|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
103-414 |
3.14e-133 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 387.35 E-value: 3.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 103 EEKEQIKCLNSRFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNMEPLFEGYIETLRREAECVEADSGRLAAELNHA 181
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 182 QESMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDTSVIVKM 261
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 262 DNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQN 341
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318101556 342 TKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQR 414
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
38-100 |
5.56e-14 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 69.30 E-value: 5.56e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 318101556 38 GLSGGFGSQSVCGAfrsGSCGRSFGYRsGGICGPSPP--CITTVSVNESLLTPLNLEIDPNAQCV 100
Cdd:pfam16208 96 GFGGGFGGGGYGGG---GFGGGGFGGR-GGFGGPPCPpgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
153-387 |
6.89e-10 |
|
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: 61.62 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 153 FEGYI-----ETLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVALRATA--------ENEFVALKKDVDCAYLR 219
Cdd:TIGR02169 223 YEGYEllkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 220 KSDLEANAEALTQETDFL---RRMYDEETRILHSHISDTSVIVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAESWYR 296
Cdd:TIGR02169 303 IASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 297 TKCEEMKATvirhgETLRRTREEINELNRMI-------QRLTAEIENAKCQNTKLEAAVTQSeqqgEAALADARCKLAEL 369
Cdd:TIGR02169 383 TRDELKDYR-----EKLEKLKREINELKRELdrlqeelQRLSEELADLNAAIAGIEAKINEL----EEEKEDKALEIKKQ 453
|
250
....*....|....*...
gi 318101556 370 EGALQKAKQDMACLLKEY 387
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-415 |
4.06e-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: 52.75 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 123 RFLEQQNKLLETKWQFYQNRKccESnmeplFEGYIETLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEevalratA 202
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRL--EE-----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-------L 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 203 ENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILHSHISDtsvivKMDNSRDLN-MDCVVAEIKAQYD 281
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAeLEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 282 DIASRSRAEAESWyrtkcEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALAD 361
Cdd:TIGR02168 355 SLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 318101556 362 A-RCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 415
Cdd:TIGR02168 430 LeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-415 |
5.98e-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: 52.37 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 92 EIDPNAQCVKhEEKEQIKCLNSRFAAFIDKVRFLEQQNKLLETKWQfYQNRKCCESNMEplfegyIETLRREAECVEADS 171
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKD------LARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 172 GRLAAELNHAQESMEGYKKRYEEEVALRATAENEfvalkkdvdcaylrKSDLEANAEALTQETDFLRRMYDEETRILhsh 251
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------------IEELEAQIEQLKEELKALREALDELRAEL--- 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 252 isdtsvivkmdnsRDLNmdcvvaeikaqyddiasRSRAEAeswyRTKCEEMKATVIRHGETLRRTREEINELNRMIQRLT 331
Cdd:TIGR02168 813 -------------TLLN-----------------EEAANL----RERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 332 AEIENAKCQNTKLEAAV---TQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEvmnsklgLDVEIITYRRLL 408
Cdd:TIGR02168 859 AEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-------LREKLAQLELRL 931
|
....*..
gi 318101556 409 EGEEQRL 415
Cdd:TIGR02168 932 EGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-415 |
1.42e-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: 47.74 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 188 YKKRYEE-EVALRATAEN----EFVA--LKKDVDcaylrksDLEANAEAlTQETDFLRrmydEETRILHSHISDTSVIVK 260
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEK-AERYKELK----AELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 261 MDNSRDLNMDcvVAEIKAQYDDIASRSRAEAESWYRTKCE--EMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 338
Cdd:TIGR02168 238 REELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 339 CQNTKLEAAVTQSEQQGE---AALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 415
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-376 |
2.16e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 159 TLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLR 238
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 239 RMYDEetrilhshisdtsVIVKMDNSRDL--NM-------DCVVAE---IKAQYDDiaSRSRAEAESwyRTKceEMKA-T 305
Cdd:pfam01576 580 QELDD-------------LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318101556 306 VIRHGETLRRTREEINELNRMiqrLTAEIE---NAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKA 376
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
313-381 |
7.41e-05 |
|
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: 43.07 E-value: 7.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 318101556 313 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMA 381
Cdd:pfam11559 47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
313-415 |
1.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 313 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 389
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 318101556 390 VMNSKLGLDVEIITYRRLLEGEEQRL 415
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-393 |
2.03e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 313 LRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 389
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
....
gi 318101556 390 VMNS 393
Cdd:COG4942 109 LLRA 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
157-379 |
2.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 157 IETLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEvALRATAENEFVALKKDVDCaylRKSDLEANAEALTQETDF 236
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEA-ARKAEEERKAEEARKAEDA---KKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 237 LRRMydEETRilhshisDTSVIVKMDNSRDLNMDCVVAEIKAQYDDIASRSRAEAEswyRTKCEEM-KATVIRHGETLRR 315
Cdd:PTZ00121 1242 AKKA--EEER-------NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 318101556 316 TREEinelNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQD 379
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
125-391 |
2.27e-04 |
|
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: 43.73 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 125 LEQQNKLLETKWQFYQNRKccesNMEPLFEGYIETLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVALRATAEN 204
Cdd:pfam07888 40 LQERAELLQAQEAANRQRE----KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 205 EFVALKKDVDCAYLRKSDLEANAEALTQ-----ETDfLRRMYDEETRI------------------------LHSHIS-- 253
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQrvlerETE-LERMKERAKKAgaqrkeeeaerkqlqaklqqteeeLRSLSKef 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 254 ----------DTSVIVKMD------------NSRDLNMDCVVAEIKAQYD--------------DIAS----RSRAEAE- 292
Cdd:pfam07888 195 qelrnslaqrDTQVLQLQDtittltqklttaHRKEAENEALLEELRSLQErlnaserkveglgeELSSmaaqRDRTQAEl 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 293 --------------SWYRTKCEEMKATVIRHGETLRRT----REEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQ 354
Cdd:pfam07888 275 hqarlqaaqltlqlADASLALREGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDC 354
|
330 340 350
....*....|....*....|....*....|....*..
gi 318101556 355 GEAALADARCKLAELEGALQKAKQDMACLLKEYQEVM 391
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
168-379 |
2.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 168 EADSGRLAAELNHAQESMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRI 247
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 248 L---------HSHISDTSVIVKMDNSRDlnmdcvvAEIKAQYDDIASRSRAEaeswyrtkceemkatvirHGETLRRTRE 318
Cdd:COG4942 106 LaellralyrLGRQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELRADLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318101556 319 EINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQD 379
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-330 |
2.36e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 103 EEKEQIKCLNSRFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCESNMEPLFEGYIETLRREAECVEADSGRLAAELNHAQ 182
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 183 ESMEGYKKRYEEEVALRATAENEFVALKKdvdcaylRKSDLEANAEALTQETDFLRRMYDEETRILHshisdtsvivkmd 262
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLA------------- 925
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 318101556 263 nsrDLNMDCvvAEIKAQYDDIASRSRAEaeswYRTKCEEMKATVIRHGETLRRTREEINELNRMIQRL 330
Cdd:TIGR02168 926 ---QLELRL--EGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-395 |
3.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 311 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEA---AVTQSEQQGEAALADARCKLAELEGALQKAKQDMACLLKEY 387
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
....*...
gi 318101556 388 QEVMNSKL 395
Cdd:COG4372 174 QALSEAEA 181
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
153-338 |
4.43e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 153 FEGYIETLRREAECVEADSGRLaaELNHAQESMEGYKKR----Y---EEEVAlratAENeFVALKKDVDCAYLRKsdLEA 225
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERidqlYdilEREVK----ARK-YVEKNSDTLPDFLEH--AKE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 226 NAEALTQETDFLRRMYdeetrilhsHISDTsvivKMDNSRDLNMDcvVAEIKAQYDDIASRS----------RAEAESWY 295
Cdd:PRK04778 325 QNKELKEEIDRVKQSY---------TLNES----ELESVRQLEKQ--LESLEKQYDEITERIaeqeiayselQEELEEIL 389
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 318101556 296 RTkCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAK 338
Cdd:PRK04778 390 KQ-LEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIK 431
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
311-415 |
7.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 311 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQgeaaLADARCKLAELEGALQKAKQDMACLLKEYQEV 390
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100
....*....|....*....|....*
gi 318101556 391 MNSKLGLDVEIITyrrlLEGEEQRL 415
Cdd:COG4372 107 QEEAEELQEELEE----LQKERQDL 127
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
101-394 |
1.08e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 101 KHEEKEQIKCLNSRFAAFIDKVRFLEQQNKLLE-TKWQFYQNRKCCESNMEPLFEGYIETLR----------REAECVEA 169
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKsRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrtvREKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 170 DSGRLAAELNhaQESMEGYKKRYEEEValrataENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEETRILH 249
Cdd:TIGR00606 323 DCQRELEKLN--KERRLLNQEKTELLV------EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 250 SHisdTSVIVKM-DNSRDLNMDCvvAEIKAQyddiaSRSRAEAESWYRTKCEEMKATVIRHGETLRRTREEINELNRMIQ 328
Cdd:TIGR00606 395 FH---TLVIERQeDEAKTAAQLC--ADLQSK-----ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 329 RLTAEIENAkcqnTKLEAAVTQSEQqgEAALAD----ARCKLAElEGALQKAKQDMACLLKEYQEVMNSK 394
Cdd:TIGR00606 465 QLEGSSDRI----LELDQELRKAER--ELSKAEknslTETLKKE-VKSLQNEKADLDRKLRKLDQEMEQL 527
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
274-381 |
1.45e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 274 AEIKAQYDDIASRSRAEAESwyrtkceemKATVIRHGETLR------RTREEINELNRMIQRLTAEIENAKCQNTKLEAA 347
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 318101556 348 VTQSEQQ--GEAALADARCKLAELEGALQKAKQDMA 381
Cdd:PRK11281 110 NDEETREtlSTLSLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
273-415 |
1.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 273 VAEIKAQYDDIASRSRAEAESWYrtkceEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSE 352
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318101556 353 QQG----------EAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 415
Cdd:COG1196 344 EELeeaeeeleeaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
173-360 |
2.15e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 173 RLAAELNHAQESMEGYKKRYEEEVALRATAENEFVALKkDVDC--AYLRKSD----LEANA---EALTQETDFLRRMYDE 243
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQrrAHFSYEDaaemLAKNSdlnEKLRQRLEQAEQERTR 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 244 ETRILHSHISD----TSVIVKMDNSRDLNMDcVVAEIKAQYDDIASRSRAEAESWYRTKCEEMkatvirHGEtLRRTREE 319
Cdd:PRK04863 1004 AREQLRQAQAQlaqyNQVLASLKSSYDAKRQ-MLQELKQELQDLGVPADSGAEERARARRDEL------HAR-LSANRSR 1075
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 318101556 320 INELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALA 360
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
126-360 |
2.81e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 126 EQQNKLLETKWQFYQNRKCCESnMEPLfegyIETLRREAECVEAdsgrLAAELNHAQESMEGYKKRYE--EEVALRATA- 202
Cdd:COG3096 900 EELDAAQEAQAFIQQHGKALAQ-LEPL----VAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQQIFalSEVVQRRPHf 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 203 --ENEFVALKKDVDCAYLRKSDLEANAEALTQETDFLRRMYDEetrilhsHISDTSVIVKMDNSRDLNMDcVVAEIKAQY 280
Cdd:COG3096 971 syEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQ-------YSQYNQVLASLKSSRDAKQQ-TLQELEQEL 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 281 DDIASRSRAEAESWYRTKCEEMKatvirhgETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALA 360
Cdd:COG3096 1043 EELGVQADAEAEERARIRRDELH-------EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-409 |
3.97e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 158 ETLRREAECVEADSGRLAAELNHAQESMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQETDFL 237
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 238 RRMYDEetriLHSHISDtsvivkmdnsrdlnMDCVVAEIKAQYDDIASRSRAEAESWYRTKCEEMKATVIRHGETLRRTR 317
Cdd:TIGR02169 757 KSELKE----LEARIEE--------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 318 EEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQGE----------AALADARCKLAELEGALQKAKQDMACLLKEY 387
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260
....*....|....*....|..
gi 318101556 388 QEVMNSKLGLDVEIITYRRLLE 409
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLS 920
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-379 |
4.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 273 VAEIKAQYDDIASRSRAEAESWYRtkcEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAKCQNT--KLEAAV-T 349
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDE---EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELeE 480
|
90 100 110
....*....|....*....|....*....|..
gi 318101556 350 QSEQQGEAALADARCKLAE--LEGALQKAKQD 379
Cdd:COG4717 481 LKAELRELAEEWAALKLALelLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
272-415 |
6.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 272 VVAEIKAQYDDIAsRSRAEAESW--YRTKCEEMKATVI-----RHGETLRRTREEINELNRMIQRLTAEIENAKCQNTKL 344
Cdd:COG1196 194 ILGELERQLEPLE-RQAEKAERYreLKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 318101556 345 EAAVTQSEQQGEAALADarckLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDVEIITYRRLLEGEEQRL 415
Cdd:COG1196 273 RLELEELELELEEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-415 |
7.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 311 ETLRRTREEINELNRMIQRLTAEIENAKcqnTKLEAAVTQSEQQGEAALADARCKLAELEGALQKAKQDmaclLKEYQEV 390
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE----LEEAQEE 221
|
90 100
....*....|....*....|....*
gi 318101556 391 MNSKLGlDVEIITYRRLLEGEEQRL 415
Cdd:COG4717 222 LEELEE-ELEQLENELEAAALEERL 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-389 |
7.49e-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: 7.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 318101556 311 ETLRRTREEINELNRMIQRLTAEIENAKCQNTKLEAAVTQSEQQgeaaLADARCKLAELEGALQKAKQDMACLLKEYQE 389
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAE 94
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
298-370 |
8.34e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 36.41 E-value: 8.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 318101556 298 KCEEMKATVIRHGETLRRTREEINELNRMIQRLTAEIENAkcqNTKLEAAvtqsEQQGEAALADARCKLAELE 370
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENA---QEKLERL----REQAEEKREAAQARLEELR 116
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
286-411 |
9.01e-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: 38.16 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 318101556 286 RSRAEAESWyrtkcEEMKATVIRHGETLRRTREE--------------INELNRMIQRltAEIENAKCQNTKLEAAVTQS 351
Cdd:pfam14992 44 RSLAEDEER-----EELNFTIMEKEDALQELELEtaklekkneilvksVMELQRKLSR--KSDKNTGLEQETLKQMLEEL 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 318101556 352 E---QQGEAALADARCKLAELEGALQKAKQ---DMACLLKEYQEVMNsKLGLDVEIityrRLLEGE 411
Cdd:pfam14992 117 KvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILR-KMEEEKET----RLLEKE 177
|
|
| |
