|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
105-416 |
7.89e-137 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 396.60 E-value: 7.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 105 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKL-QFYQNRECCQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 184 QEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTSVVVKL 263
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 264 DNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQN 343
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992713279 344 SKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQR 416
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
4-102 |
8.06e-15 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 72.00 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 4 GSYCGGRAF---SCISACGPR---PGRCCITAAPYRGISCYRGLTGGFGSHS---VCGGFRAGSCGRS------------ 62
Cdd:pfam16208 32 GGGGGGGGFgsrSLYNLGGSKsisISVAGGGSRPGSGFGFGGGGGGGFGGGFgggGGGGFGGGGGFGGgfggggyggggf 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 992713279 63 ----FGYRSGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 102
Cdd:pfam16208 112 ggggFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
105-436 |
1.50e-12 |
|
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: 70.10 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 105 EEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECcQSNLEPlFEGYI-----ETLRREAECVEADSGRLASE 179
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQAL-LKEKRE-YEGYEllkekEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 180 LNHVQEVLEGYKKKYEEEVSLRATA--------ENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---RRLYEEEIR 248
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 249 VLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATvirhgETLRRTKEEINELNRM 328
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-----EKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 329 IQRLTAEVENAKCQNSKLEAAVAQSEQ---QGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMN---------SK 396
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvekelSK 487
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 992713279 397 LGLDIEIATYRRLLEGEEQRlceGVGSVNVCVSSSRGGVV 436
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVR---GGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-425 |
9.54e-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: 54.68 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 104 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN-------RECCQSNLEPLFEGYIETLRREAECVEADSGRL 176
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 177 ASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSH 253
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 254 ISDT--SVVVKLDNSRDLNMDciIAEIKAQYDDIVT---RSRAEAESWYRSKcEEMKATVIRHGETLRRTKEEINELNRM 328
Cdd:TIGR02168 833 IAATerRLEDLEEQIEELSED--IESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 329 IQRLTAEVENAKCQNSKLEAAVAQSEQQgeaalsdarckLAELEGALqkakqdMACLIREYQEVMNSKLGLDIEIATYRR 408
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVR-----------IDNLQERL------SEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340
....*....|....*....|
gi 992713279 409 ---LLEGEEQRLcegvGSVN 425
Cdd:TIGR02168 973 rlkRLENKIKEL----GPVN 988
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
161-378 |
1.12e-06 |
|
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: 51.33 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 161 TLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALiqeidflr 240
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 241 rlyEEEIRVLQSHISDtsVVVKLDNSRDL--NM-------DCIIAE---IKAQYDDivTRSRAEAESwyRSKceEMKA-T 307
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992713279 308 VIRHGETLRRTKEEINELNRMiqrLTAEVE---NAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKA 378
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
159-408 |
1.52e-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: 50.15 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 159 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVdcaylrkSDLEANVEALIQEIDF 238
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 239 LRRLYEEEIRVLQSHISDTSVVVKLdNSRDLNmdciIAEIKAQYDDIVTRSRAEaeswyrskceemkatvirHGETLRRT 318
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLL-SPEDFL----DAVRRLQYLKYLAPARRE------------------QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 319 KEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLG 398
Cdd:COG4942 159 LAELAALRAELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|
gi 992713279 399 LDIEIATYRR 408
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-417 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 190 YKKKYEE-EVSLRATAEN----EFVA--LKKDVDcaylrksDLEANVEALIQEIDflrrlYEEEIRVLQSHISDTSVVVK 262
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEKAERYKE-----LKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 263 LDNSRDLNMdcIIAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAK 340
Cdd:TIGR02168 238 REELEELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 341 CQNSKLEAAVAQSEQQGE---AALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 417
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
91-411 |
1.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 91 LNLEIDPNAQCVKQEE--KEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEgYIETLRREAEC 168
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKE-EIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 169 VEADSGRLASELNHVQEVLEGYKKKYEEevsLRATAEnEFVALKKDVDcAYLRKSDLEANVEALIQEIDFLRRLYEEEIR 248
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 249 VLQSHISDTSVvvklDNSRDLNMDCIIAEIKAQYDDIVTRSR---------AEAESWYRSKCEEMKATVIRHGETLRRTK 319
Cdd:PRK03918 325 GIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHElyeeakakkEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 320 EE----INELNRMIQRLTAEVENAKCQNSKLEAAVAQ--------SEQQGEAALSDARCKLAELEGALQKAKQDMACLIR 387
Cdd:PRK03918 401 EEieeeISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340
....*....|....*....|....
gi 992713279 388 EYQEVmNSKLGLDIEIATYRRLLE 411
Cdd:PRK03918 481 ELREL-EKVLKKESELIKLKELAE 503
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
103-393 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 103 KQEEKEQIKSLNSRfAAFIDKVRFLEQQNKLLETKLQfyQNREccqsNLEPLFEGYIETLRREAECVEADSGRLASELNH 182
Cdd:pfam07888 55 RQREKEKERYKRDR-EQWERQRRELESRVAELKEELR--QSRE----KHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 183 VQEVLE-------GYKKKYEEEVSLRATAE--NEFVALKKDVdcaYLRKSDLEANVEALIQEidfLRRLYEE-------- 245
Cdd:pfam07888 128 EARIREleediktLTQRVLERETELERMKEraKKAGAQRKEE---EAERKQLQAKLQQTEEE---LRSLSKEfqelrnsl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 246 -----EIRVLQSHISDTSVVVKLDNSRDLNMDCIIAE-----------------IKAQYDDIVT-RSRAEAEsWYRSKCE 302
Cdd:pfam07888 202 aqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAqRDRTQAE-LHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 303 ----------------EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALS 362
Cdd:pfam07888 281 aaqltlqladaslalrEGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|.
gi 992713279 363 DARCKLAELEGALQKAKQDMACLIREYQEVM 393
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
92-391 |
6.03e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 92 NLEIDPNAQcVKQEEKEQIKSLnsRFAAFIDKVRFLEQQNKLL-ETKLQFYQNRECCQSNLEPLfEGYIETLrrEAECVE 170
Cdd:PLN02939 108 IAAIDNEQQ-TNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLnQARLQALEDLEKILTEKEAL-QGKINIL--EMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 171 ADSG-RLASELNHVQEVLEGYKKKYEEEVSLRATAENEFV-ALKKDVDCAYLRKSDLEANVEALIQEIdflrrlyeeeir 248
Cdd:PLN02939 182 TDARiKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDVLKEENMLLKDDIQFLKAEL------------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 249 vlqSHISDT-SVVVKLDNSRDLnMDCIIAEIKAQY----DDIVTRSRAEAESWYrskceemkatvirhgetlrrtkEEIN 323
Cdd:PLN02939 250 ---IEVAETeERVFKLEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWW----------------------EKVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 324 ELNRMIQRLTAEVENAKC---QNSKLEAAVAQSEQQ-GEAALSDARC--------KLAELEGALQKAKQDMACLIREYQE 391
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASlKEANVSKFSSykvellqqKLKLLEERLQASDHEIHSYIQLYQE 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
105-417 |
9.26e-05 |
|
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: 45.01 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 105 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLET-------------KLQFYQNRECC--QSNLEPLFEGYiETLRREAECV 169
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVelnklekqkkenkKNIDKFLTEIKkkEKELEKLNNKY-NDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 170 EADSGRLASELNHVQE-----------------VLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEAL 232
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKnidkiknkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 233 IQEIDFLRRLYEEEIRVLQSHISDtsvvVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHG 312
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 313 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEgALQKAKQDMACLIREYQEV 392
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
330 340
....*....|....*....|....*...
gi 992713279 393 MNSKlglDIEIATY---RRLLEGEEQRL 417
Cdd:TIGR04523 407 NQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
127-396 |
1.24e-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: 44.71 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 127 LEQQNKLLETKLQFYQNRECCQSNLEPLFeGYIETLRREAECVEadsgRLASELNHVQEVLEGYKKKYEEEV-------S 199
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIhdleiqlT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 200 LRATAENEFVA----LKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTsVVVKLDNSRDLNMDCII 275
Cdd:pfam05483 461 AIKTSEEHYLKevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI-INCKKQEERMLKQIENL 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 276 AEIKAQYDDIVTRSRAEaeswYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQ 355
Cdd:pfam05483 540 EEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 992713279 356 QGEA----------ALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSK 396
Cdd:pfam05483 616 ENKAlkkkgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-391 |
1.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 198 VSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSHISDTSvvvklDNSRDLNmdci 274
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQ-----AEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 275 iAEIKAQYDDIVTRSRAEAESWYRSKCEEM------KATVIRHGETLRR----TKEEINELNRMIQRLT---AEVENAKC 341
Cdd:COG3883 79 -AEIEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKiadaDADLLEELKADKAELEakkAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992713279 342 QNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQE 391
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-379 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 104 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFyqnreccQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 183
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 184 QEVLEGYKKK-------YEEEVSLRATAENEFVALKKDVDCAylrKSDLEANVEAL---IQEIDFL---RRLYEEEIRVL 250
Cdd:TIGR04523 439 NSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELkskEKELKKLneeKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 251 QSHISDTsvvvkLDNSRDLNMDciIAEIKAQYDDIvtrsraeaeswyRSKCEEMKatvirhgETLRRT--KEEINELNRM 328
Cdd:TIGR04523 516 TKKISSL-----KEKIEKLESE--KKEKESKISDL------------EDELNKDD-------FELKKEnlEKEIDEKNKE 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 992713279 329 IQRLTAEVENAKCQNSKLEAAVAQSEQQ-----GEAALSDArcKLAELEGALQKAK 379
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEkkdliKEIEEKEK--KISSLEKELEKAK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
156-372 |
1.72e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 156 EGYIETLrreaecVEADSGRLASELNHVQEVLEGYKKKYEE-EVSLRA-TAENEFVALKKDVDCAYLRKSDLEANVEALI 233
Cdd:COG3206 159 EAYLEQN------LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 234 QEIDFLRRLYEEeirvLQSHISDTSvvvklDNSRDLNMDCIIAEIKAQYDDIVTRsRAEAESWYRSKCEEMKATVirhgE 313
Cdd:COG3206 233 AELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----A 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 314 TLRRTKEEIN-ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGeAALSDARCKLAELE 372
Cdd:COG3206 299 QIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-425 |
3.87e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 160 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL 239
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 240 RRL-----------------YEEEIRVLQSHISDTSVVVKLDNSRDLNMdcIIAEIKAQYDDI----------------- 285
Cdd:TIGR02169 757 KSElkelearieeleedlhkLEEALNDLEARLSHSRIPEIQAELSKLEE--EVSRIEARLREIeqklnrltlekeyleke 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 286 ---VTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQR---LTAEVENAKCQNSKLEaavaQSEQQGEA 359
Cdd:TIGR02169 835 iqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELE----RKIEELEA 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992713279 360 ALSDARCKLAELEGALQKAKQDMACL---IREYQEVMNSKLGLDIEIATYRRLlegeEQRLcEGVGSVN 425
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIedpKGEDEEIPEEELSLEDVQAELQRV----EEEI-RALEPVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-375 |
4.40e-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: 43.12 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 103 KQEEKEQIKSLNSRFAAFIDKV-----RFLEQQNKL--LETKLQFYQNR-ECCQSNLEPLfEGYIETLRREAECVEADSG 174
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIeelqkELYALANEIsrLEQQKQILRERlANLERQLEEL-EAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 175 RLASELNHVQEVLEGYKKKYEEEVSLRATAEN-------EFVALKKDVDCAYL--------------RKSDLEANVEALI 233
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESrleeleeQLETLRSKVAQLELqiaslnneierleaRLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 234 QEIDFLRRLYEEeirvlqshisdtsvvvkldnsrdlnmdciiAEIKAQYDDIVTRSRAEaeswyrskcEEMKATVIRHGE 313
Cdd:TIGR02168 421 QEIEELLKKLEE------------------------------AELKELQAELEELEEEL---------EELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992713279 314 TLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAV--AQSEQQGEAALSDARCKLAELEGAL 375
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
274-391 |
5.08e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 274 IIAEIKAQYDDIvtrsRAEAESWYRSKCEEMKAT---VIRHGETLRRTKEEI----NELNRMIQRLTAEVENAKCQNSKL 346
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKLekrLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 992713279 347 EAAVAQSEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLIREYQE 391
Cdd:PRK12704 134 EELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
112-365 |
7.19e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 112 SLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccqsnleplfegyIETLRREAECVEadsgrLASELNHVQEVLEGYK 191
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFRQKNGLVD-----LSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 192 KKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEAN--VEALIQEIDFLRRLYEEEIRVLQShisDTSVVVKLDNSrdl 269
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP---NHPDVIALRAQ--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 270 nmdciIAEIKAQYDDIVTRSRAEAESWYrskcEEMKATVIRHGETLRRTKEEINELNRM---IQRLTAEVENAKCQNSKL 346
Cdd:COG3206 300 -----IAALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESL 370
|
250
....*....|....*....
gi 992713279 347 EAAVAQSEQQGEAALSDAR 365
Cdd:COG3206 371 LQRLEEARLAEALTVGNVR 389
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
275-417 |
1.19e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 275 IAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQ 352
Cdd:COG1196 248 LEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992713279 353 SEQQGEAALSdarcKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 417
Cdd:COG1196 328 LEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
159-381 |
1.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 159 IETLRREAECVEADSGRLASELNHVQEVlegykKKYEEEVSLRATAENEFVALKKDVdcaylRKSDLEANVEAlIQEIDF 238
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARKAEAARKAEEERKAEEA-----RKAEDAKKAEA-VKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 239 LRRLYEEEIRVlqSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAEswyRSKCEEM-KATVIRHGETLRR 317
Cdd:PTZ00121 1235 AKKDAEEAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992713279 318 TKEEinelNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQD 381
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
302-417 |
1.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 302 EEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQgeaalsdarckLAELEGALQKAKQD 381
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDER-----------IERLERELSEARSE 456
|
90 100 110
....*....|....*....|....*....|....*.
gi 992713279 382 MACLIREYQEVMNsklgLDIEIATYRRLLEGEEQRL 417
Cdd:COG2433 457 ERREIRKDREISR----LDREIERLERELEEERERI 488
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
92-408 |
1.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 92 NLEIDPNAQCVKQEEK------EQIKSLNSRFAAFIDKVRFLEQQ----NKLLETKLQFYQNRECCQSNLEPLFEGYIET 161
Cdd:PRK01156 196 NLELENIKKQIADDEKshsitlKEIERLSIEYNNAMDDYNNLKSAlnelSSLEDMKNRYESEIKTAESDLSMELEKNNYY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 162 LRREAECVEADSGRLASELNHV-------------QEVLEGYK---KKYEEEVSLRATAE---NEFVALKKDVDCAYLRK 222
Cdd:PRK01156 276 KELEERHMKIINDPVYKNRNYIndyfkykndienkKQILSNIDaeiNKYHAIIKKLSVLQkdyNDYIKKKSRYDDLNNQI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 223 SDL---EANVEALIQEIDFL---RRLYEEEIRVLQSHISDTSVVVKLDNSRdlnMDCIIAEIKAQYDDIVTR-------- 288
Cdd:PRK01156 356 LELegyEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKLQDISSKvsslnqri 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 289 ----------SRAEAESWYRSKC--------EEMKATVIRH-GETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAA 349
Cdd:PRK01156 433 ralrenldelSRNMEMLNGQSVCpvcgttlgEEKSNHIINHyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 992713279 350 VAQSEQQGEAALSDARCKLAELEGALQKAKQDMAclirEYQEVMNSKLGLDIEIATYRR 408
Cdd:PRK01156 513 EINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLDSKR 567
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
313-397 |
1.73e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 313 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 392
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 992713279 393 MNSKL 397
Cdd:COG4372 177 SEAEA 181
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-417 |
1.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 225 LEANVEALIQEIDFLRRLyEEEIRVLQSHISdtsvvvKLDNSRDLnmdciIAEIKAQYDDIVTRSRAEAEswYRSKCEEM 304
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELE------ELREELEK-----LEKLLQLLPLYQELEALEAE--LAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 305 katvirhgETLRRTKEEINELNRMIQRLTAEVENAKcqnSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMAC 384
Cdd:COG4717 149 --------EELEERLEELRELEEELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|...
gi 992713279 385 LIREYQEVMNsklglDIEIATYRRLLEGEEQRL 417
Cdd:COG4717 218 AQEELEELEE-----ELEQLENELEAAALEERL 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-417 |
2.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 169 VEADSGRLA--SELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRR---LY 243
Cdd:TIGR02168 666 AKTNSSILErrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 244 EEEIRVLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQyddivtrsRAEAESWYRSKCEEMKATvirhGETLRRTKEEIN 323
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------IEELEAQIEQLKEELKAL----REALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 324 ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEI 403
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250
....*....|....
gi 992713279 404 ATYRRLLEGEEQRL 417
Cdd:TIGR02168 890 ALLRSELEELSEEL 903
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
315-417 |
2.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 315 LRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQ---GEAALSDARCKLAELEGALQKAKQDMACLIREYQE 391
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 992713279 392 VMNSKLGLDIEIATYRRLLEGEEQRL 417
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
226-413 |
2.10e-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: 40.09 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 226 EANVEAL--IQEidflrrlYEEEIRVLQSHISDTSVVVKLDNSRDLNmdCIIAEikaqyddivtRSRAEAEswyrskCEE 303
Cdd:pfam14992 17 EANQVLLlkIQE-------KEEEIQSLEREITLTRSLAEDEEREELN--FTIME----------KEDALQE------LEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 304 MKATVIRHGETLRRtkeEINELNRMIQRltAEVENAKCQNSKLEAAVAQSE---QQGEAALSDARCKLAELEGALQKAKQ 380
Cdd:pfam14992 72 ETAKLEKKNEILVK---SVMELQRKLSR--KSDKNTGLEQETLKQMLEELKvklQQSEESCADQEKELAKVESDYQSVHQ 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 992713279 381 ---DMACLIREYQEVMNSklgldIEIATYRRLLEGE 413
Cdd:pfam14992 147 lceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-425 |
2.69e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 105 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN--RECCQSNLEPlfegyiETLRREAECVeadsgrLASELNH 182
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSP------EDLSRRIEQL------QQREIVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 183 VQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSD------LEANVEALIQEIDFLRRLYEEEIRVLQSHISD 256
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHkalvrrLQRRVLLLTKERDGYRAILESYDKELTMSNYS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 257 TSVVVKLDNSRDL--NMDCIIAEIKAQYddivtrSRAEAE-SWYRSKCE--EMKATVIRHGETLR---RTKEEINELNRM 328
Cdd:pfam05557 376 PQLLERIEEAEDMtqKMQAHNEEMEAQL------SVAEEElGGYKQQAQtlERELQALRQQESLAdpsYSKEEVDSLRRK 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 329 IQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdaRCKLAEL-EGALQKAKQDMACLIREYQEvmnsklgldiEIATYR 407
Cdd:pfam05557 450 LETLELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLsMNPAAEAYQQRKNQLEKLQA----------EIERLK 517
|
330
....*....|....*...
gi 992713279 408 RLLEGEEQRLcEGVGSVN 425
Cdd:pfam05557 518 RLLKKLEDDL-EQVLRLP 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
93-391 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 93 LEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEGY----IETLRREAEC 168
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---QATIDTRTSAFrdlqGQLAHAKKQQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 169 vEADSGRLASELNHVQEVLEGYKKKYEEEVSL-RATAENEFvaLKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEI 247
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTAQCEKLEKIHLQESaQSLKEREQ--QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 248 RVLQSHIS-------DTSVVVKLDNS--------RDLNMDCI-----IAEIKAQYDDIVTRSRAEAESWYRSKCEEMKAT 307
Cdd:TIGR00618 511 IHPNPARQdidnpgpLTRRMQRGEQTyaqletseEDVYHQLTserkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 308 -----VIRHGETLRRTKEEINELNRmIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdarcklAELEGALQKAKQDM 382
Cdd:TIGR00618 591 nitvrLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREH 663
|
....*....
gi 992713279 383 ACLIREYQE 391
Cdd:TIGR00618 664 ALSIRVLPK 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-417 |
3.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 104 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQF---YQNRECCQSNLEPLFEGYIETLRREAECVEA--DSGRLAS 178
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplYQELEALEAELAELPERLEELEERLEELRELeeELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 179 ELNHVQEVLEgykkkyEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYE------------EE 246
Cdd:COG4717 171 ELAELQEELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqleneleaaaleER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 247 IRVLQSHISDTSVVVKLDNSRDLNMDCII---------------------------AEIKAQYDDIVTRSRAEAESW--- 296
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELeel 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 297 ---YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKcQNSKLEAAVAQSEQQGEAALSDARcKLAELEG 373
Cdd:COG4717 325 laaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAE-EYQELKE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 992713279 374 ALQKAKQDMACLIREYQEVM--NSKLGLDIEIATYRRLLEGEEQRL 417
Cdd:COG4717 403 ELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEEL 448
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
103-381 |
4.18e-03 |
|
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: 39.56 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 103 KQEEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECCQSNleplfegyIETLRREAECV--EADSGRLASEL 180
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKR--ETETGIQNLTAEIEQGQESLTEN--------LEAIKEEIENIvgEVELSKSSEEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 181 NHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDvdcaylRKSDLEANVEALIQEIDFLRRLYEEEIRVLqshisdtsvv 260
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLL---------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 261 VKLDNSRDLNMDCIIAEIKAQYDDivtrsraeaeswyrskceemkatviRHGETLRRTKEEINELNRMIQRLTAEVENAK 340
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEE-------------------------AYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 992713279 341 CQNSKLEAAvaqseqqGEAALSDARCKLAELEGALQKAKQD 381
Cdd:COG5185 499 ATLEKLRAK-------LERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-257 |
4.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 105 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQ---FYQNRECCQ--SNLEPLFEGYIE----------------TLR 163
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEelgFESVEELEErlKELEPFYNEYLElkdaekelereekelkKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 164 REAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRatAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---- 239
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLkeel 703
|
170 180
....*....|....*....|
gi 992713279 240 --RRLYEEEIRVLQSHISDT 257
Cdd:PRK03918 704 eeREKAKKELEKLEKALERV 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-410 |
5.39e-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: 38.98 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 313 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 392
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|....*...
gi 992713279 393 MNSklgLDIEIATYRRLL 410
Cdd:COG4942 96 RAE---LEAQKEELAELL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-241 |
8.21e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 79 TTVSVNESLLTPLNLEIdpnAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRecCQSN----LEPL 154
Cdd:COG4913 269 ERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNggdrLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 155 fEGYIETLRREAECVEADSGRLASELNHVQEVL----EGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVE 230
Cdd:COG4913 344 -EREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|.
gi 992713279 231 ALIQEIDFLRR 241
Cdd:COG4913 423 ELEAEIASLER 433
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
316-383 |
8.52e-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: 36.91 E-value: 8.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992713279 316 RRTKEEINELNRM----IQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMA 383
Cdd:pfam11559 51 LEFRESLNETIRTleaeIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
290-378 |
8.75e-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: 36.90 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 290 RAEAESWyRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARcKLA 369
Cdd:pfam12718 6 KLEAENA-QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR-KIQ 83
|
....*....
gi 992713279 370 ELEGALQKA 378
Cdd:pfam12718 84 LLEEELEES 92
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
155-395 |
9.92e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 38.28 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 155 FEGYIETLRREAECVEADSGRLasELNHVQEVLEGYKKK----Y---EEEVslraTAENeFVALKKDVDCAYLRKsdLEA 227
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREV----KARK-YVEKNSDTLPDFLEH--AKE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 228 NVEALIQEIDFLRRLYeeeirvlqsHISDTsvvvKLDNSRDLNMDciIAEIKAQYDDIVTRS----------RAEAESWY 297
Cdd:PRK04778 325 QNKELKEEIDRVKQSY---------TLNES----ELESVRQLEKQ--LESLEKQYDEITERIaeqeiayselQEELEEIL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992713279 298 RsKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAK--CQNSKL---------EAAVAQSE-QQGEAALSDAR 365
Cdd:PRK04778 390 K-QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKryLEKSNLpglpedyleMFFEVSDEiEALAEELEEKP 468
|
250 260 270
....*....|....*....|....*....|
gi 992713279 366 CKLAELEGALQKAKQDMACLIREYQEVMNS 395
Cdd:PRK04778 469 INMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| |
