|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
102-413 |
2.21e-136 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 395.44 E-value: 2.21e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 102 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKL-QFYQNRECCQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 180
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 181 QEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTSVVVKL 260
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 261 DNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQN 340
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1903220 341 SKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQR 413
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
1-99 |
9.60e-15 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 71.61 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 1 GSYCGGRAF---SCISACGPR---PGRCCITAAPYRGISCYRGLTGGFGSHS---VCGGFRAGSC--------------- 56
Cdd:pfam16208 32 GGGGGGGGFgsrSLYNLGGSKsisISVAGGGSRPGSGFGFGGGGGGGFGGGFgggGGGGFGGGGGfgggfggggyggggf 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1903220 57 -GRDFGYRSGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 99
Cdd:pfam16208 112 gGGGFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
102-433 |
2.57e-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: 69.33 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 102 EEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECcQSNLEPlFEGYI-----ETLRREAECVEADSGRLASE 176
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQAL-LKEKRE-YEGYEllkekEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 177 LNHVQEVLEGYKKKYEEEVSLRATA--------ENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---RRLYEEEIR 245
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 246 VLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATvirhgETLRRTKEEINELNRM 325
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-----EKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 326 IQRLTAEVENAKCQNSKLEAAVAQSEQ---QGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMN---------SK 393
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvekelSK 487
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1903220 394 LGLDIEIATYRRLLEGEEQRlceGVGSVNVCVSSSRGGVV 433
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVR---GGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-353 |
1.29e-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: 54.29 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 101 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN-------RECCQSNLEPLFEGYIETLRREAECVEADSGRL 173
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 174 ASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSH 250
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 251 ISDT--SVVVKLDNSRDLNMDciIAEIKAQYDDIVT---RSRAEAESWYRSKcEEMKATVIRHGETLRRTKEEINELNRM 325
Cdd:TIGR02168 833 IAATerRLEDLEEQIEELSED--IESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELESK 909
|
250 260
....*....|....*....|....*...
gi 1903220 326 IQRLTAEVENAKCQNSKLEAAVAQSEQQ 353
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 ... |
158-375 |
1.47e-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: 50.94 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 158 TLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALiqeidflr 237
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 238 rlyEEEIRVLQSHISDtsVVVKLDNSRDL--NM-------DCIIAE---IKAQYDDivTRSRAEAESwyRSKceEMKA-T 304
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1903220 305 VIRHGETLRRTKEEINELNRMiqrLTAEVE---NAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKA 375
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-405 |
2.01e-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: 49.76 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 156 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVdcaylrkSDLEANVEALIQEIDF 235
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 236 LRRLYEEEIRVLQSHISDTSVVVKLdNSRDLNmdciIAEIKAQYDDIVTRSRAEaeswyrskceemkatvirHGETLRRT 315
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLL-SPEDFL----DAVRRLQYLKYLAPARRE------------------QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 316 KEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLG 395
Cdd:COG4942 159 LAELAALRAELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|
gi 1903220 396 LDIEIATYRR 405
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-414 |
1.85e-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: 47.36 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 187 YKKKYEE-EVSLRATAEN----EFVA--LKKDVDcaylrksDLEANVEALIQEIDflrrlYEEEIRVLQSHISDTSVVVK 259
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEKAERYKE-----LKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 260 LDNSRDLNMdcIIAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAK 337
Cdd:TIGR02168 238 REELEELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 338 CQNSKLEAAVAQSEQQGE---AALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 414
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-408 |
2.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 88 LNLEIDPNAQCVKQEE--KEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEgYIETLRREAEC 165
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKE-EIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 166 VEADSGRLASELNHVQEVLEGYKKKYEEevsLRATAEnEFVALKKDVDcAYLRKSDLEANVEALIQEIDFLRRLYEEEIR 245
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 246 VLQSHISDTSVvvklDNSRDLNMDCIIAEIKAQYDDIVTRSR---------AEAESWYRSKCEEMKATVIRHGETLRRTK 316
Cdd:PRK03918 325 GIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHElyeeakakkEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 317 EE----INELNRMIQRLTAEVENAKCQNSKLEAAVAQ--------SEQQGEAALSDARCKLAELEGALQKAKQDMACLIR 384
Cdd:PRK03918 401 EEieeeISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340
....*....|....*....|....
gi 1903220 385 EYQEVmNSKLGLDIEIATYRRLLE 408
Cdd:PRK03918 481 ELREL-EKVLKKESELIKLKELAE 503
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
100-390 |
2.44e-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: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 100 KQEEKEQIKSLNSRfAAFIDKVRFLEQQNKLLETKLQfyQNREccqsNLEPLFEGYIETLRREAECVEADSGRLASELNH 179
Cdd:pfam07888 55 RQREKEKERYKRDR-EQWERQRRELESRVAELKEELR--QSRE----KHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 180 VQEVLE-------GYKKKYEEEVSLRATAE--NEFVALKKDVdcaYLRKSDLEANVEALIQEidfLRRLYEE-------- 242
Cdd:pfam07888 128 EARIREleediktLTQRVLERETELERMKEraKKAGAQRKEE---EAERKQLQAKLQQTEEE---LRSLSKEfqelrnsl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 243 -----EIRVLQSHISDTSVVVKLDNSRDLNMDCIIAE-----------------IKAQYDDIVT-RSRAEAEsWYRSKCE 299
Cdd:pfam07888 202 aqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAqRDRTQAE-LHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 300 ----------------EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALS 359
Cdd:pfam07888 281 aaqltlqladaslalrEGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|.
gi 1903220 360 DARCKLAELEGALQKAKQDMACLIREYQEVM 390
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
89-388 |
7.46e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 89 NLEIDPNAQcVKQEEKEQIKSLnsRFAAFIDKVRFLEQQNKLL-ETKLQFYQNRECCQSNLEPLfEGYIETLrrEAECVE 167
Cdd:PLN02939 108 IAAIDNEQQ-TNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLnQARLQALEDLEKILTEKEAL-QGKINIL--EMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 168 ADSG-RLASELNHVQEVLEGYKKKYEEEVSLRATAENEFV-ALKKDVDCAYLRKSDLEANVEALIQEIdflrrlyeeeir 245
Cdd:PLN02939 182 TDARiKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDVLKEENMLLKDDIQFLKAEL------------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 246 vlqSHISDT-SVVVKLDNSRDLnMDCIIAEIKAQY----DDIVTRSRAEAESWYrskceemkatvirhgetlrrtkEEIN 320
Cdd:PLN02939 250 ---IEVAETeERVFKLEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWW----------------------EKVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 321 ELNRMIQRLTAEVENAKC---QNSKLEAAVAQSEQQ-GEAALSDARC--------KLAELEGALQKAKQDMACLIREYQE 388
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASlKEANVSKFSSykvellqqKLKLLEERLQASDHEIHSYIQLYQE 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-414 |
1.39e-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: 44.63 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 102 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLET-------------KLQFYQNRECC--QSNLEPLFEGYiETLRREAECV 166
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVelnklekqkkenkKNIDKFLTEIKkkEKELEKLNNKY-NDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 167 EADSGRLASELNHVQE-----------------VLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEAL 229
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKnidkiknkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 230 IQEIDFLRRLYEEEIRVLQSHISDtsvvVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHG 309
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 310 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEgALQKAKQDMACLIREYQEV 389
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
330 340
....*....|....*....|....*...
gi 1903220 390 MNSKlglDIEIATY---RRLLEGEEQRL 414
Cdd:TIGR04523 407 NQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-393 |
1.41e-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: 44.33 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 124 LEQQNKLLETKLQFYQNRECCQSNLEPLFeGYIETLRREAECVEadsgRLASELNHVQEVLEGYKKKYEEEV-------S 196
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIhdleiqlT 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 197 LRATAENEFVA----LKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTsVVVKLDNSRDLNMDCII 272
Cdd:pfam05483 461 AIKTSEEHYLKevedLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI-INCKKQEERMLKQIENL 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 273 AEIKAQYDDIVTRSRAEaeswYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQ 352
Cdd:pfam05483 540 EEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1903220 353 QGEA----------ALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSK 393
Cdd:pfam05483 616 ENKAlkkkgsaenkQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
195-388 |
2.32e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 195 VSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSHISDTSvvvklDNSRDLNmdci 271
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQ-----AEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 272 iAEIKAQYDDIVTRSRAEAESWYRSKCEEM------KATVIRHGETLRR----TKEEINELNRMIQRLT---AEVENAKC 338
Cdd:COG3883 79 -AEIEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKiadaDADLLEELKADKAELEakkAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1903220 339 QNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQE 388
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-376 |
2.39e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 101 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFyqnreccQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 180
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 181 QEVLEGYKKK-------YEEEVSLRATAENEFVALKKDVDCAylrKSDLEANVEAL---IQEIDFL---RRLYEEEIRVL 247
Cdd:TIGR04523 439 NSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELkskEKELKKLneeKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 248 QSHISDTsvvvkLDNSRDLNMDciIAEIKAQYDDIvtrsraeaeswyRSKCEEMKatvirhgETLRRT--KEEINELNRM 325
Cdd:TIGR04523 516 TKKISSL-----KEKIEKLESE--KKEKESKISDL------------EDELNKDD-------FELKKEnlEKEIDEKNKE 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1903220 326 IQRLTAEVENAKCQNSKLEAAVAQSEQQ-----GEAALSDArcKLAELEGALQKAK 376
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEkkdliKEIEEKEK--KISSLEKELEKAK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
153-369 |
2.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 153 EGYIETLrreaecVEADSGRLASELNHVQEVLEGYKKKYEE-EVSLRA-TAENEFVALKKDVDCAYLRKSDLEANVEALI 230
Cdd:COG3206 159 EAYLEQN------LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 231 QEIDFLRRLYEEeirvLQSHISDTSvvvklDNSRDLNMDCIIAEIKAQYDDIVTRsRAEAESWYRSKCEEMKATVirhgE 310
Cdd:COG3206 233 AELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----A 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 311 TLRRTKEEIN-ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGeAALSDARCKLAELE 369
Cdd:COG3206 299 QIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-422 |
5.40e-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: 42.75 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 157 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL 236
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 237 RRL-----------------YEEEIRVLQSHISDTSVVVKLDNSRDLNMdcIIAEIKAQYDDI----------------- 282
Cdd:TIGR02169 757 KSElkelearieeleedlhkLEEALNDLEARLSHSRIPEIQAELSKLEE--EVSRIEARLREIeqklnrltlekeyleke 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 283 ---VTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQR---LTAEVENAKCQNSKLEaavaQSEQQGEA 356
Cdd:TIGR02169 835 iqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELE----RKIEELEA 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1903220 357 ALSDARCKLAELEGALQKAKQDMACL---IREYQEVMNSKLGLDIEIATYRRLlegeEQRLcEGVGSVN 422
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIedpKGEDEEIPEEELSLEDVQAELQRV----EEEI-RALEPVN 974
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
271-388 |
5.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 271 IIAEIKAQYDDIvtrsRAEAESWYRSKCEEMKAT---VIRHGETLRRTKEEI----NELNRMIQRLTAEVENAKCQNSKL 343
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKLekrLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1903220 344 EAAVAQSEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLIREYQE 388
Cdd:PRK12704 134 EELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
100-372 |
6.04e-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: 42.74 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 100 KQEEKEQIKSLNSRFAAFIDKV-----RFLEQQNKL--LETKLQFYQNR-ECCQSNLEPLfEGYIETLRREAECVEADSG 171
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIeelqkELYALANEIsrLEQQKQILRERlANLERQLEEL-EAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 172 RLASELNHVQEVLEGYKKKYEEEVSLRATAEN-------EFVALKKDVDCAYL--------------RKSDLEANVEALI 230
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESrleeleeQLETLRSKVAQLELqiaslnneierleaRLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 231 QEIDFLRRLYEEeirvlqshisdtsvvvkldnsrdlnmdciiAEIKAQYDDIVTRSRAEaeswyrskcEEMKATVIRHGE 310
Cdd:TIGR02168 421 QEIEELLKKLEE------------------------------AELKELQAELEELEEEL---------EELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1903220 311 TLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAV--AQSEQQGEAALSDARCKLAELEGAL 372
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
109-362 |
9.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 109 SLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccqsnleplfegyIETLRREAECVEadsgrLASELNHVQEVLEGYK 188
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFRQKNGLVD-----LSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 189 KKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEAN--VEALIQEIDFLRRLYEEEIRVLQShisDTSVVVKLDNSrdl 266
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP---NHPDVIALRAQ--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 267 nmdciIAEIKAQYDDIVTRSRAEAESWYrskcEEMKATVIRHGETLRRTKEEINELNRM---IQRLTAEVENAKCQNSKL 343
Cdd:COG3206 300 -----IAALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESL 370
|
250
....*....|....*....
gi 1903220 344 EAAVAQSEQQGEAALSDAR 362
Cdd:COG3206 371 LQRLEEARLAEALTVGNVR 389
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
272-414 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 272 IAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQ 349
Cdd:COG1196 248 LEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1903220 350 SEQQGEAALSdarcKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 414
Cdd:COG1196 328 LEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-378 |
1.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 156 IETLRREAECVEADSGRLASELNHVQEVlegykKKYEEEVSLRATAENEFVALKKDVdcaylRKSDLEANVEAlIQEIDF 235
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARKAEAARKAEEERKAEEA-----RKAEDAKKAEA-VKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 236 LRRLYEEEIRVlqSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAEswyRSKCEEM-KATVIRHGETLRR 314
Cdd:PTZ00121 1235 AKKDAEEAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1903220 315 TKEEinelNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQD 378
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
299-414 |
1.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 299 EEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQgeaalsdarckLAELEGALQKAKQD 378
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDER-----------IERLERELSEARSE 456
|
90 100 110
....*....|....*....|....*....|....*.
gi 1903220 379 MACLIREYQEVMNsklgLDIEIATYRRLLEGEEQRL 414
Cdd:COG2433 457 ERREIRKDREISR----LDREIERLERELEEERERI 488
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
223-410 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 223 EANVEAL--IQEidflrrlYEEEIRVLQSHISDTSVVVKLDNSRDLNmdCIIAEikaqyddivtRSRAEAEswyrskCEE 300
Cdd:pfam14992 17 EANQVLLlkIQE-------KEEEIQSLEREITLTRSLAEDEEREELN--FTIME----------KEDALQE------LEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 301 MKATVIRHGETLRRtkeEINELNRMIQRltAEVENAKCQNSKLEAAVAQSE---QQGEAALSDARCKLAELEGALQKAKQ 377
Cdd:pfam14992 72 ETAKLEKKNEILVK---SVMELQRKLSR--KSDKNTGLEQETLKQMLEELKvklQQSEESCADQEKELAKVESDYQSVHQ 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1903220 378 ---DMACLIREYQEVMNSklgldIEIATYRRLLEGE 410
Cdd:pfam14992 147 lceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-405 |
2.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 89 NLEIDPNAQCVKQEEK------EQIKSLNSRFAAFIDKVRFLEQQ----NKLLETKLQFYQNRECCQSNLEPLFEGYIET 158
Cdd:PRK01156 196 NLELENIKKQIADDEKshsitlKEIERLSIEYNNAMDDYNNLKSAlnelSSLEDMKNRYESEIKTAESDLSMELEKNNYY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 159 LRREAECVEADSGRLASELNHV-------------QEVLEGYK---KKYEEEVSLRATAE---NEFVALKKDVDCAYLRK 219
Cdd:PRK01156 276 KELEERHMKIINDPVYKNRNYIndyfkykndienkKQILSNIDaeiNKYHAIIKKLSVLQkdyNDYIKKKSRYDDLNNQI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 220 SDL---EANVEALIQEIDFL---RRLYEEEIRVLQSHISDTSVVVKLDNSRdlnMDCIIAEIKAQYDDIVTR-------- 285
Cdd:PRK01156 356 LELegyEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKLQDISSKvsslnqri 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 286 ----------SRAEAESWYRSKC--------EEMKATVIRH-GETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAA 346
Cdd:PRK01156 433 ralrenldelSRNMEMLNGQSVCpvcgttlgEEKSNHIINHyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1903220 347 VAQSEQQGEAALSDARCKLAELEGALQKAKQDMAclirEYQEVMNSKLGLDIEIATYRR 405
Cdd:PRK01156 513 EINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLDSKR 567
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
310-394 |
2.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 310 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 389
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 1903220 390 MNSKL 394
Cdd:COG4372 177 SEAEA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-414 |
2.51e-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: 40.43 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 166 VEADSGRLA--SELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRR---LY 240
Cdd:TIGR02168 666 AKTNSSILErrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 241 EEEIRVLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQyddivtrsRAEAESWYRSKCEEMKATvirhGETLRRTKEEIN 320
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------IEELEAQIEQLKEELKAL----REALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 321 ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEI 400
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250
....*....|....
gi 1903220 401 ATYRRLLEGEEQRL 414
Cdd:TIGR02168 890 ALLRSELEELSEEL 903
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
312-414 |
2.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 312 LRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQ---GEAALSDARCKLAELEGALQKAKQDMACLIREYQE 388
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 1903220 389 VMNSKLGLDIEIATYRRLLEGEEQRL 414
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-414 |
2.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 222 LEANVEALIQEIDFLRRLyEEEIRVLQSHISdtsvvvKLDNSRDLnmdciIAEIKAQYDDIVTRSRAEAEswYRSKCEEM 301
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELE------ELREELEK-----LEKLLQLLPLYQELEALEAE--LAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 302 katvirhgETLRRTKEEINELNRMIQRLTAEVENAKcqnSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMAC 381
Cdd:COG4717 149 --------EELEERLEELRELEEELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|...
gi 1903220 382 LIREYQEVMNsklglDIEIATYRRLLEGEEQRL 414
Cdd:COG4717 218 AQEELEELEE-----ELEQLENELEAAALEERL 245
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
102-422 |
3.06e-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: 40.11 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 102 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN--RECCQSNLEPlfegyiETLRREAECVeadsgrLASELNH 179
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSP------EDLSRRIEQL------QQREIVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 180 VQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSD------LEANVEALIQEIDFLRRLYEEEIRVLQSHISD 253
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHkalvrrLQRRVLLLTKERDGYRAILESYDKELTMSNYS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 254 TSVVVKLDNSRDL--NMDCIIAEIKAQYddivtrSRAEAE-SWYRSKCE--EMKATVIRHGETLR---RTKEEINELNRM 325
Cdd:pfam05557 376 PQLLERIEEAEDMtqKMQAHNEEMEAQL------SVAEEElGGYKQQAQtlERELQALRQQESLAdpsYSKEEVDSLRRK 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 326 IQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdaRCKLAEL-EGALQKAKQDMACLIREYQEvmnsklgldiEIATYR 404
Cdd:pfam05557 450 LETLELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLsMNPAAEAYQQRKNQLEKLQA----------EIERLK 517
|
330
....*....|....*...
gi 1903220 405 RLLEGEEQRLcEGVGSVN 422
Cdd:pfam05557 518 RLLKKLEDDL-EQVLRLP 534
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-388 |
3.63e-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: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 90 LEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEGY----IETLRREAEC 165
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---QATIDTRTSAFrdlqGQLAHAKKQQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 166 vEADSGRLASELNHVQEVLEGYKKKYEEEVSL-RATAENEFvaLKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEI 244
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTAQCEKLEKIHLQESaQSLKEREQ--QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 245 RVLQSHI-------SDTSVVVKLDNS--------RDLNMDCI-----IAEIKAQYDDIVTRSRAEAESWYRSKCEEMKAT 304
Cdd:TIGR00618 511 IHPNPARqdidnpgPLTRRMQRGEQTyaqletseEDVYHQLTserkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 305 -----VIRHGETLRRTKEEINELNRmIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdarcklAELEGALQKAKQDM 379
Cdd:TIGR00618 591 nitvrLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREH 663
|
....*....
gi 1903220 380 ACLIREYQE 388
Cdd:TIGR00618 664 ALSIRVLPK 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
101-414 |
5.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 101 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQF---YQNRECCQSNLEPLFEGYIETLRREAECVEA--DSGRLAS 175
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplYQELEALEAELAELPERLEELEERLEELRELeeELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 176 ELNHVQEVLEgykkkyEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYE------------EE 243
Cdd:COG4717 171 ELAELQEELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqleneleaaaleER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 244 IRVLQSHISDTSVVVKLDNSRDLNMDCII---------------------------AEIKAQYDDIVTRSRAEAESW--- 293
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELeel 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 294 ---YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKcQNSKLEAAVAQSEQQGEAALSDARcKLAELEG 370
Cdd:COG4717 325 laaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAE-EYQELKE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1903220 371 ALQKAKQDMACLIREYQEVM--NSKLGLDIEIATYRRLLEGEEQRL 414
Cdd:COG4717 403 ELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEEL 448
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-254 |
5.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 102 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQ---FYQNRECCQ--SNLEPLFEGYIE----------------TLR 160
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEelgFESVEELEErlKELEPFYNEYLElkdaekelereekelkKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 161 REAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRatAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---- 236
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLkeel 703
|
170 180
....*....|....*....|
gi 1903220 237 --RRLYEEEIRVLQSHISDT 254
Cdd:PRK03918 704 eeREKAKKELEKLEKALERV 723
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
100-378 |
5.75e-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: 39.17 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 100 KQEEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECCQSNleplfegyIETLRREAECV--EADSGRLASEL 177
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKR--ETETGIQNLTAEIEQGQESLTEN--------LEAIKEEIENIvgEVELSKSSEEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 178 NHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDvdcaylRKSDLEANVEALIQEIDFLRRLYEEEIRVLqshisdtsvv 257
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLL---------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 258 VKLDNSRDLNMDCIIAEIKAQYDDivtrsraeaeswyrskceemkatviRHGETLRRTKEEINELNRMIQRLTAEVENAK 337
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEE-------------------------AYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1903220 338 CQNSKLEAAvaqseqqGEAALSDARCKLAELEGALQKAKQD 378
Cdd:COG5185 499 ATLEKLRAK-------LERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
310-407 |
6.59e-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: 38.59 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 310 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 389
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|....*...
gi 1903220 390 MNSklgLDIEIATYRRLL 407
Cdd:COG4942 96 RAE---LEAQKEELAELL 110
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
313-380 |
9.29e-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: 9.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1903220 313 RRTKEEINELNRM----IQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMA 380
Cdd:pfam11559 51 LEFRESLNETIRTleaeIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-238 |
9.74e-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: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 76 TTVSVNESLLTPLNLEIdpnAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRecCQSN----LEPL 151
Cdd:COG4913 269 ERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNggdrLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903220 152 fEGYIETLRREAECVEADSGRLASELNHVQEVL----EGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVE 227
Cdd:COG4913 344 -EREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|.
gi 1903220 228 ALIQEIDFLRR 238
Cdd:COG4913 423 ELEAEIASLER 433
|
|
| |
