKVERLNQELNHILSGHENRIidvdalcmenRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 253
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL----------AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
84-250 |
1.04e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 84 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEaigvRHFAAHEREDLVQQLERAKEQ 163
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 164 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:COG4717 155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230
|
....*...
gi 299473762 243 KYKNALER 250
Cdd:COG4717 231 QLENELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-250 |
1.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 97 DSQDRNKHLGEEIKELQQRLGEVQ---GDNKLLRMTIAKQRLGDEAIGVRHF-------AAHEREDLVQQLER------- 159
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEerlEALEAELDALQERREALQRLAEYSWdeidvasAEREIAELEAELERldassdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 160 ---AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNH---ILSGHENRIIDVDALCMENRYLQERL------ 227
Cdd:COG4913 687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERFAAALGdavere 766
|
170 180
....*....|....*....|....*
gi 299473762 228 --KQLHEEVNLLKSNIAKYKNALER 250
Cdd:COG4913 767 lrENLEERIDALRARLNRAEEELER 791
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-208 |
1.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 21 EYLVCKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIdgdpslppekrkqanlAQLLRDSQD 100
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE----------------AQIRGNGGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 101 RNKHLGEEIKELQQRLGEVQGdnkllrmtiAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQD 180
Cdd:COG4913 339 RLEQLEREIERLERELEERER---------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE 409
|
170 180
....*....|....*....|....*...
gi 299473762 181 VKEERSSYQDKVERLNQELNHILSGHEN 208
Cdd:COG4913 410 AEAALRDLRRELRELEAEIASLERRKSN 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-195 |
3.39e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLppeKRKQANLAQLLRDSQDRNKHL 105
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 106 GEEIKELQQRLGEVQgdNKLLRMTIAkqrlgdEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEER 185
Cdd:TIGR02168 420 QQEIEELLKKLEEAE--LKELQAELE------ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
170
....*....|
gi 299473762 186 SSYQDKVERL 195
Cdd:TIGR02168 492 DSLERLQENL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-203 |
3.41e-05 |
|
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: 46.60 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDSQDRNKHLG 106
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----------EEELEELEAALRDLESRLGDLK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 107 EEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHER---------------------EDLVQQLERAKEQIE 165
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeeipeeelslEDVQAELQRVEEEIR 968
|
170 180 190
....*....|....*....|....*....|....*...
gi 299473762 166 SLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIL 203
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-339 |
3.81e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 146 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRII----DVDALCM 218
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELArleqDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 219 ENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgVLSAKQVQDLLSEDHGCSLPATpQSISDLKS 298
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE-EELEELAE 386
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 299473762 299 LATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
57-252 |
5.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 57 ANQLRERHQSLKKKYRELIDGDPSLPPEKRKQAnlAQLLRDSQDRNKH----LGEEIKELQQRLGEVQGdnKLLRMTIAK 132
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAelarLEAELERLEARLDALRE--ELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 133 QRLGDEAIGV----RHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEN 208
Cdd:COG4913 333 RGNGGDRLEQlereIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 299473762 209 RIIDvdalcmenryLQERLKQLHEEVNLLKSNIAKY-KNALERRK 252
Cdd:COG4913 413 ALRD----------LRRELRELEAEIASLERRKSNIpARLLALRD 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
58-339 |
7.13e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 58 NQLRERHQSLKK------KYRELIDGdpslppEKRKQANLAQL-LRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI 130
Cdd:COG1196 196 GELERQLEPLERqaekaeRYRELKEE------LKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 131 AKQRLGDEAIGVRHFAAHERE-DLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENR 209
Cdd:COG1196 270 EELRLELEELELELEEAQAEEyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 210 IIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgvlsAKQVQDLLSEDHgcslpat 289
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLE------- 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 299473762 290 pQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG1196 418 -RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-265 |
8.53e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 13 ARAATWDSEYLVCKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLA 92
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----------EERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 93 QLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLG-DEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDL 171
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 172 QASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERR 251
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250
....*....|....
gi 299473762 252 KNSKGQGKSSSSAL 265
Cdd:COG1196 483 LEELAEAAARLLLL 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-198 |
1.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRKQAnLAQLLRDSQDRNKHLG 106
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-LEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 107 EEIKELQQRLGEVQGDNKLLRMtiAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 186
Cdd:COG4717 153 ERLEELRELEEELEELEAELAE--LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|..
gi 299473762 187 SYQDKVERLNQE 198
Cdd:COG4717 231 QLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-201 |
1.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 27 RKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRElIDGDpslppekrkqaNLAQLLRDSqdrnKHLG 106
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-NGGD-----------RLEQLEREI----ERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 107 EEIKELQQRLGEVQGDNKLLRMTIAK-----QRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDV 181
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPAsaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
170 180
....*....|....*....|
gi 299473762 182 KEERSSYQDKVERLNQELNH 201
Cdd:COG4913 432 ERRKSNIPARLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-199 |
2.05e-04 |
|
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: 44.29 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 25 CKRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELIDGDPSLPPEKRK-QANLAQL---LRDSQD 100
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlRAELEEVdkeFAETRD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 101 RNKHLGEEIKELQQRLGEVQG--DNKLLRMTIAKQRLGD-----EAIGVRHFA-AHEREDLVQQLERAKEQIESLEHDLQ 172
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRelDRLQEELQRLSEELADlnaaiAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLS 465
|
170 180
....*....|....*....|....*..
gi 299473762 173 ASVDELQDVKEERSSYQDKVERLNQEL 199
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-253 |
9.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLkKKYRELIDGDPSLPPEKRKQANL-AQL--LRDSQDRN 102
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELeAELerLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 103 KHLGEEIKELQQRLGEVQGDNKLLRMTIAKqrlgdeaigvrhfAAHEREDLVQQLERAKEQIESLEHD------------ 170
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGR-------------LEKELEQAEEELDELQDRLEAAEDLarlelralleer 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 171 -LQASVDEL-----QDVKEERSSYQDKVERLNQELNHILSGH----ENRIIDVDALCMENRYLQERLKQLHEEvnllksN 240
Cdd:COG4913 755 fAAALGDAVerelrENLEERIDALRARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLEED------G 828
|
250
....*....|...
gi 299473762 241 IAKYKNALERRKN 253
Cdd:COG4913 829 LPEYEERFKELLN 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
160-339 |
9.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 160 AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSghenriidvdalcmENRYLQERLKQLHEEVNLLKS 239
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA--------------ELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 240 NIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcslpatpqSISDLKSLATAlletiheKNMVIQHQRQ 319
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLD------------RLSALSKIADA-------DADLLEELKA 140
|
170 180
....*....|....*....|
gi 299473762 320 TNKILGNRVAELEKKLRTLE 339
Cdd:COG3883 141 DKAELEAKKAELEAKLAELE 160
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-202 |
1.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 13 ARAATWDSEYLVCKRKLESKKEALLILSKELDTCQQERDQYKlmaNQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLA 92
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 93 QLLRDSQDRNKhlgEEIKELQQRLGEVQGDNKLlRMTIAKQRLGDEAIGVRHFAAH----EREDLVQQLERAKEQIESLE 168
Cdd:COG4913 769 ENLEERIDALR---ARLNRAEEELERAMRAFNR-EWPAETADLDADLESLPEYLALldrlEEDGLPEYEERFKELLNENS 844
|
170 180 190
....*....|....*....|....*....|....
gi 299473762 169 HDLQASVdeLQDVKEERSSYQDKVERLNQELNHI 202
Cdd:COG4913 845 IEFVADL--LSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-339 |
1.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 146 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIidvdalcmenRYLQE 225
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQEL----------AALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 226 RLKQLHEEVNLLKSNIAKYKNALERRkNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcSLPATPQSISDLKSLATALLE 305
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRA 157
|
170 180 190
....*....|....*....|....*....|....
gi 299473762 306 TIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALE 191
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-250 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLRERHQSLKKKYRELidgdpslppeKRKQANLAQLLRDsqdrnkhL 105
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----------QKELYALANEISR-------L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 106 GEEIKELQQRLGEVQGDNKLLRMTIA--KQRLGDeaigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKE 183
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEelESKLDE--------LAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299473762 184 ERSSYQDKVERLNQELNHILSghenriiDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLEL-------QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-339 |
2.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 154 VQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsgheNRIIDVDALCMENRYLQERLKQLHEE 233
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 234 VNLLKSNIAKYKNALERRKNSKGQgkssssaltgvlsAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMV 313
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAE-------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180
....*....|....*....|....*.
gi 299473762 314 IQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-341 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 151 EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQL 230
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 231 HEEVNLLKSNIAKyknaLERRKNSKGQGKSSSSALTGVLsAKQVQDLLSEdhgcsLPATPQSISDLKSLATALLETIHE- 309
Cdd:TIGR02168 315 ERQLEELEAQLEE----LESKLDELAEELAELEEKLEEL-KEELESLEAE-----LEELEAELEELESRLEELEEQLETl 384
|
170 180 190
....*....|....*....|....*....|..
gi 299473762 310 KNMVIQHQRQTNKIlGNRVAELEKKLRTLEVS 341
Cdd:TIGR02168 385 RSKVAQLELQIASL-NNEIERLEARLERLEDR 415
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
151-456 |
2.79e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 151 EDLVQQLERAKEQIESL---EHDLQASVDELQDVKEERSSYQDKVerLNQELNH---ILSGHENRIIDVDALcmENRYLQ 224
Cdd:TIGR01612 807 EDAKQNYDKSKEYIKTIsikEDEIFKIINEMKFMKDDFLNKVDKF--INFENNCkekIDSEHEQFAELTNKI--KAEISD 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 225 ERLKQLHEEVNLLKSNIAKYKNALERRknskgqgkssssaLTGVLSAKQVQDLLSEdhgCSlpATPQSISDLKSLATAL- 303
Cdd:TIGR01612 883 DKLNDYEKKFNDSKSLINEINKSIEEE-------------YQNINTLKKVDEYIKI---CE--NTKESIEKFHNKQNILk 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 304 ------LETIHEKNMVIQ-HQRQTNKILGNRVAELEKklrtlevsglwslpggkdtiLFSDPTLPSGQRSRSPLLKFVEQ 376
Cdd:TIGR01612 945 eilnknIDTIKESNLIEKsYKDKFDNTLIDKINELDK--------------------AFKDASLNDYEAKNNELIKYFND 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 377 PTENKADPKDGEAQKQEEDESCAAAEALTAPEDagrpavnspANQSRGNQCKLFHPSLPQLpSEEEVNSLGREIIKLTKE 456
Cdd:TIGR01612 1005 LKANLGKNKENMLYHQFDEKEKATNDIEQKIED---------ANKNIPNIEIAIHTSIYNI-IDEIEKEIGKNIELLNKE 1074
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-199 |
3.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 27 RKLESKKEALLILSKELDTCQQERDQYklmaNQLRERHQSLKKKYRELIDGDPSLPPEKRKQANLAQLLRDSQDRNK--- 103
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlea 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 104 ---HLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQD 180
Cdd:COG4717 140 elaELPERLEELEERLEELR--ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170
....*....|....*....
gi 299473762 181 VKEERSSYQDKVERLNQEL 199
Cdd:COG4717 218 AQEELEELEEELEQLENEL 236
|
|
| TraB_PrgY_gumN |
pfam01963 |
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ... |
60-227 |
3.57e-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: 39.26 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 60 LRERHQSLKKKYRELIDG--------DPSLPPEKRKQANLAQLLRDSQDRN--KHLGEE-IKELQQRLGEVQ-GDNKLLR 127
Cdd:pfam01963 21 LPPSVYPLPPAIEEALEAadtvvvelDLSRYTDPATQAALPKLGLLPDGKTlsDLLSPElYARLQKALAKRGlPLAALDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 128 M------------TIAKQRLGDEAIGV-RHFA--AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKV 192
Cdd:pfam01963 101 MkpwlaalllslaELAKQKAGLDPDLVdRYLAktAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLDELEKGEDLL 180
|
170 180 190
....*....|....*....|....*....|....*
gi 299473762 193 ERLnqeLNHILSGHENRIIDVDALCMENRYLQERL 227
Cdd:pfam01963 181 ETL---VEAWAEGDLEALELEAELKEAYPELYEVL 212
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
84-179 |
4.20e-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: 39.67 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 84 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQ--RLGDEAIGVRHFAAHERE--DLVQQLER 159
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgsKAEDSSLLKQKLEEHLEKlhEAQSELQK 381
|
90 100
....*....|....*....|....
gi 299473762 160 AKEQIESLEHDLQAS----VDELQ 179
Cdd:pfam05622 382 KKEQIEELEPKQDSNlaqkIDELQ 405
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
26-343 |
4.39e-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: 39.72 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDT----CQQERDQYKLMA---NQLRERHQSLKKKYRELIDGDPSLppeKRKQANLAQLLRDS 98
Cdd:pfam05557 19 KQMELEHKRARIELEKKASAlkrqLDRESDRNQELQkriRLLEKREAEAEEALREQAELNRLK---KKYLEALNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 99 QDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHERedlVQQLERAKEQIESLEHDLQASVDEL 178
Cdd:pfam05557 96 ESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAK---ASEAEQLRQNLEKQQSSLAEAEQRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 179 QDVKEERSSYQDK---VERLNQELNhilsghenRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSK 255
Cdd:pfam05557 173 KELEFEIQSQEQDseiVKNSKSELA--------RIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 256 GQGKSSSSALTGVLSAKQVQDLLSEDHGCSLPaTPQSISdlkslatalletihekNMVIQHQrQTNKILGNRVAELEKKL 335
Cdd:pfam05557 245 EEAATLELEKEKLEQELQSWVKLAQDTGLNLR-SPEDLS----------------RRIEQLQ-QREIVLKEENSSLTSSA 306
|
....*...
gi 299473762 336 RTLEVSGL 343
Cdd:pfam05557 307 RQLEKARR 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-339 |
4.54e-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: 40.04 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 149 EREDLVQQLERAKEQIESLEhdlqasvDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLK 228
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELE-------KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 229 QLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTgvlsaKQVQDLLSEdhgcslpatpqsISDLKSLATALLETIH 308
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-----AQIEQLKEE------------LKALREALDELRAELT 813
|
170 180 190
....*....|....*....|....*....|.
gi 299473762 309 EKNMVIQHQRQTNKILGNRVAELEKKLRTLE 339
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLE 844
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
107-336 |
4.66e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 107 EEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 186
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 187 SYQ--DKVERLNQELNHILS-GHENRiidvdaLCMENRylQERLKQLHEEVNLLKSNIAKYKNALERRKNSkgqgkssss 263
Cdd:TIGR00606 824 VQQvnQEKQEKQHELDTVVSkIELNR------KLIQDQ--QEQIQHLKSKTNELKSEKLQIGTNLQRRQQF--------- 886
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299473762 264 altgvlsAKQVQDLLSEDHGCsLPATPQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLR 336
Cdd:TIGR00606 887 -------EEQLVELSTEVQSL-IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
26-250 |
4.92e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 26 KRKLESKKEALLILSKELDTCQQERDQYKLMANQLR------ERHQSlKKKYRELIDgdpslppEKRKQANLAQllRDSQ 99
Cdd:PRK04863 448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRkiagevSRSEA-WDVARELLR-------RLREQRHLAE--QLQQ 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 100 DRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEAIGVRHFAAHE--REDLVQQLERAKEQIESLEH---D 170
Cdd:PRK04863 518 LRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSEARERRMALRQqleQ 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 171 LQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNLLKSNIAKYKNALER 250
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDELAARKQALDEEIER 663
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-242 |
6.06e-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: 39.67 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 38 ILSKELDTCQQERDQyklmanqlRERHQSLKKKYRElIDGDPSLppeKRKQANLAQLlrdsQDRNKHLGEEIKELQQRlg 117
Cdd:TIGR02169 195 EKRQQLERLRREREK--------AERYQALLKEKRE-YEGYELL---KEKEALERQK----EAIERQLASLEEELEKL-- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 118 EVQGDNKLLRMTIAKQRLGDEAIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQdkverlnQ 197
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE-------A 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 299473762 198 ELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 242
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
101-239 |
7.06e-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: 38.46 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473762 101 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEAIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 168
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299473762 169 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 239
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
|
|
| |
