|
Name |
Accession |
Description |
Interval |
E-value |
| KIAA1328 |
pfam15369 |
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ... |
173-495 |
0e+00 |
|
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. This family of proteins is found in eukaryotes.
Pssm-ID: 464679 Cd Length: 327 Bit Score: 548.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369 1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369 81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319
|
....*...
gi 1720392897 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
172-275 |
2.72e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100
....*....|....*....|....*...
gi 1720392897 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704 136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-277 |
1.91e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196 294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100
....*....|....*....|..
gi 1720392897 256 LTLSLSELGAARAQEQQITKKK 277
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAA 395
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
167-273 |
3.61e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|....*...
gi 1720392897 246 QKYLSEQQEKLTlslselgaARAQEQQI 273
Cdd:cd16269 268 QEALLEEGFKEQ--------AELLQEEI 287
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-274 |
2.21e-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: 40.82 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720392897 234 QYRECQEllslYQKYLSEQQEKLTLSLSELGAAR-AQEQQIT 274
Cdd:TIGR02169 897 QLRELER----KIEELEAQIEKKRKRLSELKAKLeALEEELS 934
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KIAA1328 |
pfam15369 |
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ... |
173-495 |
0e+00 |
|
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. This family of proteins is found in eukaryotes.
Pssm-ID: 464679 Cd Length: 327 Bit Score: 548.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369 1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369 81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319
|
....*...
gi 1720392897 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
172-275 |
2.72e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
90 100
....*....|....*....|....*...
gi 1720392897 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704 136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-277 |
1.91e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196 294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100
....*....|....*....|..
gi 1720392897 256 LTLSLSELGAARAQEQQITKKK 277
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAA 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
177-277 |
2.77e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 177 EDKRRIANLIKELARVSEEKEVteERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1579 70 EVEARIKKYEEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
90 100
....*....|....*....|.
gi 1720392897 257 TLSLSELgaaRAQEQQITKKK 277
Cdd:COG1579 148 DEELAEL---EAELEELEAER 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
177-276 |
3.51e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100
....*....|....*....|
gi 1720392897 257 TLSLSELGAARAQEQQITKK 276
Cdd:COG1196 382 EELAEELLEALRAAAELAAQ 401
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
167-273 |
3.61e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|....*...
gi 1720392897 246 QKYLSEQQEKLTlslselgaARAQEQQI 273
Cdd:cd16269 268 QEALLEEGFKEQ--------AELLQEEI 287
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
133-230 |
6.18e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 133 KVKASRVTDASVSMESLKgagDSVAE---QNFCKRGMKSASLKDLCLEDKR-RIANLIKELARVSEEKEVTEERLKTEQE 208
Cdd:pfam05266 57 KVKKLQVDDSRSVFESLM---ESFAElekHGFDVKAPQSRINKLLSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEID 133
|
90 100
....*....|....*....|..
gi 1720392897 209 SFEKKIRQLEEQNELIIKEREA 230
Cdd:pfam05266 134 ELEKKILELERQLALAKEKKEA 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
171-279 |
7.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 171 LKDLCLEDKRRIANLIKELARVSEEKEVTEERLKtEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQ---- 246
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEeler 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1720392897 247 -----------------KYLSEQQEKLTLSLSELGAARAQEQQITKKKNT 279
Cdd:PRK03918 377 lkkrltgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-275 |
8.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 180 RRIANLIKELARVSEEkevtEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG1196 232 LKLRELEAELEELEAE----LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90
....*....|....*.
gi 1720392897 260 LSELGAARAQEQQITK 275
Cdd:COG1196 308 EERRRELEERLEELEE 323
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-272 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 179 KRRIANLIKELARVSEEKEVTEER---LKTEQESFEKKIRQLEEQNELIIKEREALQLQYRE--------CQELLSLYQK 247
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeaelaeaEEELEELAEE 387
|
90 100
....*....|....*....|....*
gi 1720392897 248 YLSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEAL 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-274 |
2.21e-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: 40.82 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720392897 234 QYRECQEllslYQKYLSEQQEKLTLSLSELGAAR-AQEQQIT 274
Cdd:TIGR02169 897 QLRELER----KIEELEAQIEKKRKRLSELKAKLeALEEELS 934
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-324 |
2.72e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 167 KSASLKDLCLEDKRRIANLIKELARvsEEKEVTE-----ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQEL 241
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 242 LSLYQKYlSEQQEKLTLSLSELgaaRAQEQQITKKKNTPQCSLMDLDGSFLSVArpQNYGQTK-ARPKSANQVSESFTEL 320
Cdd:TIGR04523 203 LSNLKKK-IQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEKTTEISNTQ--TQLNQLKdEQNKIKKQLSEKQKEL 276
|
....
gi 1720392897 321 RNNS 324
Cdd:TIGR04523 277 EQNN 280
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-279 |
3.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
90 100
....*....|....*....|....
gi 1720392897 256 LTLSLSELGAARAQEQQITKKKNT 279
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
180-277 |
3.51e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 180 RRIANLIKELArVSEEKEVTEERLKTEQESFEKKIRQL-----EEQNELIIKEREALQLQYRECQELLSLYQ------KY 248
Cdd:pfam02463 153 ERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIidleeLKLQELKLKEQAKKALEYYQLKEKLELEEeyllylDY 231
|
90 100
....*....|....*....|....*....
gi 1720392897 249 LSEQQEKLTLsLSELGAARAQEQQITKKK 277
Cdd:pfam02463 232 LKLNEERIDL-LQELLRDEQEEIESSKQE 259
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-278 |
3.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 163 KRGMKSASLKDLcLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFE---KKIRQLEEQneliIKEREALQLQYRECQ 239
Cdd:PRK03918 222 ELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEK----VKELKELKEKAEEYI 296
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720392897 240 ELLSLYQKYLSEQQ--EKLTLSLSELGAA-RAQEQQITKKKN 278
Cdd:PRK03918 297 KLSEFYEEYLDELReiEKRLSRLEEEINGiEERIKELEEKEE 338
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
179-284 |
4.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 179 KRRIANLIKELARVSEEKEVTEERL---KTEQESFEKKIRQLEEQNELIIKEREALQlqyrecQELLSLYQKY--LSEQQ 253
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQ------EELESLQEEAeeLQEEL 117
|
90 100 110
....*....|....*....|....*....|.
gi 1720392897 254 EKLtlsLSELGAARAQEQQITKKKNTPQCSL 284
Cdd:COG4372 118 EEL---QKERQDLEQQRKQLEAQIAELQSEI 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
177-255 |
4.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720392897 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKkIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-275 |
4.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 180 RRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913 338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90
....*....|....*.
gi 1720392897 260 LSELGAARAQEQQITK 275
Cdd:COG4913 411 EAALRDLRRELRELEA 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-275 |
7.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 180 RRIANLIKELARVSEEKEVTEErLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913 668 REIAELEAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
90
....*....|....*.
gi 1720392897 260 LSELGAARAQEQQITK 275
Cdd:COG4913 747 LRALLEERFAAALGDA 762
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-276 |
8.63e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
90 100
....*....|....*....|.
gi 1720392897 256 LTLSLSELGAARAQEQQITKK 276
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLEL 464
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
187-273 |
9.59e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 37.98 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392897 187 KELARVSEEKEVTEERLKTEQESFEKKIRQ-LEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQ--EKLTLSLSEL 263
Cdd:pfam15991 22 RERKKQEQEAKMEEERLRREREEREKEDRMtLEETKEQILKLEKKLADLKEEKHQLFLQLKKVLHEDEtrKRQLKEQSEL 101
|
90
....*....|
gi 1720392897 264 GAARAQEQQI 273
Cdd:pfam15991 102 FALQQAAAQV 111
|
|
| |
