|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-369 |
9.09e-10 |
|
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: 61.61 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEaqgekirdlefCLEEHREKVNATEEmlqqelLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAE-----------KAERYKELKAELRE------LELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 183 LTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMK-----------IKVGQMQYE 251
Cdd:TIGR02168 248 LKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanleRQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 252 KQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANE 331
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELE-ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370463087 332 EKDRKIEDLRQCLNRykkmQDTVVLAQGKKGKDGEYEE 369
Cdd:TIGR02168 404 RLEARLERLEDRRER----LQQEIEELLKKLEEAELKE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
115-346 |
8.12e-09 |
|
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: 57.85 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 115 SLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYE 194
Cdd:COG4942 3 KLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 195 DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSS-----MKIKVGQMQYEKQRMEQKWESLKDELASL 269
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463087 270 KEQLEEKESEVKRLQEKLvckmkgegVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 346
Cdd:COG4942 163 AALRAELEAERAELEALL--------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-340 |
1.33e-08 |
|
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: 58.16 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 90 MTNGHLPGNGDV-----YQERLARLENDKESLVLQVSVLTDQVEAQ----GEKIRDLEFCLEEHREKVNATEEMLQQELL 160
Cdd:TIGR02169 655 MTGGSRAPRGGIlfsrsEPAELQRLRERLEGLKRELSSLQSELRRIenrlDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 161 SRTSLEtqklDLMAEISNLKLKLTAV--EKDRLDYE--DKFRDTEGLIQEINDL--RLKVSEMDSERLQYEKKLKSTKSL 234
Cdd:TIGR02169 735 LKERLE----ELEEDLSSLEQEIENVksELKELEARieELEEDLHKLEEALNDLeaRLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 235 MAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL------VCKMKGEGVEIVDRDENFKKK 308
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKeeleeeLEELEAALRDLESRLGDLKKE 890
|
250 260 270
....*....|....*....|....*....|..
gi 1370463087 309 LKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 340
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-346 |
1.99e-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: 57.37 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSV-------LTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAE 175
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 176 ISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQRM 255
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATE---RRLEDLEEQIEELSEDIESLAAEIEELEELIEELES---ELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 256 EQKWESLKDELASLKEQLEEKESEVKRLQEKL------VCKMKGEGVEIVDRDENFKKKLKEK-NIEVQKMKKAVESLMA 328
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELeelrekLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIED 965
|
250
....*....|....*...
gi 1370463087 329 ANEEKDRKIEDLRQCLNR 346
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-349 |
9.76e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRL 212
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 213 KV---SEMDSERLQYEKKLKSTKSLMAKLSSmKIKvgqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvc 289
Cdd:PRK03918 291 KAeeyIKLSEFYEEYLDELREIEKRLSRLEE-EIN------GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-- 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 290 KMKGEGVEIVDRDENFKKKLKEKNIEvqKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 349
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-287 |
3.20e-07 |
|
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: 52.84 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellSRTSLETQKLDL---------M 173
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAELEAQKEELaellralyrL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 174 AEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQ 249
Cdd:COG4942 117 GRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370463087 250 YEKQRM----EQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942 195 AERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-349 |
3.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 173 MAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKkLKSTKSLMAKLSSMKIKVGQMQYEK 252
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 253 QRMEQKWEslkdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE 332
Cdd:COG4717 149 EELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*..
gi 1370463087 333 KDRKIEDLRQCLNRYKK 349
Cdd:COG4717 225 LEEELEQLENELEAAAL 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-354 |
4.14e-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: 53.14 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 180 KLKLTAVEKDRLDYEDKFRDTEGLIQEindLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNN----------EIERLEARL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 260 ESLKDELASLKEQLEE-----KESEVKRLQEKLVCKMKGEgVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKD 334
Cdd:TIGR02168 410 ERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEEL-EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260
....*....|....*....|
gi 1370463087 335 RKIEDLRQCLNRYKKMQDTV 354
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGV 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
153-349 |
4.52e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 153 EMLQQELlsrTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDkfrdteglIQEINDLRLKVSEMDSERLQYEKKLKSTK 232
Cdd:COG4913 613 AALEAEL---AELEEELAEAEERLEALEAELDALQERREALQR--------LAEYSWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 233 SLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEK 312
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370463087 313 NIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 349
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-365 |
5.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLENDKESLV------------------------LQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ 157
Cdd:COG1196 234 LRELEAELEELEAELEeleaeleeleaelaeleaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 158 ELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRL-KVSEMDSERLQYEKKLKSTKSLMA 236
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLeAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 237 KLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEV 316
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1370463087 317 QKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQGKKGKDG 365
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-340 |
1.07e-06 |
|
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: 51.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 183 LTAVEkdrLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKWESL 262
Cdd:TIGR04523 449 DSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE----------EKKELEEKVKDL 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463087 263 KDELASLKEQLEEKESEVKRLQEKLV-CKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDL 340
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISdLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-341 |
1.46e-06 |
|
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: 51.17 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQellsRTSLETQKLDLMAEISNLKL 181
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKET----IIKNNSEIKDLTNQDSVKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 182 KLTAVEKDRLDYEDKFRDTEGLIQEIN--------DLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQ 253
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKqnleqkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 254 RMEQKWESLKDELASLKEQL--EEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANE 331
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
250
....*....|
gi 1370463087 332 EKDRKIEDLR 341
Cdd:TIGR04523 614 SLEKELEKAK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-288 |
1.79e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 100 DVYQERlaRLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK--VNATEEMLQQELLSRTSLETQKLDLMAEIS 177
Cdd:COG3206 159 EAYLEQ--NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 178 NLKLKLTAVEKDRLDYEDKFRDTEGlIQEINDLRLKVSEMDSERLQYEKKLKST----KSLMAKLSSMKikvGQMQYEKQ 253
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALR---AQLQQEAQ 312
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370463087 254 R----MEQKWESLKDELASLKEQLEEKESEVKRLQEKLV 288
Cdd:COG3206 313 RilasLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-332 |
2.75e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTD---QVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNL 179
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 180 KLKLTAVEKDRLDYED---KFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRME 256
Cdd:PRK03918 272 KKEIEELEEKVKELKElkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 257 QKWESLKdELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEK----NIEVQKMKKAVESLMAANEE 332
Cdd:PRK03918 352 KRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELKKAIEE 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
111-348 |
5.31e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 111 NDKESlvlQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDR 190
Cdd:pfam05483 236 NDKEK---QVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 191 LDYEDKFR-----------DTEGLIQEINDLR----LKVSEMDSERLQYEKKLKSTKSLMAK-LSSMKIKVGQMQYEKQR 254
Cdd:pfam05483 313 KALEEDLQiatkticqlteEKEAQMEELNKAKaahsFVVTEFEATTCSLEELLRTEQQRLEKnEDQLKIITMELQKKSSE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 255 MEQ--KWESLKD-ELASLKEQLEEKESEV--KRLQEKLVCKMKGEGVEIVdrdenFKKKLKEKniEVQKMKKAVESLMAA 329
Cdd:pfam05483 393 LEEmtKFKNNKEvELEELKKILAEDEKLLdeKKQFEKIAEELKGKEQELI-----FLLQAREK--EIHDLEIQLTAIKTS 465
|
250
....*....|....*....
gi 1370463087 330 NEEKDRKIEDLRQCLNRYK 348
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEK 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
204-349 |
6.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 204 IQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRL 283
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370463087 284 QE-----KLVCKMKGEGVEIVDRDENFKK---KLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 349
Cdd:PRK03918 286 KElkekaEEYIKLSEFYEEYLDELREIEKrlsRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE 359
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-354 |
6.78e-06 |
|
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: 49.30 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLE--------NDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQEllsrtsleTQKLDLM 173
Cdd:TIGR02169 213 YQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--------NKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 174 AEISNLKLKltaveKDRLDYEDKFRDTEGLIQEINDlrlKVSEMDSERLQYEKKLKSTKSLMAKLSSmkiKVGQMQYEKQ 253
Cdd:TIGR02169 285 GEEEQLRVK-----EKIGELEAEIASLERSIAEKER---ELEDAEERLAKLEAEIDKLLAEIEELER---EIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 254 RMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVC-------------KMKGEGVEIVDRDENFKKKLKEKNIEVQKMK 320
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleklkreinELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270
....*....|....*....|....*....|....
gi 1370463087 321 KAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTV 354
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-350 |
8.75e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKL---KST 231
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLgnvRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 232 KSLMAklssmkikvgqMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegveiVDRDENFKKKLKE 311
Cdd:COG1579 89 KEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL-----------AELEAELEEKKAE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1370463087 312 KNIEVQKMKKAVESLMAANEEKDRKI-EDLrqcLNRYKKM 350
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAKIpPEL---LALYERI 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
132-359 |
2.06e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 132 EKIRDLEFCLEEHREKVNATEEMLQQEL----LSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEi 207
Cdd:pfam01576 338 EETRSHEAQLQEMRQKHTQALEELTEQLeqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 208 ndLRLKVSEMDSERLQYEKK-------LKSTKSLMAKLSSMKIKVG---------------QMQYE---KQRMEQKWESL 262
Cdd:pfam01576 417 --LQARLSESERQRAELAEKlsklqseLESVSSLLNEAEGKNIKLSkdvsslesqlqdtqeLLQEEtrqKLNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 263 KDELASLKEQLEEkESEVKRLQEKLVCKMKGEGVEivdrdenFKKKLKEKNIEVQ-------KMKKAVESLMAANEEKDR 335
Cdd:pfam01576 495 EDERNSLQEQLEE-EEEAKRNVERQLSTLQAQLSD-------MKKKLEEDAGTLEaleegkkRLQRELEALTQQLEEKAA 566
|
250 260
....*....|....*....|....
gi 1370463087 336 KIEDLRQCLNRYKKMQDTVVLAQG 359
Cdd:pfam01576 567 AYDKLEKTKNRLQQELDDLLVDLD 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
103-287 |
4.49e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEML---------QQELLS-------RTSLE 166
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaeieeRREELGeraralyRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 167 TQKLDLMAEISNLKlklTAVekDRLDYEDKFRDTEG-LIQEINDLRLKVSEmdsERLQYEKKLKSTKSLMAKLSSMKikv 245
Cdd:COG3883 102 VSYLDVLLGSESFS---DFL--DRLSALSKIADADAdLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAK--- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1370463087 246 GQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-291 |
6.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 133 KIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDK------FRDTEGLIQE 206
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 207 INDLRLKVSEMDSERLQyekklkstksLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK 286
Cdd:COG1579 98 IESLKRRISDLEDEILE----------LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*
gi 1370463087 287 LVCKM 291
Cdd:COG1579 168 LAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
201-363 |
7.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 201 EGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLK---DELASLKEQLEEKE 277
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 278 SEVKRLQEKL--VCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVV 355
Cdd:PTZ00121 1671 EEDKKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
....*...
gi 1370463087 356 LAQGKKGK 363
Cdd:PTZ00121 1751 KDEEEKKK 1758
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-284 |
1.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 100 DVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEfclEEHREKVNATEEMLQQellsrtsletqkldlmaEISNL 179
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELE---AQIRGNGGDRLEQLER-----------------EIERL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 180 KLKLTAVEKDRLDYEDKFRdtegliqeindlRLKVSEMDSERlQYEKKLKSTKSLMAKLSSmkikvgqmqyEKQRMEQKW 259
Cdd:COG4913 351 ERELEERERRRARLEALLA------------ALGLPLPASAE-EFAALRAEAAALLEALEE----------ELEALEEAL 407
|
170 180
....*....|....*....|....*
gi 1370463087 260 ESLKDELASLKEQLEEKESEVKRLQ 284
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-287 |
1.42e-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: 44.37 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEML-----------QQELLSRTSLETQKLD 171
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleaelaeleKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 172 L---------MAEISNLKLKLTAVEKD----RLDYEDKFrdTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKL 238
Cdd:COG4942 106 LaellralyrLGRQPPLALLLSPEDFLdavrRLQYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1370463087 239 SSMKIKVGQMQYEKQRMEQKwesLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG4942 184 EEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
51-368 |
1.83e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 51 LVEDLRGLLEMMETDEKeglrcQIPDSTA-----ETLVEWLQSQMTNghLPGNGDVYQERLARLENDKESLvlqvSVLTD 125
Cdd:pfam15921 480 VVEELTAKKMTLESSER-----TVSDLTAslqekERAIEATNAEITK--LRSRVDLKLQELQHLKNEGDHL----RNVQT 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 126 QVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVE--KDRLDyeDKFRDTEGL 203
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilKDKKD--AKIRELEAR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 204 IQEINDLRLKVSEMDSERLQYEKKLKSTKSLM---AKLSSMKIKVGQMQYE--KQRMEQKWESLKDELASLKEQLEEKES 278
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 279 EVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVVLAQ 358
Cdd:pfam15921 707 ELEQTRNTLK-SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
330
....*....|
gi 1370463087 359 GKKGkdGEYE 368
Cdd:pfam15921 786 NKMA--GELE 793
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-342 |
1.92e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 76 DSTAETLVEW-LQSQMTNGhlpgNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEM 154
Cdd:PRK02224 324 EELRDRLEECrVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 155 LQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQE------------------INDLRLKVSE 216
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetIEEDRERVEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 217 MDSERLQYEKK----------LKSTKSLMAKLSSMKIKVGQMQyekQRMEQKWESL---KDELASLKEQLEEKESEVkRL 283
Cdd:PRK02224 480 LEAELEDLEEEveeveerlerAEDLVEAEDRIERLEERREDLE---ELIAERRETIeekRERAEELRERAAELEAEA-EE 555
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370463087 284 QEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKaVESLMAANEEKDRKIEDLRQ 342
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLRE 613
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
104-346 |
2.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 104 ERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKvnateemlqqellsRTSLETqkldLMAEISNLKLKL 183
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER--------------REELET----LEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 184 TAVEKDRLDYEDKFRD----TEGLIQEINDLRlkvSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:PRK02224 268 AETEREREELAEEVRDlrerLEELEEERDDLL---AEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 260 ESLKDELASLKEQLEEKESEVKRLQEKLvckmKGEGVEIVDRDEnfkkKLKEKNIEVQKMKKAVESLMAANEEKDRKIED 339
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESEL----EEAREAVEDRRE----EIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
....*..
gi 1370463087 340 LRQCLNR 346
Cdd:PRK02224 417 LREERDE 423
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
184-287 |
2.32e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 184 TAVEKDRLDYEDKFRDTEGLIQ----EINDLRLKVSEMDSERLQYEKKLKSTKSLmaklssmkikvgqmQYEKQRMEQKW 259
Cdd:COG2433 402 EHEERELTEEEEEIRRLEEQVErleaEVEELEAELEEKDERIERLERELSEARSE--------------ERREIRKDREI 467
|
90 100
....*....|....*....|....*...
gi 1370463087 260 ESLKDELASLKEQLEEKESEVKRLQEKL 287
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELKRKL 495
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
218-361 |
2.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 218 DSERLQYEKKLKSTKS----LMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL-----V 288
Cdd:COG3883 15 DPQIQAKQKELSELQAeleaAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 289 CKMKGEGV-------------EIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQDTVV 355
Cdd:COG3883 95 LYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
....*.
gi 1370463087 356 LAQGKK 361
Cdd:COG3883 175 AQQAEQ 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
123-369 |
2.72e-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: 43.86 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 123 LTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEisnLKLKLTAVEKDRLDYEDKFRDTEG 202
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 203 LIQEINDLRLKVSEMDSERLQYEKKLKS-------------------------TKSLMAKLSSMKIKVGQMQYEKQRMEQ 257
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKlqqekellekeierlketiiknnseIKDLTNQDSVKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 258 KWESLKDELASLKEQLEEKESEVKRLQEKLVckmkgegvEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKI 337
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELK--------KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
250 260 270
....*....|....*....|....*....|..
gi 1370463087 338 EDLRQCLNRYKKMQDTVVLAQGKKGKDGEYEE 369
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKEIEE 572
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-355 |
3.03e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 119 QVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKlkltaVEKDRLDYEdKFR 198
Cdd:pfam10174 395 KINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLK-----EQREREDRE-RLE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 199 DTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKvgqmqyekqrMEQKWESLKDELASLKEQLEEKES 278
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLK----------KDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 279 EVKRLQEKLVCKMKGEgvEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEE-------KDRKIEDLRQCLNRYKKMQ 351
Cdd:pfam10174 539 QLKKAHNAEEAVRTNP--EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQ 616
|
....
gi 1370463087 352 DTVV 355
Cdd:pfam10174 617 NKKV 620
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-342 |
3.59e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 104 ERLARLENDKESLVLQVSvltdQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSletqkldlmaEISNLKLKL 183
Cdd:pfam05483 394 EEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK----------EIHDLEIQL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 184 TAVEKDRLDYedkFRDTEGLIQEINDLRLKVSEMDSE----RLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKW 259
Cdd:pfam05483 460 TAIKTSEEHY---LKEVEDLKTELEKEKLKNIELTAHcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 260 ESLKDELASLKEQLEEKESEVKRLQEKLVCKM-KGEGVEIVDRDENFKKKLKEKNIEVQ--KMKKAVESlmaaneeKDRK 336
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLdKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIEN-------KNKN 609
|
....*.
gi 1370463087 337 IEDLRQ 342
Cdd:pfam05483 610 IEELHQ 615
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
109-340 |
3.78e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 109 LENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEE---MLQQELLSRTSLETQKLDLMAEISNLKLKLTA 185
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 186 VEKDRLDYE------------------DKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQ 247
Cdd:PRK01156 268 ELEKNNYYKeleerhmkiindpvyknrNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 248 M-QYEKQRM-----EQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGV---EIVDRDENFKKKLKEKNIEVQK 318
Cdd:PRK01156 348 YdDLNNQILelegyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIdpdAIKKELNEINVKLQDISSKVSS 427
|
250 260
....*....|....*....|..
gi 1370463087 319 MKKAVESLMAANEEKDRKIEDL 340
Cdd:PRK01156 428 LNQRIRALRENLDELSRNMEML 449
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
102-369 |
4.17e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKL 181
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 182 KLTAVEKDRLDYEDKFRDTEGLIQEINDL--RLKVSEMDSERlqyEKKLKSTKSLMAKlssmKIKVGQMQYEKQRmeqKW 259
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERLewRQQTEVLSPEE---EKELVEKIKELEK----ELEKAKKALEKNE---KL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 260 ESLKDELASLKEQLEEKESEVKRLQEKLVcKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIED 339
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQ-ELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
250 260 270
....*....|....*....|....*....|
gi 1370463087 340 LRQCLNRYKKMQDTVVLAQGKKGKDGEYEE 369
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
205-342 |
5.69e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 205 QEINDLRLKVSEmdsERLQYEKKLKSTKSLMAklssmkikvgQMQYEKQRMEQKWESLKDELASLKEQLEEK-------- 276
Cdd:PRK00409 516 EKLNELIASLEE---LERELEQKAEEAEALLK----------EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikea 582
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463087 277 ESEVKRLQEKLVCKMKGEGVEIVDRD-ENFKKKLKEKNIEVQKMKKAVESLMAANEEKDR-KIEDLRQ 342
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKAHElIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvKYLSLGQ 650
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
164-341 |
5.99e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 164 SLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEmdserlQYEKKLKSTKSLMAKLssmkI 243
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEK------EAQQAIKEAKKEADEI----I 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 244 KVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEK------------LVCKMKGEGVEIVDRDE------NF 305
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKqeelkvgdevkyLSLGQKGEVLSIPDDKEaivqagIM 670
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1370463087 306 KKKLKEKNIEVQKMKKAVESLMAANE-EKDRKIE---DLR 341
Cdd:PRK00409 671 KMKVPLSDLEKIQKPKKKKKKKPKTVkPKPRTVSlelDLR 710
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
103-347 |
8.78e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKI-RDLEFCLEEHREKVNATEEmlqqellSRTSLETQKLDLMAEISNLKl 181
Cdd:PRK05771 56 SEALDKLRSYLPKLNPLREEKKKVSVKSLEELiKDVEEELEKIEKEIKELEE-------EISELENEIKELEQEIERLE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 182 KLTAVEKDrLDYEDKFRDTE---GLIQEINDLRLKvSEMDSERLQYEKKLKSTKSLMA-KLSSMKIKVG----QMQYEKQ 253
Cdd:PRK05771 128 PWGNFDLD-LSLLLGFKYVSvfvGTVPEDKLEELK-LESDVENVEYISTDKGYVYVVVvVLKELSDEVEeelkKLGFERL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 254 RMEQKwESLKDELASLKEQLEEKESEVKRLQEKLvckmkgegVEIVDRDENFKKKLKEKN-IEVQkmkKAVESLMAANEE 332
Cdd:PRK05771 206 ELEEE-GTPSELIREIKEELEEIEKERESLLEEL--------KELAKKYLEELLALYEYLeIELE---RAEALSKFLKTD 273
|
250 260
....*....|....*....|....
gi 1370463087 333 K---------DRKIEDLRQCLNRY 347
Cdd:PRK05771 274 KtfaiegwvpEDRVKKLKELIDKA 297
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
102-527 |
9.86e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLENDKESLVlqvSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELlsrtslETQKLDLMAEISNLKL 181
Cdd:PTZ00108 986 YLVRLDLYKKRKEYLL---GKLERELARLSNKVRFIKHVINGELVITNAKKKDLVKEL------KKLGYVRFKDIIKKKS 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 182 KLTAVEKDrldyEDKFRDTEGLIQEINDLRLKVSEMDserlqYekklkstkslmakLSSMKIkvgqmqyekqrmeqkWES 261
Cdd:PTZ00108 1057 EKITAEEE----EGAEEDDEADDEDDEEELGAAVSYD-----Y-------------LLSMPI---------------WSL 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 262 LKDELASLKEQLEEKESEVKRLQEKLVCKM-------------KGEGVEIVDRDE----NFKKKLKEKNIEVQKMKKAVE 324
Cdd:PTZ00108 1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMwledldkfeealeEQEEVEEKEIAKeqrlKSKTKGKASKLRKPKLKKKEK 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 325 SLMAANEEKDRKIEDLRqclnRYKKMQDTVVLAQGKKGKDGEYEELLNSSSISSLLDAQGFSDLEKSPSPTPVMGSPScd 404
Cdd:PTZ00108 1180 KKKKSSADKSKKASVVG----NSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKS-- 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 405 pfntsvPEEFHTTILQVSIPSLLPATVSMETSEKSKLTPKPET-SFEENDGNIILGATVDTQLCDKLLTSSLQKSSSLGN 483
Cdd:PTZ00108 1254 ------SEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKrPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKS 1327
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1370463087 484 LKKETSDGEKetiqKTSEDRAPAESRPFGTLPPRPPGQDTSMDD 527
Cdd:PTZ00108 1328 EKKTARKKKS----KTRVKQASASQSSRLLRRPRKKKSDSSSED 1367
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
68-342 |
1.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 68 EGLRCQIPDSTAETLVEWLQSQMTNGHLPGNGDVYQERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREK 147
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 148 VNATEEML----QQELLSRTSLE-TQKLDLM---------------AEISNLKLKLTAVEKDRLDYEDKFRDTEGLI--- 204
Cdd:pfam10174 533 CSKLENQLkkahNAEEAVRTNPEiNDRIRLLeqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTlrq 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 205 -----QEINDLRLKVSEMDSERLQ-YEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRmeQKWESLKDELASLKEQLEEKES 278
Cdd:pfam10174 613 mkeqnKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDG 690
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370463087 279 EV--------KRLQEKLVCKMKGEGVEIVDRDENFKkkLKEknIEVQKMKKAVESLMAANEEKDRKIEDLRQ 342
Cdd:pfam10174 691 HLtnlraerrKQLEEILEMKQEALLAAISEKDANIA--LLE--LSSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| DUF16 |
pfam01519 |
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only ... |
105-156 |
1.77e-03 |
|
Protein of unknown function DUF16; The function of this protein is unknown. It appears to only occur in Mycoplasma pneumoniae. The crystal structure revealed that this domain is composed of two separated homotrimeric coiled-coils.
Pssm-ID: 396208 [Multi-domain] Cd Length: 95 Bit Score: 37.89 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1370463087 105 RLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQ 156
Cdd:pfam01519 26 RLTKIETKVDKLGEQINKLEQKVDKQGEQIKELQVEQKAQGEQINAVGETLQ 77
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-338 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLK 182
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 183 LTAVEKDRLDYEdkfRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAklssmkikvgqmqyekQRMEQKWESL 262
Cdd:TIGR02168 903 LRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL----------------EEAEALENKI 963
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463087 263 KDELASLKEQLEEKESEVKRLqeklvckmkGE-GVEIVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 338
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKEL---------GPvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
100-351 |
2.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 100 DVYQERLaRLENDKESLVLQVSVL-TDQVEAQ--GEKIRD--LEFCLEEHREKVNATEEMLQQELlsrTSLETQKLDLMA 174
Cdd:COG3206 121 ERLRKNL-TVEPVKGSNVIEISYTsPDPELAAavANALAEayLEQNLELRREEARKALEFLEEQL---PELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 175 EISNLKLK--LTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLS------SMKIKVG 246
Cdd:COG3206 197 ALEEFRQKngLVDLSEEAKLLLQQLSELE---SQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviqQLRAQLA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 247 QMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVESL 326
Cdd:COG3206 274 ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
250 260
....*....|....*....|....*
gi 1370463087 327 MAANEEKDRKIEDLRQCLNRYKKMQ 351
Cdd:COG3206 354 RRLEREVEVARELYESLLQRLEEAR 378
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-349 |
2.17e-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: 41.21 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 251 EKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKL------VCKMKGEGVEIVDRDENFKKKLKEKNIEVQKMKKAVE 324
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100
....*....|....*....|....*
gi 1370463087 325 SLMAANEEKDRKIEDLRQCLNRYKK 349
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEE 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
110-349 |
2.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 110 ENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ----ELLSRTSLETQKLDL------MAEISNL 179
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelaEQLKELEEKLKKYNLeelekkAEEYEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 180 KLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKL-----KSTKSLMAKLSSMK------IKVGQM 248
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEpfyneyLELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 249 QYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEivdRDENFKKKLKEKNIEVQKMKKAVESLMA 328
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEK 687
|
250 260
....*....|....*....|.
gi 1370463087 329 ANEEKDRKIEDLRQCLNRYKK 349
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREK 708
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
132-349 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 132 EKIRDLEFCLEEHREKVNATEEMLQQELLSRTSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDlR 211
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-Q 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 212 LKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEklvckm 291
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR------ 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370463087 292 kgegveivdrdenfkkKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKK 349
Cdd:TIGR04523 364 ----------------ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
125-350 |
3.51e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 125 DQVEAQGEKIRDLEFCLEEHREK----VNATEEMLQQEL--LSRT--SLETQKLDLMAEISNLKLkltAVEKDRLDYEDK 196
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELRQKkgaePSRLYSLYEKEIedLRRQldTLTVERARLQLELDNLRL---AAEDFRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 197 FRDTEGLIQEINDLRLKVSEMDSERLQYEKKLkstkslmaklssmkikvgqmqyekqrmeqkwESLKDELASLKEQLEEk 276
Cdd:pfam00038 95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKI-------------------------------ESLKEELAFLKKNHEE- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370463087 277 esEVKRLQEKLvckmkGEGVEIVDRDENFKKKLKE--KNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNRYKKM 350
Cdd:pfam00038 143 --EVRELQAQV-----SDTQVNVEMDAARKLDLTSalAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDA 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
103-314 |
3.79e-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: 40.42 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVSVLTDQVEAQGE-------KIRDLEFCLEEHREKVNATE----------EMLQQELLSRTSL 165
Cdd:TIGR01612 1536 KNKFAKTKKDSEIIIKEIKDAHKKFILEAEkseqkikEIKKEKFRIEDDAAKNDKSNkaaidiqlslENFENKFLKISDI 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 166 ETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDtegliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKV 245
Cdd:TIGR01612 1616 KKKINDCLKETESIEKKISSFSIDSQDTELKENG-----DNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDV 1690
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370463087 246 GQMQ--YEKQRMEQkwesLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKKKLKEKNI 314
Cdd:TIGR01612 1691 DQHKknYEIGIIEK----IKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGD 1757
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
103-341 |
4.14e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 103 QERLARLENDKESLVLQVS-VLTDQVEAQGEKIRDLE------------FCLEEHREKVNATEEMLQ--QELLSRTSLET 167
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNkALAERKDSANERLNSLEaqlkqldkkhqaWLEEQKEQKREARTEKQAywQVVEGALDAQL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 168 QKLD--LMAEISNLKLKLTAVEKDRlDYEDKFRDTEG-----LIQEINDLRLKVSEMDSER---LQYEKKLKSTKSLmak 237
Cdd:pfam12128 732 ALLKaaIAARRSGAKAELKALETWY-KRDLASLGVDPdviakLKREIRTLERKIERIAVRRqevLRYFDWYQETWLQ--- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 238 lssmkikvgqmqyEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDENFKK-KLKEKNIEV 316
Cdd:pfam12128 808 -------------RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGlRCEMSKLAT 874
|
250 260
....*....|....*....|....*
gi 1370463087 317 QKMKKAVESLMAANEEKDRKIEDLR 341
Cdd:pfam12128 875 LKEDANSEQAQGSIGERLAQLEDLK 899
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
221-338 |
4.29e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.03 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 221 RLQYEKKLKSTKSLMAKlssmkiKVGQMQYEKQRMEQKWESLKDELASLK---EQLEEKESEVKRLQEKLVCKMKGEGVE 297
Cdd:pfam10168 545 REEYLKKHDLAREEIQK------RVKLLKLQKEQQLQELQSLEEERKSLSeraEKLAEKYEEIKDKQEKLMRRCKKVLQR 618
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1370463087 298 IVDRDENFKKKLKEKNIEVQKMKKAVESLMAANEEKDRKIE 338
Cdd:pfam10168 619 LNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMN 659
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
232-342 |
4.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 232 KSLMAKLSSMKIKVGQM--QYEKQRMEQKWESL---KDELASLKEQLE----EKESEVKRLQEKLVckmkgegveivDRD 302
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRIleEAKKEAEAIKKEALleaKEEIHKLRNEFEkelrERRNELQKLEKRLL-----------QKE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370463087 303 ENFKKK---LKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQ 342
Cdd:PRK12704 96 ENLDRKlelLEKREEELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-349 |
6.06e-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: 39.62 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 106 LARLENDKESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQ--ELLSRTSLETQKLDLMAEISNLKLKL 183
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 184 TAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLSSMKIKVgqmQYEKQRMEQKWESLK 263
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKE---KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI---KSKKNKLKQEVKQIK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 264 DELASLKEQLEEKESEVKRLQEKlvckmkgegveIVDRDENFKKKLKEKNIEVQK--MKKAVESLMAANEEKDRKIEDLR 341
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTK-----------IDDIIELMKDWLKELSLHYKKyiTRMIRIKDLPKLEEKYKEIEKEL 720
|
....*...
gi 1370463087 342 QCLNRYKK 349
Cdd:TIGR04523 721 KKLDEFSK 728
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-350 |
6.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 104 ERLARLEN--DKESLVLQVSVLTDQVEAQGEK-----IRDLEFCLEEHRE------KVNATEEMLQQELLSRTSLETQKL 170
Cdd:PRK03918 480 KELRELEKvlKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKlkekliKLKGEIKSLKKELEKLEELKKKLA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 171 DLMAEISNLKLKLTAVEK--DRLDYEDkFRDTEGLIQEIND-----LRLKVSEMDSERLQYE-KKLKST----------- 231
Cdd:PRK03918 560 ELEKKLDELEEELAELLKelEELGFES-VEELEERLKELEPfyneyLELKDAEKELEREEKElKKLEEEldkafeelaet 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 232 ----KSLMAKLSSMKIKVGQMQYEkqRMEQKWESLKDELASLKEQLEEKES---EVKRLQEKLvckmkgegveivdrdEN 304
Cdd:PRK03918 639 ekrlEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKrreEIKKTLEKL---------------KE 701
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370463087 305 FKKKLKEKNIEVQKMKKAVEslmaaneekdrKIEDLRQCLNRYKKM 350
Cdd:PRK03918 702 ELEEREKAKKELEKLEKALE-----------RVEELREKVKKYKAL 736
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
267-349 |
6.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 267 ASLKEQLEEKESEVKRLQEKLVCKMKGEGVEIVDRDEnfkKKLKEKNIEVQKMKKAVESLMAANEEKDRKIEDLRQCLNR 346
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE---EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
...
gi 1370463087 347 YKK 349
Cdd:COG2433 453 ARS 455
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
163-349 |
7.77e-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: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 163 TSLETQKLDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSlmaklssmk 242
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ--------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 243 iKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKRLQEKLVCKMKGEG---VEIVD----RDENFKKKLKEKNIE 315
Cdd:TIGR04523 240 -EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDlnnqKEQDWNKELKSELKN 318
|
170 180 190
....*....|....*....|....*....|....
gi 1370463087 316 VQKMKKAVESLMAANEEkdrKIEDLRQCLNRYKK 349
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNK---IISQLNEQISQLKK 349
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
102-351 |
8.46e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 102 YQERLARLENDKESLVLQVSVLTdqveaqgEKIRDLEfCLEEHREKVNATEEMLQQELLSrtSLETQKLDLMAEISNLKL 181
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDID-------EKIVDLK-KRKEYLESEEINKSINEYNKIE--SARADLEDIKIKINELKD 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 182 KLTAVEKDRLDYED-KFRDTEGLIQEINDLRLKVSEMDSE--RLQYEKKLKSTKSLMAKLSSMKIK-----------VGQ 247
Cdd:PRK01156 544 KHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIDIEtnRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIRE 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 248 MQYEKQRMEQKW----------ESLKDELASLKEQLEEKESEVKRLQEklvckMKGEGVEIVDRDENFKKKLKEKNIEVQ 317
Cdd:PRK01156 624 IENEANNLNNKYneiqenkiliEKLRGKIDNYKKQIAEIDSIIPDLKE-----ITSRINDIEDNLKKSRKALDDAKANRA 698
|
250 260 270
....*....|....*....|....*....|....
gi 1370463087 318 KMKKAVESLMAANEEKDRKIEDLRQCLNRYKKMQ 351
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLESMKKIK 732
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
170-340 |
8.96e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.96 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 170 LDLMAEISNLKLKLTAVEKDRLDYEDKFRDTEgliQEINDLRLKVSEMDSERLQYEKKLK-------STKSLMAKLSSMK 242
Cdd:pfam13851 22 RNNLELIKSLKEEIAELKKKEERNEKLMSEIQ---QENKRLTEPLQKAQEEVEELRKQLEnyekdkqSLKNLKARLKVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 243 IKVGQMQYEKQRMEQKWESLKDELASLKEQLEEKESEVKR--------LQEKLvcKMKGEGVEIvdRDENFKKKLKEKNI 314
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglknllLEKKL--QALGETLEK--KEAQLNEVLAAANL 174
|
170 180
....*....|....*....|....*.
gi 1370463087 315 EVQKMKKAVESLMAANEEKDRKIEDL 340
Cdd:pfam13851 175 DPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
114-351 |
9.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 114 ESLVLQVSVLTDQVEAQGEKIRDLEFCLEEHREKVNATEEMLQQellsRTSLETQKLDLMAEISNLKLKLTAVEKDRLDY 193
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQ----IADDEKSHSITLKEIERLSIEYNNAMDDYNNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 194 EDKFRDTEGLIQEINDLRLKVSEMDSERLQYEKKLKSTKSLMAKLssMKIKVGQMQYEKQRMEQKWeSLKDELASLKEQL 273
Cdd:PRK01156 238 KSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH--MKIINDPVYKNRNYINDYF-KYKNDIENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 274 EEKESEVKRLQEklvcKMKGEGVEIVDRDENFKKK------------LKEKNIEVQKMKKAVESLMAANEEKDRKIEDLR 341
Cdd:PRK01156 315 SNIDAEINKYHA----IIKKLSVLQKDYNDYIKKKsryddlnnqileLEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS 390
|
250
....*....|
gi 1370463087 342 QCLNRYKKMQ 351
Cdd:PRK01156 391 AFISEILKIQ 400
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-342 |
9.49e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.95 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 77 STAETLVEWLQSQMtnghlpgngDVYQERlARLEN--------DKESLVLQV-SVLTDQVEAQGEKIRDLEFCLEEHREK 147
Cdd:pfam15921 288 SSARSQANSIQSQL---------EIIQEQ-ARNQNsmymrqlsDLESTVSQLrSELREAKRMYEDKIEELEKQLVLANSE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 148 VnaTEEMLQQELLSRTS--LETQKLDLMAEISNLKLKLTAVEKDRLDYEDkfRDTEGLIQeINDLRLKVSEMDSERLQYE 225
Cdd:pfam15921 358 L--TEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWD--RDTGNSIT-IDHLRRELDDRNMEVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370463087 226 KKLKSTKSLMAklssmkikvGQMQYEKQRMEQKWESLkDELASLKEQLEEKESEVKRLQEKLVC-KMKGEGVEIVDRDEN 304
Cdd:pfam15921 433 ALLKAMKSECQ---------GQMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSERTVSDLT 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370463087 305 FKKKLKEK-----NIEVQKMKKAV------------------------ESLMAANEEKDRKIEDLRQ 342
Cdd:pfam15921 503 ASLQEKERaieatNAEITKLRSRVdlklqelqhlknegdhlrnvqtecEALKLQMAEKDKVIEILRQ 569
|
|
| |
