|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
110-421 |
1.95e-136 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 396.21 E-value: 1.95e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 110 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKL-QFYQNRECCQSNLEPLFAGYIETLRREAECVEADSGRLASELNHV 188
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 189 QEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRILQSHISDTSVVVKL 268
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 269 DNSRDLNMDCIVAEIKAQYDDIATRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQN 348
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169790841 349 SKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQR 421
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
4-107 |
6.39e-15 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 72.00 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 4 GFNSIGCGFRPGNF---SCVSACGPR---PSRCCITAAPYRGISCYRGLTGGFGSHS---VCGGFRAGSCGRS------- 67
Cdd:pfam16208 27 GGGGGGGGGGGGGFgsrSLYNLGGSKsisISVAGGGSRPGSGFGFGGGGGGGFGGGFgggGGGGFGGGGGFGGgfggggy 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 169790841 68 ---------FGYRSGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 107
Cdd:pfam16208 107 ggggfggggFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-441 |
5.05e-13 |
|
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: 71.64 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 110 EEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECcQSNLEP----LFAGYIETLRREAECVEADSGRLASEL 185
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQAL-LKEKREyegyELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 186 NHVQEVLEGYKKKYEEEVALRATA--------ENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---RRLYEEEIRI 254
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 255 LQSHISDTSVVVKLDNSRDLNMDCIVAEIKAQYDDIatRSRAEAESwyrskcEEMKATVIRHG---ETLRRTKEEINELN 331
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD------KEFAETRDELKdyrEKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 332 RMIQRLTAEVENAKCQNSKLEAAVAQSEQ---QGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMN--------- 399
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvekel 485
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 169790841 400 SKLGLDIEIATYRRLLEGEEQRlceGVEAVNVCVSSSRGGVV 441
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVR---GGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-361 |
3.33e-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: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 109 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN-RECCQSNLEPLFAGY------IETLRREAECVEADSGRL 181
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeLEQLRKELEELSRQIsalrkdLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 182 ASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRILQSH 258
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 259 ISDT--SVVVKLDNSRDLNMDciVAEIKAQYDDIAT---RSRAEAESWYRSKcEEMKATVIRHGETLRRTKEEINELNRM 333
Cdd:TIGR02168 833 IAATerRLEDLEEQIEELSED--IESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELESK 909
|
250 260
....*....|....*....|....*...
gi 169790841 334 IQRLTAEVENAKCQNSKLEAAVAQSEQQ 361
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
156-383 |
5.79e-07 |
|
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: 52.48 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 156 LEPLFAGYIETLRREAECVEAdsgrLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVE 235
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRN----VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 236 ALiqeidflrrlyEEEIRILQSHISDtsVVVKLDNSRDL--NM-------DCIVAE---IKAQYDDiaTRSRAEAESwyR 303
Cdd:pfam01576 570 KL-----------EKTKNRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--R 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 304 SKceEMKA-TVIRHGETLRRTKEEINELNRMiqrLTAEVE---NAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGA 379
Cdd:pfam01576 633 EK--ETRAlSLARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDE 707
|
....
gi 169790841 380 LQKA 383
Cdd:pfam01576 708 LQAT 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-413 |
4.20e-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: 48.99 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVdcaylrkSDLEANVEALIQEIDF 243
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 244 LRRLYEEEIRILQSHISDTSVVVKLdNSRDLNmdciVAEIKAQYDDIATRSRAEaeswyrskceemkatvirHGETLRRT 323
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLL-SPEDFL----DAVRRLQYLKYLAPARRE------------------QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 324 KEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLG 403
Cdd:COG4942 159 LAELAALRAELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|
gi 169790841 404 LDIEIATYRR 413
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
203-396 |
8.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 203 VALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRILQSHISDTSvvvklDNSRDLNmdci 279
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQ-----AEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 280 vAEIKAQYDDIATRSRAEAESWYRSKCEEM------KATVIRHGETLRR----TKEEINELNRMIQRLT---AEVENAKC 346
Cdd:COG3883 79 -AEIEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKiadaDADLLEELKADKAELEakkAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 169790841 347 QNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQE 396
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-422 |
1.17e-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: 48.13 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 195 YKKKYEE-EVALRATAEN----EFVA--LKKDVDcaylrksDLEANVEALIQEIDflrrlYEEEIRILQSHISDTSVVVK 267
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEKAERYKE-----LKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 268 LDNSRDLNMdcIVAEIKAQYDDIATRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAK 345
Cdd:TIGR02168 238 REELEELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 346 CQNSKLEAAVAQSEQQGE---AALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 422
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
108-398 |
2.51e-05 |
|
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: 46.81 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 108 KQEEKEQIKSLNSRfAAFIDKVRFLEQQNKLLETKLQfyQNREccqsNLEPLFAGYIETLRREAECVEADSGRLASELNH 187
Cdd:pfam07888 55 RQREKEKERYKRDR-EQWERQRRELESRVAELKEELR--QSRE----KHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 188 VQEVLE-------GYKKKYEEEVALRATAE--NEFVALKKDVdcaYLRKSDLEANVEALIQEidfLRRLYEE-------- 250
Cdd:pfam07888 128 EARIREleediktLTQRVLERETELERMKEraKKAGAQRKEE---EAERKQLQAKLQQTEEE---LRSLSKEfqelrnsl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 251 -----EIRILQSHISDTSVVVKLDNSRDLNMDCIVAEIKAQYDDIAT------------------RSRAEAEsWYRSKCE 307
Cdd:pfam07888 202 aqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNAserkveglgeelssmaaqRDRTQAE-LHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 308 ----------------EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALS 367
Cdd:pfam07888 281 aaqltlqladaslalrEGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|.
gi 169790841 368 DARCKLAELEGALQKAKQDMACLIREYQEVM 398
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
96-416 |
3.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 96 LNLEIDPNAQCVKQEE--KEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLqfyqnrECCQSNLEPL--FAGYIETLRREA 171
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREEL------EKLEKEVKELeeLKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 172 ECVEADSGRLASELNHVQEVLEGYKKKYEEevaLRATAEnEFVALKKDVDcAYLRKSDLEANVEALIQEIDFLRRLYEEE 251
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 252 IRILQSHISDTSVvvklDNSRDLNMDCIVAEIKAQYDDIATRSR---------AEAESWYRSKCEEMKATVIRHGETLRR 322
Cdd:PRK03918 323 INGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHElyeeakakkEELERLKKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 323 TKEE----INELNRMIQRLTAEVENAKCQNSKLEAAVAQ--------SEQQGEAALSDARCKLAELEGALQKAKQDMACL 390
Cdd:PRK03918 399 AKEEieeeISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340
....*....|....*....|....*.
gi 169790841 391 IREYQEVmNSKLGLDIEIATYRRLLE 416
Cdd:PRK03918 479 RKELREL-EKVLKKESELIKLKELAE 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
174-377 |
7.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 174 VEADSGRLASELNHVQEVLEGYKKKYEE-EVALRA-TAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEe 251
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 252 iriLQSHISDTSvvvklDNSRDLNMDCIVAEIKAQYDDIATRsRAEAESWYRSKCEEMKATVirhgETLRRTKEEIN-EL 330
Cdd:COG3206 245 ---LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----AQIAALRAQLQqEA 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 169790841 331 NRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGeAALSDARCKLAELE 377
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-396 |
7.74e-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: 45.44 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 165 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL 244
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 245 RRL-----------------YEEEIRILQSHISDTSVVVKLDNSRDLNMdcIVAEIKAQYDDI----------------- 290
Cdd:TIGR02169 757 KSElkelearieeleedlhkLEEALNDLEARLSHSRIPEIQAELSKLEE--EVSRIEARLREIeqklnrltlekeyleke 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 291 ---ATRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQR---LTAEVENAKCQNSKLEaavaQSEQQGEA 364
Cdd:TIGR02169 835 iqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELE----RKIEELEA 910
|
250 260 270
....*....|....*....|....*....|..
gi 169790841 365 ALSDARCKLAELEGALQKAKQDMACLIREYQE 396
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
164-383 |
1.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDcaylrksDLEANVEALIQEI-D 242
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 243 FLRRLYEEEirilqshiSDTSVVVKLDNSRDLN--------MDCIVAEIKAQYDDIATRsRAEAESwYRSKCEEMKATVI 314
Cdd:COG3883 91 RARALYRSG--------GSVSYLDVLLGSESFSdfldrlsaLSKIADADADLLEELKAD-KAELEA-KKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169790841 315 RHGETLRRTKEEIN----ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKA 383
Cdd:COG3883 161 ALKAELEAAKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
97-396 |
1.03e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 97 NLEIDPNAQcVKQEEKEQIKSLnsRFAAFIDKVRFLEQQNKLL-ETKLQFYQNRECCQSNLEPLfAGYIETLrrEAECVE 175
Cdd:PLN02939 108 IAAIDNEQQ-TNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLnQARLQALEDLEKILTEKEAL-QGKINIL--EMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 176 ADSG-RLASELNHVQEVLEGYKKKYEEEVALRATAENEFV-ALKKDVDCAYLRKSDLEANVEALIQEIdflrrlyeeeir 253
Cdd:PLN02939 182 TDARiKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDVLKEENMLLKDDIQFLKAEL------------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 254 ilqSHISDT-SVVVKLDNSRDLnMDCIVAEIKAQY----DDIATRSRAEAESWYrskceemkatvirhgetlrrtkEEIN 328
Cdd:PLN02939 250 ---IEVAETeERVFKLEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWW----------------------EKVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 329 ELNRMIQRLTAEVENAKC---QNSKLEAAVAQSEQQ-GEAALSDARC--------KLAELEGALQKAKQDMACLIREYQE 396
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASlKEANVSKFSSykvellqqKLKLLEERLQASDHEIHSYIQLYQE 383
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-380 |
1.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 108 KQEEKEQIKSLNSRFAAFIDKV-----RFLEQQNKL--LETKLQFYQNR-ECCQSNLEPLfAGYIETLRREAECVEADSG 179
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIeelqkELYALANEIsrLEQQKQILRERlANLERQLEEL-EAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 180 RLASELNHVQEVLEGYKKKYEEEVALRATAEN-------EFVALKKDVDCAYL--------------RKSDLEANVEALI 238
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESrleeleeQLETLRSKVAQLELqiaslnneierleaRLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 239 QEIDFLRRLYEEeirilqshisdtsvvvkldnsrdlnmdcivAEIKAQYDDIATRSRAEaeswyrskcEEMKATVIRHGE 318
Cdd:TIGR02168 421 QEIEELLKKLEE------------------------------AELKELQAELEELEEEL---------EELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169790841 319 TLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAV--AQSEQQGEAALSDARCKLAELEGAL 380
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-422 |
1.61e-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: 44.24 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 110 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLET-------------KLQFYQNRECC--QSNLEPLFAGYiETLRREAECV 174
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVelnklekqkkenkKNIDKFLTEIKkkEKELEKLNNKY-NDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 175 EADSGRLASELNHVQE-----------------VLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEAL 237
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKnidkiknkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 238 IQEIDFLRRLYEEEIRILQSHISDtsvvVKLDNSRDLNMDCIVAEIKAQYDDIATRSRAEAESWYRSKCEEMKATVIRHG 317
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 318 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEgALQKAKQDMACLIREYQEV 397
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
330 340
....*....|....*....|....*...
gi 169790841 398 MNSKlglDIEIATY---RRLLEGEEQRL 422
Cdd:TIGR04523 407 NQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-422 |
2.38e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREA-----------ECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKdvdcaylRKSDLEA 232
Cdd:COG1196 202 LEPLERQAekaeryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 233 NVEALIQEIDFLR-RLYEEEIRILQshisdtsvvvkLDNSRDLNmdcivAEIKAQYDDIATRSRAEAESWyRSKCEEMKA 311
Cdd:COG1196 275 ELEELELELEEAQaEEYELLAELAR-----------LEQDIARL-----EERRRELEERLEELEEELAEL-EEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 312 TVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAV---AQSEQQGEAALSDARCKLAELEGALQKAKQDMA 388
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270
....*....|....*....|....*....|....
gi 169790841 389 CLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 422
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-422 |
2.45e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 174 VEADSGRLA--SELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRR---LY 248
Cdd:TIGR02168 666 AKTNSSILErrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 249 EEEIRILQSHISDtsvvvkldnsrdlnmdcIVAEIKAQYDDIATRSRAEAESwyRSKCEEMKATVIRH-------GETLR 321
Cdd:TIGR02168 746 EERIAQLSKELTE-----------------LEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLkeelkalREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 322 RTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEVMNSK 401
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
250 260
....*....|....*....|.
gi 169790841 402 LGLDIEIATYRRLLEGEEQRL 422
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEEL 903
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-386 |
3.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREAECVEADSGRLASELNHVQEVlegykKKYEEEVALRATAENEFVALKKDVdcaylRKSDLEANVEAlIQEIDF 243
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARKAEAARKAEEERKAEEA-----RKAEDAKKAEA-VKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 244 LRRLYEEEIRilQSHISDTSVVVKLDNSRDLNMDCIVAEIKAQYDDIATRSRAEAEswyRSKCEEM-KATVIRHGETLRR 322
Cdd:PTZ00121 1235 AKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169790841 323 TKEEinelNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQD 386
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
117-370 |
4.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 117 SLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccqsnleplfagyIETLRREAECVEadsgrLASELNHVQEVLEGYK 196
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFRQKNGLVD-----LSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 197 KKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEAN--VEALIQEIDFLRRLYEEEIRILQShisDTSVVVKLDNSRdl 274
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP---NHPDVIALRAQI-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 275 nmdcivAEIKAQYDDIATRSRAEAESWYrskcEEMKATVIRHGETLRRTKEEINELNRM---IQRLTAEVENAKCQNSKL 351
Cdd:COG3206 301 ------AALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESL 370
|
250
....*....|....*....
gi 169790841 352 EAAVAQSEQQGEAALSDAR 370
Cdd:COG3206 371 LQRLEEARLAEALTVGNVR 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
279-396 |
5.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 279 IVAEIKAQYDDIatrsRAEAESWYRSKCEEMKA---TVIRHGETLRRTKEEI----NELNRMIQRLTAEVENAKCQNSKL 351
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKlekRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 169790841 352 EAAVAQSEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLIREYQE 396
Cdd:PRK12704 134 EELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
97-413 |
5.76e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 97 NLEIDPNAQCVKQEEK------EQIKSLNSRFAAFIDKVRFLEQQ----NKLLETKLQFYQNRECCQSNL--EPLFAGYI 164
Cdd:PRK01156 196 NLELENIKKQIADDEKshsitlKEIERLSIEYNNAMDDYNNLKSAlnelSSLEDMKNRYESEIKTAESDLsmELEKNNYY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 165 ETLRREAECVEADSG-----------RLASELNHVQEVLEGYK---KKYEEevALRATAE-----NEFVALKKDVDCAYL 225
Cdd:PRK01156 276 KELEERHMKIINDPVyknrnyindyfKYKNDIENKKQILSNIDaeiNKYHA--IIKKLSVlqkdyNDYIKKKSRYDDLNN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 226 RKSDL---EANVEALIQEIDFL---RRLYEEEIRILQSHISDTSVVVKLDNSRdlnMDCIVAEIKAQYDDIATR------ 293
Cdd:PRK01156 354 QILELegyEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKLQDISSKvsslnq 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 294 ------------SRAEAESWYRSKC--------EEMKATVIRH-GETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLE 352
Cdd:PRK01156 431 riralrenldelSRNMEMLNGQSVCpvcgttlgEEKSNHIINHyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169790841 353 AAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMAclirEYQEVMNSKLGLDIEIATYRR 413
Cdd:PRK01156 511 SEEINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLDSKR 567
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
108-369 |
7.64e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 108 KQEEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECCQSNleplfagyIETLRREAECV--EADSGRLASEL 185
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKR--ETETGIQNLTAEIEQGQESLTEN--------LEAIKEEIENIvgEVELSKSSEEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 186 NHVQEVLEGYKKKYEEEVALRATAENEFVALKKDvdcaylRKSDLEANVEALIQEIDFLRRLYEEEIRILQSHISDtsvv 265
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLLNELISE---- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 266 vkLDNSRDLNMDCIVAEIKAQYDDIATRSRaeaeswyrskceemkatvirhgETLRRTKEEINELNRMIQRLTAEVENAK 345
Cdd:COG5185 450 --LNKVMREADEESQSRLEEAYDEINRSVR----------------------SKKEDLNEELTQIESRVSTLKATLEKLR 505
|
250 260
....*....|....*....|....
gi 169790841 346 CQNSKLEAAVAQSEQQGEAALSDA 369
Cdd:COG5185 506 AKLERQLEGVRSKLDQVAESLKDF 529
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
307-422 |
7.97e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 307 EEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQgeaalsdarckLAELEGALQKAKQD 386
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDER-----------IERLERELSEARSE 456
|
90 100 110
....*....|....*....|....*....|....*.
gi 169790841 387 MACLIREYQEVMNsklgLDIEIATYRRLLEGEEQRL 422
Cdd:COG2433 457 ERREIRKDREISR----LDREIERLERELEEERERI 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
230-422 |
9.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 230 LEANVEALIQEIDFLRRLyEEEIRILQSHISdtsvvvKLDNSRDLnmdciVAEIKAQYDDIATRSRAEAEswYRSKCEEM 309
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELE------ELREELEK-----LEKLLQLLPLYQELEALEAE--LAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 310 katvirhgETLRRTKEEINELNRMIQRLTAEVENAKcqnSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMAC 389
Cdd:COG4717 149 --------EELEERLEELRELEEELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|...
gi 169790841 390 LIREYQEVMNsklglDIEIATYRRLLEGEEQRL 422
Cdd:COG4717 218 AQEELEELEE-----ELEQLENELEAAALEERL 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
318-402 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 318 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 397
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 169790841 398 MNSKL 402
Cdd:COG4372 177 SEAEA 181
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
281-388 |
1.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 281 AEIKAQYDDIATRSRAEAESwyrskceemKATVIRHGETLR------RTKEEINELNRMIQRLTAEVENAKCQNSKLEAA 354
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 169790841 355 VAQSEQQGEAALSDARC--KLAELEGALQKAKQDMA 388
Cdd:PRK11281 110 NDEETRETLSTLSLRQLesRLAQTLDQLQNAQNDLA 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
320-422 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 320 LRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQ---GEAALSDARCKLAELEGALQKAKQDMACLIREYQE 396
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 169790841 397 VMNSKLGLDIEIATYRRLLEGEEQRL 422
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
320-428 |
1.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 320 LRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAA-----LSDARCKLAELEGALQKAKQDmaclIREY 394
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEER----LEEL 158
|
90 100 110
....*....|....*....|....*....|....
gi 169790841 395 QEVMNSKLGLDIEIATYRRLLEGEEQRLCEGVEA 428
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
110-430 |
2.05e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 110 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN---RECCQSNLEPLFAGYIETLRREAECVEADSGRLASELN 186
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaqDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 187 HVQEVLegykKKYEEEVA-LRATAENEFVALKKDVdcAYLRKsdLEANVEALIQEIDFLRRLYEEEIRILQSHISDTSVV 265
Cdd:pfam05557 308 QLEKAR----RELEQELAqYLKKIEDLNKKLKRHK--ALVRR--LQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 266 VKLDNSRDL--NMDCIVAEIKAQYddiatrSRAEAE-SWYRSKCE--EMKATVIRHGETLR---RTKEEINELNRMIQRL 337
Cdd:pfam05557 380 ERIEEAEDMtqKMQAHNEEMEAQL------SVAEEElGGYKQQAQtlERELQALRQQESLAdpsYSKEEVDSLRRKLETL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 338 TAEVENAKCQNSKLEAAVAQSEQQGEAALSdaRCKLAEL-EGALQKAKQDMACLIREYQEvmnsklgldiEIATYRRLLE 416
Cdd:pfam05557 454 ELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLsMNPAAEAYQQRKNQLEKLQA----------EIERLKRLLK 521
|
330
....*....|....
gi 169790841 417 GEEQRLcEGVEAVN 430
Cdd:pfam05557 522 KLEDDL-EQVLRLP 534
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
292-418 |
3.71e-03 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 39.32 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 292 TRSRAEAESWyrskcEEMKATVIRHGETLRRTKEE--------------INELNRMIQRltAEVENAKCQNSKLEAAVAQ 357
Cdd:pfam14992 43 TRSLAEDEER-----EELNFTIMEKEDALQELELEtaklekkneilvksVMELQRKLSR--KSDKNTGLEQETLKQMLEE 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169790841 358 SE---QQGEAALSDARCKLAELEGALQKAKQ---DMACLIREYQEVMNSklgldIEIATYRRLLEGE 418
Cdd:pfam14992 116 LKvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-396 |
3.73e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 98 LEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFAGY----IETLRREAEC 173
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---QATIDTRTSAFrdlqGQLAHAKKQQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 174 vEADSGRLASELNHVQEVLEGYK-KKYEEEVALRATAENEFvaLKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEI 252
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKEREQ--QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 253 RILQSHI-------SDTSVVVKLDNS--------RDLNMDCI-----VAEIKAQYDDIATRSRAEAESWYRSKCEEMKAT 312
Cdd:TIGR00618 511 IHPNPARqdidnpgPLTRRMQRGEQTyaqletseEDVYHQLTserkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 313 -----VIRHGETLRRTKEEINELNRmIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdarcklAELEGALQKAKQDM 387
Cdd:TIGR00618 591 nitvrLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREH 663
|
....*....
gi 169790841 388 ACLIREYQE 396
Cdd:TIGR00618 664 ALSIRVLPK 672
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-415 |
4.19e-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: 39.36 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 318 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 397
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|....*...
gi 169790841 398 MNSklgLDIEIATYRRLL 415
Cdd:COG4942 96 RAE---LEAQKEELAELL 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-443 |
5.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEevaLRATAEnEFVALKKdvdcaylRKSDLEANV---EALIQE 240
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKE---LEELKE-EIEELEK-------ELESLEGSKrklEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 241 IDFLRRLYEEEIRILQSHISDtsvVVKLDNSRDLNMdcivaEIKAQYDDIATRSRaeaeswyrsKCEEMKATVIRHGETL 320
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKE---LKELKEKAEEYI-----KLSEFYEEYLDELR---------EIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 321 RRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAqseqqgeaALSDARCKLAELEgalqKAKQDMAC-----LIREYQ 395
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHE--------LYEEAKAKKEELE----RLKKRLTGltpekLEKELE 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 169790841 396 EVMNSKLGLDIEIATYRRLLEGEEQRLCEGVEAVNVCVSSSRGGVVCG 443
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
295-383 |
6.20e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 37.28 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 295 RAEAESWyRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARcKLA 374
Cdd:pfam12718 6 KLEAENA-QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR-KIQ 83
|
....*....
gi 169790841 375 ELEGALQKA 383
Cdd:pfam12718 84 LLEEELEES 92
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
321-388 |
6.71e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.30 E-value: 6.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169790841 321 RRTKEEINELNRM----IQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMA 388
Cdd:pfam11559 51 LEFRESLNETIRTleaeIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-246 |
7.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 84 TTVSVNESLLTPLNLEIdpnAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRecCQSN----LEPL 159
Cdd:COG4913 269 ERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNggdrLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 160 fAGYIETLRREAECVEADSGRLASELNHVQEVL----EGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVE 235
Cdd:COG4913 344 -EREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|.
gi 169790841 236 ALIQEIDFLRR 246
Cdd:COG4913 423 ELEAEIASLER 433
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
164-261 |
8.64e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 36.46 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169790841 164 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDF 243
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELNELKAEIAELKAEAESAKAELEE 89
|
90
....*....|....*...
gi 169790841 244 LRRLYEEEIRILQSHISD 261
Cdd:pfam07926 90 SEESWEEQKKELEKELSE 107
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
305-377 |
9.21e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 36.02 E-value: 9.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169790841 305 KCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAkcqNSKLEAAvaqsEQQGEAALSDARCKLAELE 377
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENA---QEKLERL----REQAEEKREAAQARLEELR 116
|
|
| |
