|
Name |
Accession |
Description |
Interval |
E-value |
| SH3_MIA3 |
cd11893 |
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or ... |
37-109 |
1.45e-45 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212826 Cd Length: 73 Bit Score: 158.47 E-value: 1.45e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433638 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVGRTFGYFPKDLIQVVHEYT 109
Cdd:cd11893 1 RCADEECSMLLCRGKAVKDFTGPDCRFLSFKKGETIYVYYKLSGRRTDLWAGSVGFDFGYFPKDLLDVNHLYT 73
|
|
| SH3_MIA_like |
cd11760 |
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a ... |
37-109 |
9.17e-39 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity protein and similar proteins; MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. MIA is a member of the recently identified family that also includes MIA-like (MIAL), MIA2, and MIA3 (also called TANGO); the biological functions of this family are not yet fully understood.
Pssm-ID: 212694 Cd Length: 76 Bit Score: 139.15 E-value: 9.17e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVG---RTFGYFPKDLIQVVHEYT 109
Cdd:cd11760 1 LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGgdaGLFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
38-109 |
1.25e-25 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed specifically in hepatocytes and its expression is controlled by hepatocyte nuclear factor 1 binding sites in the MIA2 promoter. It inhibits the growth and invasion of hepatocellular carcinomas (HCC) and may act as a tumor suppressor. A mutation in MIA2 in mice resulted in reduced cholesterol and triglycerides. Since MIA2 localizes to ER exit sites, it may function as an ER-to-Golgi trafficking protein that regulates lipid metabolism. MIA2 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA3 (also called TANGO). MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212825 Cd Length: 73 Bit Score: 101.84 E-value: 1.25e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1022433638 38 CADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVGRTFGYFPKDLIQVVHEYT 109
Cdd:cd11892 2 CGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
36-124 |
1.82e-18 |
|
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands. It binds peptide ligands with sequence similarity to type III human fibronectin repeats.
Pssm-ID: 212823 Cd Length: 98 Bit Score: 82.23 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 36 KLCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEVWAGSVGRTF--------GYFPKDLIQVVHE 107
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYygeqaarlGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 1022433638 108 YTKEELQVPTDETDFVC 124
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
37-108 |
3.20e-18 |
|
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and the vestibule of the inner ear and may contribute to inner ear dysfunction in humans. MIAL is a member of the recently identified family that also includes MIA, MIA2, and MIA3 (also called TANGO); MIA is the most studied member of the family. MIA is a single domain protein that adopts a Src Homology 3 (SH3) domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. MIA is secreted from malignant melanoma cells and it plays an important role in melanoma development and invasion. MIA is expressed by chondrocytes in normal tissues and may be important in the cartilage cell phenotype. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212824 Cd Length: 83 Bit Score: 81.06 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLAR--GWPEVWAGSVGR--------TFGYFPKDLIQVVH 106
Cdd:cd11891 1 LCADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKenGAGEFWSGSVYSeryvdqmgIVGYFPSNLVKEQT 80
|
..
gi 1022433638 107 EY 108
Cdd:cd11891 81 VY 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1217-1526 |
2.59e-14 |
|
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: 78.96 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1217 SEKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES-ERE 1295
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1296 QNvknQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHA 1375
Cdd:TIGR02169 788 LS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1376 ELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMM 1455
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022433638 1456 DVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 1526
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1212-1591 |
3.29e-14 |
|
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: 78.14 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1212 TEQQISEKLKTIMKENTELVQKLSNYEQKIK----ESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEilDDTAKNLR 1287
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1288 VMLESEREQNVKNQDLISENKKSIEKLKDVIS------MNA-SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1360
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkelTNSeSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1361 EQLQQEIEDWSKLHAELSEQIKSF-------EKSQKDLEVALTHKDDNINALTNCITQLNLL--ECESESEGQNKG---- 1427
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLETQlkvl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1428 ----GNDSDELANGEVGGDRNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQ 1503
Cdd:TIGR04523 474 srsiNKIKQNLEQKQKELKSKEKELKKLNE--EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1504 A--AKAGLEDECKTLRQKVEIL---NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYK---RRIEE 1575
Cdd:TIGR04523 552 FelKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkenEKLSS 631
|
410
....*....|....*.
gi 1022433638 1576 MEDELQKTERSFKNQI 1591
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1214-1521 |
6.16e-12 |
|
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: 71.24 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 1293
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKL 1373
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1374 HAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKggndSDELANGEvggDRNEKMKNQIKQ 1453
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE---SKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022433638 1454 MMD-VSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQVKKLEDDRNSLQAAkaglEDECKTLRQKVE 1521
Cdd:TIGR02168 920 LREkLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1220-1600 |
1.12e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1220 LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVK 1299
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1300 NQDLISENKKSIEKLKDVISMnasefSEVQIALNEAKLSEEKVKSECHRVQEENARLKK---KKEQLQQEIEDWSKLHAE 1376
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1377 LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLnllecesesegqnkggndSDELanGEVGGDRnEKMKNQIKQMMD 1456
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL------------------ESRL--GDLKKER-DELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1457 vSRTQTAISVVEEDLKLLQLKLRASvstkcNLEDQVKKLEDdrnslqAAKAGLEDECKTLrqkveILNELYQQKEMALQk 1536
Cdd:TIGR02169 904 -KIEELEAQIEKKRKRLSELKAKLE-----ALEEELSEIED------PKGEDEEIPEEEL-----SLEDVQAELQRVEE- 965
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 1537 klsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE---RSFKNQIATHEKKAHE 1600
Cdd:TIGR02169 966 --------------EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1306-1581 |
2.72e-11 |
|
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: 68.93 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1306 ENKKSIEKLKDVISMNASEFSEVQIALNEAKlseekvksechrvqEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFE 1385
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR--------------KELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1386 KSQKDLEVALTHKDDNINALTNCITQlnLLECESESEGQNKGGNDSDELANGEVGGDRNEkMKNQIKQM----MDVSRTQ 1461
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEE--LEERLEEAEEELAEAEAEIEELEAQIEQLKEE-LKALREALdelrAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1462 TAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE---MALQKKL 1538
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealALLRSEL 896
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1022433638 1539 SQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 1581
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1232-1577 |
5.49e-11 |
|
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: 68.16 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1232 QKLSNYEQKIKESKKHVQETRKQnmilsdeaikykdkIKTLEKNQEILDDTAKNLRVMLESEREQnvknqdlISENKKSI 1311
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA--------------LAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1312 EKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDL 1391
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1392 EVALThkdDNINALTNCITQLNLLECESE-SEGQNKGGNDSDELANGEVG--GDRNEKMKNQIKQMMDvsrtqtAISVVE 1468
Cdd:TIGR02168 816 NEEAA---NLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEelEELIEELESELEALLN------ERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1469 EDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKV----EILNELYQQKEMALQKKLSQEEYE 1544
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKIEDD 966
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1022433638 1545 RQEREHRLSAADEK-----AV--SAAEEVKTYKRRIEEME 1577
Cdd:TIGR02168 967 EEEARRRLKRLENKikelgPVnlAAIEEYEELKERYDFLT 1006
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1218-1536 |
2.36e-10 |
|
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: 66.15 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1218 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRK---------------QNMILSDEAIKYKDKIKTLEKNQEILDDT 1282
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1283 AKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 1362
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1363 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddniNALTNCITQLNLLECESESEGQnKGGNDSDELANGEVGGD 1442
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1443 RNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 1522
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330
....*....|....
gi 1022433638 1523 LNELYQQKEMALQK 1536
Cdd:pfam02463 488 LLLSRQKLEERSQK 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1262-1592 |
3.02e-10 |
|
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: 65.85 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1262 AIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNvknqdliSENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEK 1341
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1342 VKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNlleceses 1421
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN-------- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1422 egqnkggndsDELANGEVGGDRNEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNS 1501
Cdd:TIGR02168 817 ----------EEAANLRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1502 LQAAKAGLEDECKTLRQKVEILN----ELYQQKEmALQKKLSQEEYE----RQEREHRLSAADEKAVSAAEEVKTYKRRI 1573
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELEskrsELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
330
....*....|....*....
gi 1022433638 1574 EEMEDELQKTERSFKNQIA 1592
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIK 982
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1529 |
3.13e-10 |
|
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: 65.43 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEK---LKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsdeaikyKDKIKTLEKNQEILDDTAKNLRvm 1289
Cdd:TIGR04523 362 QRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLK-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1290 leserEQNVKNQDLISENKKSIEKLKdvismnasefsevqIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 1369
Cdd:TIGR04523 433 -----ETIIKNNSEIKDLTNQDSVKE--------------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1370 WSKLHAELSEQIKSFEKSQKDLEvalthkdDNINALTNCITQLNLLECESESE---GQNKGGNDSDELANGEVGGDRNEK 1446
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLT-------KKISSLKEKIEKLESEKKEKESKisdLEDELNKDDFELKKENLEKEIDEK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1447 MKNqIKQMmdvSRTQTAISVVEEDLKLL-------QLKLRASVSTKcnlEDQVKKLEDDRNSLQAAKAGLEDECKTLRQK 1519
Cdd:TIGR04523 567 NKE-IEEL---KQTQKSLKKKQEEKQELidqkekeKKDLIKEIEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
330
....*....|
gi 1022433638 1520 VEILNELYQQ 1529
Cdd:TIGR04523 640 KNKLKQEVKQ 649
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1644-1917 |
4.51e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.34 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1644 KPMPGKPNTQNPPRrgPLSQNGSFGPSPVSGGECSPPLTVEP--PVRPLSATLNRRDMPRSEFGSVDGPlPHPRWSAEAS 1721
Cdd:PHA03247 2700 DPPPPPPTPEPAPH--ALVSATPLPPGPAAARQASPALPAAPapPAVPAGPATPGGPARPARPPTTAGP-PAPAPPAAPA 2776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1722 GKPSPSDPGSGTATMMNSSSRGSSPTRVLDEGKQTVLQEPEVPSVPSITSLAERPVAVnmAPKGPPPFPGVPLMSTPMGG 1801
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA--QPTAPPPPPGPPPPSLPLGG 2854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1802 PVPPPIRygpppqLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPG 1881
Cdd:PHA03247 2855 SVAPGGD------VRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927
|
250 260 270
....*....|....*....|....*....|....*.
gi 1022433638 1882 TRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQ 1917
Cdd:PHA03247 2928 QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1213-1639 |
9.15e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEkLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES 1292
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1293 EREqnvknqdlISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQEIEDWSK 1372
Cdd:COG4717 155 LEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1373 LHAELSEQIKSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNLLECESESEGQNKG 1427
Cdd:COG4717 221 ELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1428 GNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLqAAKA 1507
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1508 GLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTE 1584
Cdd:COG4717 380 GVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1022433638 1585 RSFKNQIATHEKkahenwlkaraaeraiaeeKREAANLRHKLLELTQKMAMLQEE 1639
Cdd:COG4717 456 AELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1214-1629 |
1.43e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAK---NLRVML 1290
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1291 ESeREQNVKN--------QDLISENKKSIEKLKDvismNASEFSEVQ-IALNEAKLSE--EKVKSECHRVQEENARLKKK 1359
Cdd:PRK03918 248 ES-LEGSKRKleekirelEERIEELKKEIEELEE----KVKELKELKeKAEEYIKLSEfyEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1360 KEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEV---------ALTHKDDNINALTNCITQLNLLECESESEGQNKGGND 1430
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1431 SDELANgEVGGDRNEkMKNQIKQMMD-VSRTQTAISVV--------EEDLKLLQLKLRASVStkcNLEDQVKKLEDDRNS 1501
Cdd:PRK03918 403 IEEEIS-KITARIGE-LKKEIKELKKaIEELKKAKGKCpvcgreltEEHRKELLEEYTAELK---RIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1502 LQAAKAGLEDECKTLRqKVEILNELYQQKEmALQKKLSQEEYErqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 1581
Cdd:PRK03918 478 LRKELRELEKVLKKES-ELIKLKELAEQLK-ELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1022433638 1582 KTErSFKNQIATHEKKAHEnwlkaraaeraiaeEKREAANLRHKLLEL 1629
Cdd:PRK03918 550 KLE-ELKKKLAELEKKLDE--------------LEEELAELLKELEEL 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1241-1584 |
5.76e-09 |
|
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: 61.61 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1241 IKESKKHVQETRKQnmilSDEAIKYKDKiktleKNQeiLDDTAKNLRVM-LESEREQNVKNQDLISENKKSIEKLKDVIS 1319
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKEL-----KAE--LRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1320 MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD 1399
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1400 DNINALTNCITQLNLLECESESEGQNkggndsdelangevggdRNEKMKNQIKQMMDVSRtqtAISVVEEDLKLLQLKLR 1479
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEE-----------------LESRLEELEEQLETLRS---KVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1480 asvstkcNLEDQVKKLEDDRNSLQAAKAGLEDEcKTLRQKVEILNELYQQKEMA--LQKKLSQEEYERQEREHRLSAADE 1557
Cdd:TIGR02168 404 -------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*..
gi 1022433638 1558 KAVSAAEEVKTYKRRIEEMEDELQKTE 1584
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1639 |
1.15e-08 |
|
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: 60.42 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEKLKTIMKE--NTELVQK-----LSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKN 1285
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1286 lrvmlesEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 1365
Cdd:TIGR04523 115 -------DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1366 EIED-----------------WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI----TQLN----------- 1413
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNqlkdeqnkikk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1414 -LLECESESEGQNKGGND-SDELA---------NGEVGGDRNEKMKNQIKQM--------MDVSRTQTAISVVEEDLKLL 1474
Cdd:TIGR04523 268 qLSEKQKELEQNNKKIKElEKQLNqlkseisdlNNQKEQDWNKELKSELKNQekkleeiqNQISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1475 QLKLRASVSTKCNL-------EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALqKKLSQEEYERQE 1547
Cdd:TIGR04523 348 KKELTNSESENSEKqreleekQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-KKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1548 REHRLSAADEKAVSAAEE-----------VKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKaraaERAIAEEK 1616
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDltnqdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK----EKELKKLN 502
|
490 500
....*....|....*....|...
gi 1022433638 1617 REAANLRHKLLELTQKMAMLQEE 1639
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEK 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1214-1405 |
1.33e-08 |
|
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: 59.01 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEIL-DDTAKNLRVMLES 1292
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1293 EREQNVK---NQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 1369
Cdd:COG4942 117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1022433638 1370 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 1405
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1216-1600 |
2.12e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1216 ISEKLKTIMKENTELVQKLSNYEQKIKESKKhVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLEsERE 1295
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1296 QNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLH 1374
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1375 AELSEQIKSFEKSQKDLEVA----------LT--HKDDNINALTNCITQL--NLLECESESEGQNKGGNDSDELANGEVG 1440
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgreLTeeHRKELLEEYTAELKRIekELKEIEEKERKLRKELRELEKVLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1441 GDRNEKMKNQIKQM------MDVSRTQTAISVVEEdLKLLQLKLRASVStkcNLEDQVKKLEDDRNSLQA---AKAGLED 1511
Cdd:PRK03918 495 LIKLKELAEQLKELeeklkkYNLEELEKKAEEYEK-LKEKLIKLKGEIK---SLKKELEKLEELKKKLAElekKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1512 ECKTLRQK--------VEILNELYQQKEMALQK--KLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 1581
Cdd:PRK03918 571 ELAELLKEleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
410
....*....|....*....
gi 1022433638 1582 KTERSFKNQiaTHEKKAHE 1600
Cdd:PRK03918 651 ELEKKYSEE--EYEELREE 667
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1261-1581 |
3.80e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1261 EAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDvismnasEFSEVQIALNEAKLSEE 1340
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1341 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddninaltncitQLNLLECESE 1420
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA------------EAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1421 SEgqnkggndsdelangEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRN 1500
Cdd:COG1196 367 LL---------------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1501 SLQAAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL 1580
Cdd:COG1196 432 ELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
.
gi 1022433638 1581 Q 1581
Cdd:COG1196 508 E 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1214-1639 |
8.95e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 1293
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISENKK-----SIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK---EQLQQ 1365
Cdd:TIGR02168 420 QQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1366 EIEDWSK--------------LHAELSEQIKSFEKSQKDLEVAL-------THKDDN-----INALT-NCITQLNLLECE 1418
Cdd:TIGR02168 500 NLEGFSEgvkallknqsglsgILGVLSELISVDEGYEAAIEAALggrlqavVVENLNaakkaIAFLKqNELGRVTFLPLD 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1419 SESEGQNKgGNDSDELAN--GEVG-GDRNEKMKNQIKQMMD--------VSRTQTAIsvveEDLKLLQLKLR-------- 1479
Cdd:TIGR02168 580 SIKGTEIQ-GNDREILKNieGFLGvAKDLVKFDPKLRKALSyllggvlvVDDLDNAL----ELAKKLRPGYRivtldgdl 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1480 ---------ASVSTKC----------NLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEM---ALQKK 1537
Cdd:TIGR02168 655 vrpggvitgGSAKTNSsilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKD 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1538 LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHENWLKARAAERAIAE 1614
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTL 814
|
490 500
....*....|....*....|....*
gi 1022433638 1615 EKREAANLRHKLLELTQKMAMLQEE 1639
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERR 839
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1647-1931 |
8.97e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.64 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1647 PGKPNTQNPPRRGPL--SQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKP 1724
Cdd:PHA03247 2670 LGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1725 SPSDPGSGTATMMNSSSRGSSPTRVLDEGKQTVLQEPEV-------PSVPSITSLAERPVAV------------------ 1779
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesrESLPSPWDPADPPAAVlapaaalppaaspagplp 2829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1780 ---NMAPKGPPPFPGVPLMSTPMGGPVPPPIRygpppqLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGRRDLPLHP 1856
Cdd:PHA03247 2830 pptSAQPTAPPPPPGPPPPSLPLGGSVAPGGD------VRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPP 2902
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433638 1857 RGflpghaPFRPlgslgpreyfiPGTRLPPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQDCSQALKQSP 1931
Cdd:PHA03247 2903 DQ------PERP-----------PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1214-1639 |
9.62e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKH-------VQETRKQNMILSDEAIKYKDKIktleknQEILDDTAKNL 1286
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseLTEARTERDQFSQESGNLDDQL------QKLLADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1287 RvMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 1361
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1362 ------QLQQEIEDWSKLHAELSEQIKSFEKSQK---DLEVALTHKDDNINALTNCITQL---------NLLECESESEG 1423
Cdd:pfam15921 463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrsrvdlklqELQHLKNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1424 QNKGGNDSDELANGEVGGDRN-EKMKNQIKQMMDV----SRTQTAISV----VEEDLKLLQLKLRASVSTKCNLEDQVKK 1494
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1495 LEDDRNSLQAAK-----AGLE----------------DECKTLRQKVEILNELYQqkemALQKKLSQEEYERQEREHRLS 1553
Cdd:pfam15921 623 LEARVSDLELEKvklvnAGSErlravkdikqerdqllNEVKTSRNELNSLSEDYE----VLKRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1554 AADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKM 1633
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
....*.
gi 1022433638 1634 AMLQEE 1639
Cdd:pfam15921 779 STVATE 784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1225-1600 |
1.27e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1225 KENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLI 1304
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1305 SENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKKEQLQQEIEDWSKLHAELSEQIK 1382
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1383 SFEKSQKdLEVALTHKDDNINALTNCiTQLNLLEcESESEGQNKGGNDSDELANGEVGGDRNEKMK-NQIKQMMDVSRT- 1460
Cdd:PTZ00121 1559 KAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKv 1635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1461 -QTAISVVEEDLKLLQLKlRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQkkLS 1539
Cdd:PTZ00121 1636 eQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEE--LK 1708
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022433638 1540 QEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSfKNQIAtHEKKAHE 1600
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIA-HLKKEEE 1767
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1209-1410 |
2.16e-07 |
|
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: 56.18 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1209 YQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRV 1288
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1289 MLE-SEREQNVKNQD---LISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLkkKKEQLQ 1364
Cdd:TIGR04523 483 NLEqKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL--KKENLE 560
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1022433638 1365 QEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCIT 1410
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
49-105 |
2.19e-07 |
|
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 49.13 E-value: 2.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 49 RGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWpevWAGSVGRTFGYFPKDLIQVV 105
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGKDNDGW---WEGETGGRVGLVPSTAVEEI 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1218-1531 |
3.34e-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: 55.83 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1218 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQN 1297
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1298 VKNQDLISENKKSIEKLkdvismnasefsevqialneaklseekvksechrvQEENARLKKKKEQLQQEIEDWSKLHAEL 1377
Cdd:TIGR02168 319 EELEAQLEELESKLDEL-----------------------------------AEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1378 SEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLN--LLECESESEGQnkggNDSDELANGEVGGDRNEKMKNQIKqmm 1455
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNneIERLEARLERL----EDRRERLQQEIEELLKKLEEAELK--- 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 1456 dvsRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKE 1531
Cdd:TIGR02168 437 ---ELQAELEELEEELEELQEELER-------LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1205-1623 |
3.60e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1205 KDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMI--LSDEAIKYKDKIKTLEKNQEILDDT 1282
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1283 AKNLRvmlESEREQNVKNQdliSENKKSIEKLKdvismnaSEFSEVQIALNEAKLSEEKVKSECHRVQEENAR----LKK 1358
Cdd:PTZ00121 1424 KKKAE---EKKKADEAKKK---AEEAKKADEAK-------KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1359 KKEQLQQEIEDWSKLHAE--LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELAN 1436
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAkkKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1437 GEVGGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEdQVKKLEDDRNSLQAAKAGLEDECKTL 1516
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1517 RQkVEILNELYQQKEMALQKKlsqeEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEdELQKTERSFKNQIATHEK 1596
Cdd:PTZ00121 1650 EE-LKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKK 1723
|
410 420
....*....|....*....|....*..
gi 1022433638 1597 KAHENWLKARAAERAIAEEKREAANLR 1623
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1213-1416 |
5.59e-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: 55.06 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEKLKTIMKENTELV---QKLSNYEQKIKESKKHVQETRKQ----NMILSDEAIKYKDKIKTLEKNQEILDDTAKN 1285
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1286 LRVM---LESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 1362
Cdd:TIGR02168 840 LEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1022433638 1363 LQQEIED----WSKLHAELSEQIKSF-EKSQKDLEVALTHKDDNINALTNCITQLNLLE 1416
Cdd:TIGR02168 920 LREKLAQlelrLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1212-1585 |
7.07e-07 |
|
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: 54.36 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1212 TEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILddTAKNLRVMlE 1291
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 SEREQNVKNQDLIsENKKSIEKLKDVISMNAS-EFSEVQIA-LNEAKLSEEKVKSECH----------RVQEENARLKKK 1359
Cdd:pfam05557 175 LEFEIQSQEQDSE-IVKNSKSELARIPELEKElERLREHNKhLNENIENKLLLKEEVEdlkrklereeKYREEAATLELE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1360 KEQLQQEIEDWSKLHAE----------LSEQIKSFEKSQkdlevaLTHKDDNiNALTNCITQLNLLECESESEGQNKGGN 1429
Cdd:pfam05557 254 KEKLEQELQSWVKLAQDtglnlrspedLSRRIEQLQQRE------IVLKEEN-SSLTSSARQLEKARRELEQELAQYLKK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1430 DSDElangevggdrNEKMKNQIKQmmdVSRTQTAISVVEEDLKLLQLKLR------ASVSTKCNLEDQVKKLEDDRNSLQ 1503
Cdd:pfam05557 327 IEDL----------NKKLKRHKAL---VRRLQRRVLLLTKERDGYRAILEsydkelTMSNYSPQLLERIEEAEDMTQKMQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1504 AAKAGLEDECKTLRQKVEILNELYQQKEMALQKKlsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKT 1583
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-------------RQQESLADPSYSKEEVDSLRRKLETLELERQRL 460
|
..
gi 1022433638 1584 ER 1585
Cdd:pfam05557 461 RE 462
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1645-1916 |
8.30e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1645 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRsefgsvdGPLPHPRWSAEASgKP 1724
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA-------GPLPPPTSAQPTA-PP 2840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1725 SPSDPGSGTATMMNSSSRGSsPTRVLDEGKQTVlQEPEVPSVPSITSLAERPVAVNMAPKGPPPFPGVPLMSTPMGGPVP 1804
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGG-DVRRRPPSRSPA-AKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1805 PPIRYGPPPQLCGPFGPRPlpppfgpgmRPPlglrefapgvPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREYFIPGTRL 1884
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPP---------RPQ----------PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1022433638 1885 PPPTHG-PQEYPPPPAVRDLLPSG-----------SRDEPPPAS 1916
Cdd:PHA03247 2980 PQPAPSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1229-1523 |
9.73e-07 |
|
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: 54.30 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1229 ELVQKLSNYEQKIKESKKHVQETRKQNmILSDEAikykDKIKTLEKNQEILDDTAK------------NLRVMLESEREQ 1296
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEA-IERQLA----SLEEELEKLTEEISELEKrleeieqlleelNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1297 N-VKNQdlISENKKSIEKLKDVISMNASEfsevqiaLNEAKLSEEKVKSECHRVQEEnarlkkkKEQLQQEIEDWSKLHA 1375
Cdd:TIGR02169 290 LrVKEK--IGELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1376 ELSEQIKSFEKSQKDLEVALTHKDDninalTNCITQLNLLECESESEGQNKGGNDSdeLANGEVGGDRNEKMKNQIKQM- 1454
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDK-----EFAETRDELKDYREKLEKLKREINEL--KRELDRLQEELQRLSEELADLn 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433638 1455 MDVSRTQTAISVVEEDLKLLQLKLRAS----VSTKCNLEDQVKKLEDDRNSLQAakagLEDECKTLRQKVEIL 1523
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEA 495
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1645-1920 |
1.06e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.17 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1645 PMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKP 1724
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1725 SPSDPGSGTATMMN---------SSSRGSSPTRVLDEGKQTVLQEPEV--------PSVPSITSLAeRPVAVNMAPKgPP 1787
Cdd:PHA03247 2634 AANEPDPHPPPTVPpperprddpAPGRVSRPRRARRLGRAAQASSPPQrprrraarPTVGSLTSLA-DPPPPPPTPE-PA 2711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1788 PFPGVPLMSTPMgGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPlglREFAPGVPPgRRDLPLHPRGFLPGHAPFR 1867
Cdd:PHA03247 2712 PHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPATPGGPARPA---RPPTTAGPP-APAPPAAPAAGPPRRLTRP 2786
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1022433638 1868 PLGSLGPREYFIPGTRLPPPTHGPQEYPPPPAVRDLLPSGSrDEPPPASQSTS 1920
Cdd:PHA03247 2787 AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP-LPPPTSAQPTA 2838
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1225-1634 |
1.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1225 KENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEilddtAKNLRVMLESEREQNVKNQdli 1304
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE-----AAEKKKEEAKKKADAAKKK--- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1305 SENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEE-KVKSECHRVQEE---NARLKKKKEQLQQEIEDWSKLH--AELS 1378
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKAEeaKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1379 EQIKSFEKSQKDLEVALTHKDDNINALTnciTQLNLLECESESEGQNKggndSDELANGEVGGDRNEKMKNQIKQMMDVS 1458
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1459 RTQTAISVVEEDLKLLQLKlRASVSTKCnleDQVKKLEDDRNSL--------QAAKAGLEDECKTLRQKVEI-LNELYQQ 1529
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELK-KAEEKKKA---EEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEKKMkAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1530 KEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTykrriEEMEDELQKTERSFKnqiATHEKKAHENWLKARAAE 1609
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK-----AEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDE 1687
|
410 420
....*....|....*....|....*
gi 1022433638 1610 RAIAEEKREAANLRHKLLELTQKMA 1634
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1214-1583 |
2.05e-06 |
|
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: 53.05 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESE 1293
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISENKKSIEKLKDVISMNASEFSEV---QIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 1370
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1371 SKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQ 1450
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1451 IKQ--MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQ 1528
Cdd:pfam02463 905 ESQklNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1022433638 1529 QKEMALQKKLSQEEyerqerehRLSAADEKAVSAAEEVKTyKRRIEEMEDELQKT 1583
Cdd:pfam02463 985 EKEERYNKDELEKE--------RLEEEKKKLIRAIIEETC-QRLKEFLELFVSIN 1030
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1635-1915 |
2.06e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 53.23 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1635 MLQEEPVIVKPMPGKPNTQNPPRRGPlSQNGSFGPSPvsgGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSvdGPLPHP 1714
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGT-TQAATAGPTP---SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ--TPTLHP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1715 RwsaeasGKPSPSDPgsgtatmMNSSSRGSSPTRVLDEGKQTVLQEPEVPSVPSitSLAERPVAVNMaPKGPPPFPGVPL 1794
Cdd:pfam03154 240 Q------RLPSPHPP-------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPH--SLQTGPSHMQH-PVPPQPFPLTPQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1795 MSTPMGGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrEFAPGVPPGRRDLPLHPRGFLPG-HAPFRPLGSLG 1873
Cdd:pfam03154 304 SSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---PPAPLSMPHIKPPPTTPIPQLPNpQSHKHPPHLSG 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1022433638 1874 PREYFIPGTRLPPP---------THGPQEYPPPPAvrDLLPSGSRDEPPPA 1915
Cdd:pfam03154 381 PSPFQMNSNLPPPPalkplsslsTHHPPSAHPPPL--QLMPQSQQLPPPPA 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1215-1585 |
3.00e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1215 QISEKLKTIMKENTELVQKLSNYEqKIKESKKHVQETRKQNMILSDEaiKYKDKIKTLEKNQEILDDTAKNLRvmlesER 1294
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT-----AR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1295 EQNVKNQdlISENKKSIEKLKD------VISMNASEFSEVQIaLNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIE 1368
Cdd:PRK03918 414 IGELKKE--IKELKKAIEELKKakgkcpVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1369 DWSKLHA--ELSEQIKSFEKSQKDLevalthkddNINALTNCITQLNLLECES-ESEGQNKGGNDSDELANG-------- 1437
Cdd:PRK03918 491 KESELIKlkELAEQLKELEEKLKKY---------NLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEElkkklael 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1438 -EVGGDRNEKMKNQIKQMMdvSRTQTAISVVEEDLKLLQ------LKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE 1510
Cdd:PRK03918 562 eKKLDELEEELAELLKELE--ELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022433638 1511 DECKTLRQKVEILNELYQQKEMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 1585
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1213-1585 |
4.40e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEKlktimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KYKDK 1268
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1269 IKTLEKNQEILDDTAKNLRVMLESEREQnvkNQDLISE---NKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSE 1345
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEE---RDDLLAEaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1346 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNLLECESESEGQN 1425
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1426 KGGNDSDElANGEVGGDRNEKMKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQlKLRASVSTkcnLEDQVKKLE 1496
Cdd:PRK02224 421 RDELRERE-AELEATLRTARERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1497 DDRNSLQAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSAAEEV 1566
Cdd:PRK02224 496 ERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEAREEV 574
|
410
....*....|....*....
gi 1022433638 1567 KTYKRRIEEMEDELQKTER 1585
Cdd:PRK02224 575 AELNSKLAELKERIESLER 593
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1644-1920 |
4.72e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.10 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1644 KPMPGKPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTVEPPVRPLSATLNRRDMPRSefgsVDGPLPHPRWSAEASGK 1723
Cdd:PHA03307 83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRP----VGSPGPPPAASPPAAGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1724 PsPSDPGSGTAtmmnsSSRGSSPtrvldegkqtVLQEPEVPSVPSITSLAERPVAVN-MAPKGPPPFPGVPLM-----ST 1797
Cdd:PHA03307 158 S-PAAVASDAA-----SSRQAAL----------PLSSPEETARAPSSPPAEPPPSTPpAAASPRPPRRSSPISasassPA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1798 PMGGPVPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGlrefaPGVPPGRRDLPLHPRGFLPGHAPFRPLGSLGPREy 1877
Cdd:PHA03307 222 PAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPA-----PITLPTRIWEASGWNGPSSRPGPASSSSSPRERS- 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1878 fipGTRLPPPTHGPQEYPPPPAVRDL-------LPSGSRDEPPPASQSTS 1920
Cdd:PHA03307 296 ---PSPSPSSPGSGPAPSSPRASSSSsssressSSSTSSSSESSRGAAVS 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1213-1404 |
6.68e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLES 1292
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1293 EreqNVknQDLISenkkSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 1372
Cdd:COG3883 112 E---SF--SDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|..
gi 1022433638 1373 LHAELSEQIKSFEKSQKDLEVALTHKDDNINA 1404
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1225-1412 |
9.16e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1225 KENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLI 1304
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1305 SENKKSIEKLKDVISM-----------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKL 1373
Cdd:COG4942 100 EAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1022433638 1374 HAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQL 1412
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1585 |
1.07e-05 |
|
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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1350 QEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLN--LLECESESEGQNKg 1427
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaeLAELEKEIAELRA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1428 gndsdELAngevggDRNEKMKNQIKQMMDVSRT--------QTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDR 1499
Cdd:COG4942 98 -----ELE------AQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1500 NSLQAAKAGLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 1579
Cdd:COG4942 160 AELAALRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*.
gi 1022433638 1580 LQKTER 1585
Cdd:COG4942 236 AAAAAE 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1218-1632 |
1.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1218 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILD-DTAKNLRVMLESEREQ 1296
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1297 NVKNQDLiseNKKSIEKLKDVISMNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLKK-KKEQLQQEIEDWSKLH- 1374
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAE----AARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEd 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1375 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE-CESESEGQNKGGNDSDELANGEvggdrNEKMKNQIKQ 1453
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAE-----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1454 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQVKKLEDDRNSLQAAKAGLEDECKTL----------------- 1516
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaekkkeea 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1517 RQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEK 1596
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
410 420 430
....*....|....*....|....*....|....*.
gi 1022433638 1597 KAHENWLKARAAERAIAEEKREAANLRhKLLELTQK 1632
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKK 1491
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1295-1532 |
1.67e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1295 EQNVKNQDLISENKKSIeklkDVISMNASEFSEvQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIEDWSKLH 1374
Cdd:PHA02562 167 EMDKLNKDKIRELNQQI----QTLDMKIDHIQQ-QIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1375 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLE-----------CESE-SEGQNKGGNDSDELANGEVGGD 1442
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQiSEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1443 RNEKMKNQIKQMMDVSRTQTaisvveEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 1522
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|
gi 1022433638 1523 LNELYQQKEM 1532
Cdd:PHA02562 391 IVKTKSELVK 400
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1203-1538 |
4.05e-05 |
|
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: 48.42 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1203 VVKDRVYQVTEQQISEKLKTIMKENTELVQKLS-NYEQKIKESKKHVQETRKQNMILSDEAIKYKdkiKTLEKNQEILDD 1281
Cdd:COG5185 192 ISELKKAEPSGTVNSIKESETGNLGSESTLLEKaKEIINIEEALKGFQDPESELEDLAQTSDKLE---KLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1282 TAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNAS-EFSEVQIALNEAKLSEEKVKSEchrVQEENARLKKKK 1360
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRE---TETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1361 EQLQQEI-EDWSKLHAELSE--QIKSFEKSQKDLEVALTH----KDDNINALTNCITQLNLLEcesESEGQNKGGNDSD- 1432
Cdd:COG5185 346 EQGQESLtENLEAIKEEIENivGEVELSKSSEELDSFKDTiestKESLDEIPQNQRGYAQEIL---ATLEDTLKAADRQi 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1433 ELANGEVGGDR--NEKMKNQIKQMMDvSRTQTAISVVEEDLKLLQLKLRASVSTkcnLEDQVKKLEDDRNSLQAAKAGLE 1510
Cdd:COG5185 423 EELQRQIEQATssNEEVSKLLNELIS-ELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLK 498
|
330 340
....*....|....*....|....*...
gi 1022433638 1511 DECKTLRQKVEILNELYQQKEMALQKKL 1538
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1317-1565 |
5.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1317 VISMNASEFSEVQIALNEAKLSEekvksechrVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 1396
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSE---------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1397 HKDDNINALTNCITQLNlleceseSEGQNKGGNDS--DELANGEVGGDRNEKMkNQIKQMMDvsRTQTAISVVEEDLKLL 1474
Cdd:COG3883 76 EAEAEIEERREELGERA-------RALYRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1475 QLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 1554
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|.
gi 1022433638 1555 ADEKAVSAAEE 1565
Cdd:COG3883 226 AAAAAAAAAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1214-1386 |
5.86e-05 |
|
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: 46.46 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQeildDTAKNLRVMLESE 1293
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL----GNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REqnvknqdlISENKKSIEKLKDVIS--MNASEFSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEdws 1371
Cdd:COG1579 96 KE--------IESLKRRISDLEDEILelMERIEELEEELAELEAELAELEA-----ELEEKKAELDEELAELEAELE--- 159
|
170
....*....|....*
gi 1022433638 1372 KLHAELSEQIKSFEK 1386
Cdd:COG1579 160 ELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1447-1600 |
7.63e-05 |
|
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: 46.07 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1447 MKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 1526
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1527 ---YQQ--------KEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 1594
Cdd:COG1579 75 ikkYEEqlgnvrnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*.
gi 1022433638 1595 EKKAHE 1600
Cdd:COG1579 155 EAELEE 160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1313-1579 |
7.83e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1313 KLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE 1392
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1393 VALTHKDDNINALTNCITQLnllecesesegQNKGGNDSDELANGE--VGGDRNEKMKNQI-KQMMDVSRTQTAISVVEE 1469
Cdd:TIGR02169 751 QEIENVKSELKELEARIEEL-----------EEDLHKLEEALNDLEarLSHSRIPEIQAELsKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1470 DLKLLQLKLRASVSTKCNLEDQVKKLEDDRNS-------LQAAKAGLEDECKTLRQKVEILNELYQ---------QKEM- 1532
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLr 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1022433638 1533 ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 1579
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1214-1557 |
8.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTimKENTELVQKLSNYEQKIKESKKHVQETrkqnmilsdeaikyKDKIKTLEKNQEILDDTAKNLRVMLESE 1293
Cdd:COG1196 216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEEL--------------EAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISENKKSIEKLkdvismnasefsEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEIEDWSKL 1373
Cdd:COG1196 280 ELELEEAQAEEYELLAELARL------------EQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1374 HAELSEQIKSFEKSQKDLEVALTHKddninaltncitQLNLLECESESEGQNKggndsdelangevggDRNEKMKNQIKQ 1453
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEA------------EAELAEAEEELEELAE---------------ELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1454 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMA 1533
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340
....*....|....*....|....
gi 1022433638 1534 LQKKLSQEEYERQEREHRLSAADE 1557
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEAD 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1210-1506 |
9.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1210 QVTEQQISEKLKTIMKENTELVQKLSNYEQ-KIK-ESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLR 1287
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1288 VMLESEREQNVKNQDLISENKKSIEKL-------KDVISMNASEFSEVQIAlNEAKLSEEKVKSECHRVQEENARLKKKK 1360
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeaKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1361 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANgevg 1440
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN---- 1822
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 1441 gDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTK-CNLEDQVKKLEDDRNSLQAAK 1506
Cdd:PTZ00121 1823 -DSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKeADFNKEKDLKEDDEEEIEEAD 1888
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1647-1921 |
1.02e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1647 PGKPNTQNPPR-RGPLSQNGsfGPSPVSGGECSPPlTVEPPVRPLSATLNrrDMPRSEfgsvdgPLpHPR---W------ 1716
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGGPPDPD-APPAPSRLAPAILP--DEPVGE------PV-HPRmltWirglee 2542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1717 --SAEASGKPSPSDPGSGTATmmnsSSRGSSPTRvldegkqtvlQEPEvPSVPSITSLAERPVA--------VNMAPKGP 1786
Cdd:PHA03247 2543 laSDDAGDPPPPLPPAAPPAA----PDRSVPPPR----------PAPR-PSEPAVTSRARRPDAppqsarprAPVDDRGD 2607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1787 PPFPGVPLMSTPMGGPvpppirygpppqlcgpfgPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGHA-- 1864
Cdd:PHA03247 2608 PRGPAPPSPLPPDTHA------------------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRArr 2669
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 1865 PFRPLGSL----GPREYFIPGTRLP------PPTHGPQEYPPPPAVRDLLPSgsrdepPPASQSTSQ 1921
Cdd:PHA03247 2670 LGRAAQASsppqRPRRRAARPTVGSltsladPPPPPPTPEPAPHALVSATPL------PPGPAAARQ 2730
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1213-1628 |
1.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1213 EQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRK-QNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLE 1291
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 SEREQNVKNqdlISENKKSIEKLKDVISMNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLK--KKKEQLQQEIED 1369
Cdd:PTZ00121 1169 ARKAEDAKK---AEAARKAEEVRKAEELRKAEDARKAE----AARKAEEERKAEEARKAEDAKKAEavKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1370 wsklhAELSEQIKSFEKSQKDLEVALTHKDDNINALtncitqlnllecesESEGQNKggndSDELANGEvggdrNEKMKN 1449
Cdd:PTZ00121 1242 -----AKKAEEERNNEEIRKFEEARMAHFARRQAAI--------------KAEEARK----ADELKKAE-----EKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1450 QIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKveilnelyQQ 1529
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--------EE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1530 KEMALQKKLSQEEYerqerehRLSAADEKA--VSAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHEnwLKARA 1607
Cdd:PTZ00121 1365 KAEAAEKKKEEAKK-------KADAAKKKAeeKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEE--KKKAD 1434
|
410 420
....*....|....*....|.
gi 1022433638 1608 AERAIAEEKREAANLRHKLLE 1628
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEE 1455
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1207-1392 |
1.09e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1207 RVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLE-KNQEILDDTAKN 1285
Cdd:COG5022 853 RSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLEFKTELIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1286 LRVMLES------------EREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKlseeKVKSECHRVQEEN 1353
Cdd:COG5022 933 LKKLLNNidleegpsieyvKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK----NFKKELAELSKQY 1008
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1022433638 1354 ARLKKKKEQLQQEIEDWSKLHAELS--EQIKSFEKSQKDLE 1392
Cdd:COG5022 1009 GALQESTKQLKELPVEVAELQSASKiiSSESTELSILKPLQ 1049
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1215-1598 |
1.16e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1215 QISEKLKTIMKENTELVQKLSNYE--------------------------------QKIKESKKHVQETRKQNMILSDEA 1262
Cdd:TIGR01612 1366 EVKEYTKEIEENNKNIKDELDKSEklikkikddinleeckskiestlddkdideciKKIKELKNHILSEESNIDTYFKNA 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1263 IKYKDKIKTLEKNQEILDDTAKNLrvmLESEREQNVKNQDL----ISENKKSIEKLKDVISMNASEFSEVQIALNEAKLS 1338
Cdd:TIGR01612 1446 DENNENVLLLFKNIEMADNKSQHI---LKIKKDNATNDHDFnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKD 1522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1339 EEKVKSECHRVQEEN--ARLKKKKEQLQQEIEDWSK---LHAELSEQ-IKSFEKSQKDLEVALTHKDDNINALTNCITQL 1412
Cdd:TIGR01612 1523 VTELLNKYSALAIKNkfAKTKKDSEIIIKEIKDAHKkfiLEAEKSEQkIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSL 1602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1413 NLLEcesesegqNKGGNDSDELANGEVGGDRNEKMKNQIKQmMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQV 1492
Cdd:TIGR01612 1603 ENFE--------NKFLKISDIKKKINDCLKETESIEKKISS-FSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKK 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1493 KKLEDDRNSLQAAKAGLEDECKTLRQK-VEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKR 1571
Cdd:TIGR01612 1674 KELDELDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNT 1753
|
410 420
....*....|....*....|....*..
gi 1022433638 1572 RIEEMEDELQKTERSFKNQIATHEKKA 1598
Cdd:TIGR01612 1754 EIGDIYEEFIELYNIIAGCLETVSKEP 1780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1214-1392 |
1.19e-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: 47.37 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDdtaKNLRVMLESE 1293
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEEL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISEN---KKSIEKLKdvismnaSEFSEVQIALNEAKLSEEKVKsecHRVQEENARLKKKKEQLqQEIEDW 1370
Cdd:TIGR02169 871 EELEAALRDLESRLgdlKKERDELE-------AQLRELERKIEELEAQIEKKR---KRLSELKAKLEALEEEL-SEIEDP 939
|
170 180
....*....|....*....|..
gi 1022433638 1371 SKLHAELSEQIKSFEKSQKDLE 1392
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQ 961
|
|
| SH3_p40phox |
cd11869 |
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil ... |
49-105 |
1.36e-04 |
|
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil cytosol factor 4 (NCF-4), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. It contains an N-terminal PX domain, a central SH3 domain, and a C-terminal PB1 domain that interacts with p67phox. The SH3 domain of p40phox binds to canonical polyproline and noncanonical motifs at the C-terminus of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212802 Cd Length: 54 Bit Score: 41.33 E-value: 1.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 49 RGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWPEvwaGSVGRTFGYFPKDLIQVV 105
Cdd:cd11869 1 RAEALFDFTGNSKLELNFKAGDVIFLLSRVNKDWLE---GTVRGATGIFPLSFVKII 54
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1270-1406 |
1.76e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1270 KTLEKNQEILDDTAKnlRVMLESEREQNVKNQDLISENKKSIEKLKdvismnaSEF-SEVQIALNEAKLSEEKVKSECHR 1348
Cdd:PRK12704 27 KIAEAKIKEAEEEAK--RILEEAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022433638 1349 VQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkdDNINALT 1406
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1208-1390 |
1.97e-04 |
|
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).
Pssm-ID: 439149 [Multi-domain] Cd Length: 224 Bit Score: 44.71 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1208 VYQVTEQQIseklktIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK--------YKDKIKTLEKNQEIL 1279
Cdd:cd21116 15 VTAILNQPN------INLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgynntfqsYYPDLIELADNLIKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1280 DDTAKN-LRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 1358
Cdd:cd21116 89 DQGAKQqLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAID 168
|
170 180 190
....*....|....*....|....*....|..
gi 1022433638 1359 KKEQLQQeieDWSKLHAELSEQIKSFEKSQKD 1390
Cdd:cd21116 169 ALEKLSN---DWQTLDSDIKELITDLEDAESS 197
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1724-1921 |
1.99e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.68 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1724 PSPSDpgsgtatmmNSSSRGSSPTRVLDEGKQTVLQEPEVPSVPSITSLAERPVAVNMAPkgPPPFPGVPLMSTPmggPV 1803
Cdd:pfam03154 149 PSPQD---------NESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP--TPSAPSVPPQGSP---AT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1804 PPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLpgHAPFRPLG---SLGPREYFIP 1880
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSL--HGQMPPMPhslQTGPSHMQHP 292
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1022433638 1881 GTRLP---PPTHGPQEYPPPPAVRDLLPSGSRDE-PPPASQSTSQ 1921
Cdd:pfam03154 293 VPPQPfplTPQSSQSQVPPGPSPAAPGQSQQRIHtPPSQSQLQSQ 337
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1204-1537 |
2.00e-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: 46.25 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1204 VKDRVYQVTEQQISEK--LKTIMKENTELV-QKLSNYE------QKIKESKKHVQETRKQNMIL---SDEAIKYKDKIKT 1271
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEhyLKEVEDLKTELEkEKLKNIEltahcdKLLLENKELTQEASDMTLELkkhQEDIINCKKQEER 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1272 LEKNQEILDDTAKNLRVMLESEREQNVKNQDlisENKKSIEKlkdviSMNASEFSEVQIALNEAKLSEEKVKSECHRVQE 1351
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGD---EVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1352 ENArlKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNciTQLNLLECESESEGQNKGgnds 1431
Cdd:pfam05483 604 ENK--NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID--NYQKEIEDKKISEEKLLE---- 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1432 dELANGEVGGDRNEKMKNQIKQ-----------MMDVSRTQTAISVVEED--LKLLQLKLRASVSTKCNLEDQVKKLedd 1498
Cdd:pfam05483 676 -EVEKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI--- 751
|
330 340 350
....*....|....*....|....*....|....*....
gi 1022433638 1499 RNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQKK 1537
Cdd:pfam05483 752 KAELLSLKKQLEIE----KEEKEKLKMEAKENTAILKDK 786
|
|
| SH3 |
smart00326 |
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
48-103 |
2.10e-04 |
|
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.
Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 40.98 E-value: 2.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 48 YRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWpevWAGSVGR-TFGYFPKDLIQ 103
Cdd:smart00326 3 PQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGW---WKGRLGRgKEGLFPSNYVE 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1238-1623 |
2.18e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1238 EQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNqdliSENKKSIEKLKDV 1317
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1318 ismnasefSEVQIAlNEAKLSEEKVKSECHRVQEENARlkkKKEQLQQEIEDWSKLHAELSeqiKSFEKSQKDLEVAlth 1397
Cdd:PTZ00121 1287 --------EEKKKA-DEAKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAA--- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1398 kddninaltncitqlnllecESESEGQNKGGNDSDELANGEVGGDRNEKMKNQI--KQMMDVSRTQTAISVVEEDLKLLQ 1475
Cdd:PTZ00121 1349 --------------------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1476 lKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLE-DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 1554
Cdd:PTZ00121 1409 -ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1022433638 1555 ADEKAVSAAEEVKTYKRRIEEME--DELQKTERSFKnqiATHEKKAHEnwlKARAAERAIAEEKREAANLR 1623
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKK---ADEAKKAEE---AKKADEAKKAEEKKKADELK 1552
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1292-1584 |
2.41e-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: 46.21 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 SEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ-------LQ 1364
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedlssLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1365 QEIE-------DWSKLHAELSEQIKSFEKSQKDLEVALTH-KDDNINALTNCI--------TQLNLLECESESEGQNKgg 1428
Cdd:TIGR02169 751 QEIEnvkselkELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLeeevsrieARLREIEQKLNRLTLEK-- 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1429 ndsdELANGEVGG--DRNEKMKNQIKQMMD-VSRTQTAISVVEEDLKLLQLKLRasvstkcNLEDQVKKLEDDRNSLQAA 1505
Cdd:TIGR02169 829 ----EYLEKEIQElqEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALR-------DLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022433638 1506 KAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 1584
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-----DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1214-1585 |
2.74e-04 |
|
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: 45.94 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDtaknlrvm 1289
Cdd:pfam01576 74 EEILHELESRLEEEEERSQQLQNekkkMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED-------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1290 lesereqnvKNQDLISENKKSIEKLKDVISmNASEFSEVQIALNEAKLSEEKVKS--ECHRVQEENAR--LKKKKEQLQQ 1365
Cdd:pfam01576 146 ---------QNSKLSKERKLLEERISEFTS-NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRqeLEKAKRKLEG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1366 EIEDWSKLHAELSEQIK----SFEKSQKDLEVALTHKDDNINALTNCITQLNLLEC---------ESESEGQNKGGND-- 1430
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELEAqiselqedlESERAARNKAEKQrr 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1431 --SDEL---------------ANGEVGGDRNEKMKNQIKQMMDVSRT---------QTAISVVEEDLKLLQLKLRASVS- 1483
Cdd:pfam01576 296 dlGEELealkteledtldttaAQQELRSKREQEVTELKKALEEETRSheaqlqemrQKHTQALEELTEQLEQAKRNKANl 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1484 --TKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMA---LQKKLSQEEYERQEREHRLSAADEK 1558
Cdd:pfam01576 376 ekAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGK 455
|
410 420
....*....|....*....|....*..
gi 1022433638 1559 AVSAAEEVKTYKRRIEEMEDELQKTER 1585
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETR 482
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1637-1915 |
3.33e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1637 QEEPVIVKPMPGKPNTqnPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFG-SVDGPLPHPR 1715
Cdd:PHA03307 190 PAEPPPSTPPAAASPR--PPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlPRPAPITLPT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1716 WSAEA-----------SGKPSPSDPGSGTATMMNSSSRGSSPTRVLDEGKQtVLQEPEVPSVPSITSLAERPVAVNM-AP 1783
Cdd:PHA03307 268 RIWEAsgwngpssrpgPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS-SSSRESSSSSTSSSSESSRGAAVSPgPS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1784 KGPPPFPGVPlmSTPMGGPvpppirygpppqlcgpfgprplPPPFGPGMRPPLGLREFAPGVPPGRRDLPLHPRGFLPGH 1863
Cdd:PHA03307 347 PSRSPSPSRP--PPPADPS----------------------SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRD 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 1864 APFRplgslgpreyfIPGTRLP--PPTHGPQEYPPPPAVRDLLPSGS---RDEPPPA 1915
Cdd:PHA03307 403 ATGR-----------FPAGRPRpsPLDAGAASGAFYARYPLLTPSGEpwpGSPPPPP 448
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1185-1319 |
3.75e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1185 TAFLGIASFAI-------FLWRTVL-VVKDRvyqvtEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 1256
Cdd:cd06503 1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433638 1257 ILsDEAIKYKDKIKtleknQEILDDTAKnlrvmlESEREQNVKNQDLISENKKSIEKLKDVIS 1319
Cdd:cd06503 70 II-EEARKEAEKIK-----EEILAEAKE------EAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1470-1639 |
3.85e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1470 DLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELY---QQKEMALQKKLSQEEYERQ 1546
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1547 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 1623
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170
....*....|....*.
gi 1022433638 1624 HKLLELTQKMAMLQEE 1639
Cdd:COG1196 386 EELLEALRAAAELAAQ 401
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1212-1394 |
4.42e-04 |
|
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: 45.12 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1212 TEQQISEKLKTIMKENTELVQKLsnyeqkikesKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLE 1291
Cdd:pfam05557 370 TMSNYSPQLLERIEEAEDMTQKM----------QAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 SEREQNV--KNQDLISENKKsIEKLKDVISM-----------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 1358
Cdd:pfam05557 440 KEEVDSLrrKLETLELERQR-LREQKNELEMelerrclqgdyDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKR 518
|
170 180 190
....*....|....*....|....*....|....*..
gi 1022433638 1359 KKEQLQQEIEDWSKLHAELSE-QIKSFEKSQKDLEVA 1394
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESA 555
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1210-1597 |
4.48e-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: 45.48 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1210 QVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETR-KQNMI-----LSDEAIKY----KDKI---------- 1269
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRdKANQLeektkLQDENLKEliekKDHLtkeledikms 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1270 --------KTLEKNQEILDDTAKNLRVMLESEREQNVKN------------------QDLISENKKSIEKLKD---VISM 1320
Cdd:pfam05483 305 lqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAkaahsfvvtefeattcslEELLRTEQQRLEKNEDqlkIITM 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1321 ----NASEFSEVQIALNEAKLSEEKVKsechRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 1396
Cdd:pfam05483 385 elqkKSSELEEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1397 HKDDNINALTNCITQLNL-LECESESEGQNKGGNDSDELANGEV---GGDRNEKMKNQIKQMMDVSRTQTAISVVEEDLK 1472
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTeLEKEKLKNIELTAHCDKLLLENKELtqeASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1473 LLQLKLRASVST------------KCNL---EDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEILN---ELYQQKEMAL 1534
Cdd:pfam05483 541 EKEMNLRDELESvreefiqkgdevKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNkniEELHQENKAL 620
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1022433638 1535 QKKlsqeeyerqerehrlSAADEKAVSAaeevktYKRRIEEMEDELQKTERSFKNQIATHEKK 1597
Cdd:pfam05483 621 KKK---------------GSAENKQLNA------YEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1630-1931 |
4.68e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1630 TQKMAMLQEEPVIVKPMPGKPNTQNPPRRGPLSQNGSFGPSPvSGGECSPPLTVEPPVRPLS-----ATLNR-------- 1696
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG-SPATSQPPNQTQSTAAPHTliqqtPTLHPqrlpsphp 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1697 --RDMPRSEFGSVDGPLPHPRWSAEASGKPSPSDPGSGTATM-----------MNSSSRGSSP----TRVLDEGKQTVLQ 1759
Cdd:pfam03154 248 plQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMqhpvppqpfplTPQSSQSQVPpgpsPAAPGQSQQRIHT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1760 EPEVPSVPSITSLAERPVA---VNMAPKGPPPFPGVPLMSTPMGGPVPPPIRYGPPPQLcgpfgprplpppfGPGMRPPL 1836
Cdd:pfam03154 328 PPSQSQLQSQQPPREQPLPpapLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQM-------------NSNLPPPP 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1837 GLR---EFAPGVPPGRRDLPLH--PRGFLPGHAPFRPLGSLGPREYFIPGTRLPPPTHGPQEYPPPP-AVRDLLPSGSRD 1910
Cdd:pfam03154 395 ALKplsSLSTHHPPSAHPPPLQlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPfPQHPFVPGGPPP 474
|
330 340
....*....|....*....|.
gi 1022433638 1911 EPPPASQSTSQDCSQALKQSP 1931
Cdd:pfam03154 475 ITPPSGPPTSTSSAMPGIQPP 495
|
|
| SH3_Sdc25 |
cd11883 |
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ... |
52-98 |
4.82e-04 |
|
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212816 Cd Length: 55 Bit Score: 39.96 E-value: 4.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1022433638 52 ALEDFTGPDCRFVNFKKGDPVYVYYKLARGWpevWAGSVGRTF-----GYFP 98
Cdd:cd11883 4 ALYDFTPKSKNQLSFKAGDIIYVLNKDPSGW---WDGVIISSSgkvkrGWFP 52
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1191-1591 |
5.35e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1191 ASFAIFLWRTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESK---KHVQETRKQNMILSDEAIKYKD 1267
Cdd:COG5185 148 DIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGtvnSIKESETGNLGSESTLLEKAKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1268 KIKTLEKNQEILDDtaknlrvmlESEREQNVKNQDLISENKKSIEKLKDvismnasefsevqialneAKLSEEKVKSEch 1347
Cdd:COG5185 228 IINIEEALKGFQDP---------ESELEDLAQTSDKLEKLVEQNTDLRL------------------EKLGENAESSK-- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1348 RVQEENARLKKKKEQLQQEIE------DWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCITQLNllecESES 1421
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeytksiDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQ----ESLT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1422 EGQNKGGNDSDELAnGEVGGDRNEKMKNQIKQMMDVSRT--------------------QTAISVVEEDLKLLQLKLRAS 1481
Cdd:COG5185 354 ENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQIEELQRQIEQA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1482 VSTKCNLEDQVKKLED-----DRNSLQAAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRL 1552
Cdd:COG5185 433 TSSNEEVSKLLNELISelnkvMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQL 512
|
410 420 430
....*....|....*....|....*....|....*....
gi 1022433638 1553 SAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 1591
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1270-1603 |
5.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1270 KTLEKNQEILDDTAKNLRVmLESEREQNvknQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRV 1349
Cdd:COG4372 31 EQLRKALFELDKLQEELEQ-LREELEQA---REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1350 QEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGN 1429
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1430 DSDELANGEVggDRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGL 1509
Cdd:COG4372 187 ELLKEANRNA--EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1510 EDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKN 1589
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330
....*....|....
gi 1022433638 1590 QIATHEKKAHENWL 1603
Cdd:COG4372 345 LLLVGLLDNDVLEL 358
|
|
| SH3 |
cd00174 |
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
52-98 |
5.58e-04 |
|
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.
Pssm-ID: 212690 [Multi-domain] Cd Length: 51 Bit Score: 39.37 E-value: 5.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1022433638 52 ALEDFTGPDCRFVNFKKGDPVYVYYKLARGWpevWAGSV-GRTFGYFP 98
Cdd:cd00174 4 ALYDYEAQDDDELSFKKGDIITVLEKDDDGW---WEGELnGGREGLFP 48
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
1727-1926 |
6.64e-04 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 44.76 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1727 SDPGSGTATMMNSSSRGSSPTRvldegkQTVLQEPEVPSVPSITSLAeRPVAV----NMAPKG----------PPPFPGV 1792
Cdd:pfam15685 5 SEPSAGAGSQKEQALDHASDSR------RTSLVEPEVTPSSPAMRLA-QGLGVwfpgSSAPPGllvppepqasPSPLPLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1793 PLMSTPMGGPVPPPIRYGPPPqlcGPFGPRPLPPPFGPGMRPPLGLRefapgVPPGRRDLPLHPRGflPGHAP-FRPLGS 1871
Cdd:pfam15685 78 LELPLPVTPPPEEAAAAAVST---APPPAVGSLLPAPSKWRKPTGTA-----VARIRGLLEASHRG--QGDPLsLRPLLP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1872 LGPREYF----IPGTRL-PPPTHGPQEYPPPPAVRDLLPSGSRDEPPPASQSTSQDCSQA 1926
Cdd:pfam15685 148 LLPRQLIekdpAPGAPApPPPTPLEPRKPPPLPPSDRQPPNRGITPALATSATSPTDSQA 207
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1233-1526 |
6.74e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1233 KLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEI---------------LDDTAKNLRV----MLESE 1293
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeckskiestlddkdIDECIKKIKElknhILSEE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNV--KNQDlisENKKSIEKLKDVISM--NASEF----------SEVQIALNEAKLSEEKVKSeCHRVQEENAR-LKK 1358
Cdd:TIGR01612 1436 SNIDTyfKNAD---ENNENVLLLFKNIEMadNKSQHilkikkdnatNDHDFNINELKEHIDKSKG-CKDEADKNAKaIEK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1359 KKEQLQQEIEDWSKLHAELSE-QIKS-FEKSQKDLEVALTHKDDNINALTncitqlnlLECESESEGQNKGGND----SD 1432
Cdd:TIGR01612 1512 NKELFEQYKKDVTELLNKYSAlAIKNkFAKTKKDSEIIIKEIKDAHKKFI--------LEAEKSEQKIKEIKKEkfriED 1583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1433 ELANGEVGG----DRNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRA-SVSTKcnlEDQVKKLEDDRNSLQAAKA 1507
Cdd:TIGR01612 1584 DAAKNDKSNkaaiDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQ---DTELKENGDNLNSLQEFLE 1660
|
330
....*....|....*....
gi 1022433638 1508 GLEDECKTLRQKVEILNEL 1526
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELDEL 1679
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1241-1531 |
7.09e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1241 IKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVI-- 1318
Cdd:pfam05911 481 IRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDFVeg 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1319 -SMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQqEIEDWSKLH-------AELSEQIKSFEKSQKD 1390
Cdd:pfam05911 561 lSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKV 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1391 --LEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAIS--- 1465
Cdd:pfam05911 640 tlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlq 719
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1022433638 1466 VVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL-NELYQQKE 1531
Cdd:pfam05911 720 ESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALeVELEEEKN 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1264-1639 |
7.58e-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: 44.67 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1264 KYKDKIKTLEKNQEILD---DTAKNLRVMLESEREQNVKNQDLISENKKSieklkdvismnasEFSEVQIALNEAKLSEE 1340
Cdd:TIGR02169 174 KALEELEEVEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKREY-------------EGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1341 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKsfeksqkdlevALThkDDNINALTnciTQLNLLECESE 1420
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK-----------DLG--EEEQLRVK---EKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1421 SegqnkgGNDSDELANgevggDRNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDR 1499
Cdd:TIGR02169 305 S------LERSIAEKE-----RELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1500 NSLQAAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKtykrRIEEMEDE 1579
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA----GIEAKINE 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1580 LQKTERSFKNQIATHEKKAHENwlkaraaERAIAEEKREAANLRHKLLELTQKMAMLQEE 1639
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQL-------AADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1195-1384 |
8.92e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1195 IFLWRTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNyEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEK 1274
Cdd:PRK12705 17 LLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-ELLLRERNQQRQEARREREELQREEERLVQKEEQLDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1275 NQEILDDTAKNLrvmLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSecHRVQEENA 1354
Cdd:PRK12705 96 RAEKLDNLENQL---EEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQR--VKKIEEEA 170
|
170 180 190
....*....|....*....|....*....|
gi 1022433638 1355 RLKKKKEQLQQEIEDWSKLHAELSEQIKSF 1384
Cdd:PRK12705 171 DLEAERKAQNILAQAMQRIASETASDLSVS 200
|
|
| SH3_Nostrin |
cd11823 |
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ... |
49-104 |
9.73e-04 |
|
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212757 [Multi-domain] Cd Length: 53 Bit Score: 38.86 E-value: 9.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 49 RGEALEDFTGPDCRFVNFKKGDPVYVYYKLARGWpevWAGSVGRTFGYFPKDLIQV 104
Cdd:cd11823 1 RCKALYSYTANREDELSLQPGDIIEVHEKQDDGW---WLGELNGKKGIFPATYVEE 53
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1218-1395 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1218 EKLKTIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIK-YKDKIKTLEK--NQEIlddTAKNLRVMLESER 1294
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEE-------LGFESVEeLEERLKELEPfyNEYL---ELKDAEKELEREE 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1295 EQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNE---AKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIEd 1369
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyEELREEYLElsRELAGLRAELEELEKRREEIKKTLE- 697
|
170 180
....*....|....*....|....*.
gi 1022433638 1370 wsKLHAELsEQIKSFEKSQKDLEVAL 1395
Cdd:PRK03918 698 --KLKEEL-EEREKAKKELEKLEKAL 720
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1214-1448 |
1.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLrvmlese 1293
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1294 REQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 1372
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 1373 LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMK 1448
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1645-1905 |
1.13e-03 |
|
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.
Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 43.26 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1645 PMPGKPNTQNPPRrgPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLNRRDMprsefgSVDGPLPHPRWSAEASG-K 1723
Cdd:pfam15279 83 ASPASTRSESVSP--GPSSSASPSSSPTSSNSSKPLISVASSSKLLAPKPHEPPS------LPPPPLPPKKGRRHRPGlH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1724 PSPSDPGSGTATMMNSSSRGSSPTRVLDEGKQTVLQEPEV----PSVPSITSLAERPVAVNMAPK--GPPPFPGVPLMST 1797
Cdd:pfam15279 155 PPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAFMEPSSmpppFLRPPPSIPQPNSPLSNPMLPgiGPPPKPPRNLGPP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1798 PMGgpvpppirygpppqlcgpfgprplpppfgpGMRPPLGLREF-----APGVPPGRrdLPLHPRGFLP-GHAPFRPLgs 1871
Cdd:pfam15279 235 SNP------------------------------MHRPPFSPHHPpppptPPGPPPGL--PPPPPRGFTPpFGPPFPPV-- 280
|
250 260 270
....*....|....*....|....*....|....*...
gi 1022433638 1872 lgpreyfiPGTRLPPPT-HG-PQEYP--PPPAVrdLLP 1905
Cdd:pfam15279 281 --------NMMPNPPEMnFGlPSLAPlvPPVTV--LVP 308
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1690-1914 |
1.29e-03 |
|
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.
Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 43.26 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1690 LSATLNRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSdpgsgTATMMNSSSRGSSPTrvldegkQTVLQEPEVPSVPSI 1769
Cdd:pfam15279 75 LSDCRRKSASPASTRSESVSPGPSSSASPSSSPTSSNS-----SKPLISVASSSKLLA-------PKPHEPPSLPPPPLP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1770 TSLAERPVAVNMAPKGPPPfpGVPLMSTPMGGPVPPPIRYGPPPQLcgpfgprpLPPPFGPGMRPPLgLREFAPGVPPGR 1849
Cdd:pfam15279 143 PKKGRRHRPGLHPPLGRPP--GSPPMSMTPRGLLGKPQQHPPPSPL--------PAFMEPSSMPPPF-LRPPPSIPQPNS 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 1850 RDLPLHPRGFLPGHAPFRPLGSLGPREYFIP-GTRLPPPTHGPQEYPPPPavrdlLPSGSRDEPPP 1914
Cdd:pfam15279 212 PLSNPMLPGIGPPPKPPRNLGPPSNPMHRPPfSPHHPPPPPTPPGPPPGL-----PPPPPRGFTPP 272
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1685-1914 |
1.52e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 41.01 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1685 PPVRPLSAtlnrrdmprsefGSVDGPLPHPrwsaeASGKPSPSDPGSGtatmmnsssrGSSPTRVLdEGKQTVLQEPEVP 1764
Cdd:pfam06346 1 PPPPPLPG------------DSSTIPLPPG-----ACIPTPPPLPGGG----------GPPPPPPL-PGSAAIPPPPPLP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1765 SVPSITSLAERPVAVNMAPkgPPPFPGVPLMSTPmggpvpppirygpppqlcgpfgprplpppfgpgmrPPLglrEFAPG 1844
Cdd:pfam06346 53 GGTSIPPPPPLPGAASIPP--PPPLPGSTGIPPP-----------------------------------PPL---PGGAG 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1845 VPPGRRDLPLHPrGFLPGHAPFrPLGslgpreyfiPGTRLPPPTHGPQEYPPPPAVRDLLPsgsrdePPP 1914
Cdd:pfam06346 93 IPPPPPPLPGGA-GVPPPPPPL-PGG---------PGIPPPPPFPGGPGIPPPPPGMGMPP------PPP 145
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1220-1435 |
1.59e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1220 LKTIMKENTELVQ----KLSNYEQKIKESKKHVQETRKQNmilSDEAIKYKDKIKTLEKNQEilddTAKNLRVMLESERE 1295
Cdd:PHA02562 172 NKDKIRELNQQIQtldmKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAK----TIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1296 QNVKNQDLISENKKSIEKLKDVISMNASEFSEV---------------QIALNEAKLSEekvksechrVQEENARLKKKK 1360
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptctqQISEGPDRITK---------IKDKLKELQHSL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433638 1361 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEvalTHKDDninaLTNCITQLNLLECESEsEGQNKGGNDSDELA 1435
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKIS---TNKQS----LITLVDKAKKVKAAIE-ELQAEFVDNAEELA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1180-1538 |
2.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1180 KPVFITAFLGIASFAIFlwrtVLVVKDRVYQVTEQ-QI-SEKLKTIMKENTELVQKLSNYEQKIKeskkhvqetrkqnMI 1257
Cdd:COG3206 28 KWLILLVFLLVLALALL----YALLLPPVYEASATlLVePQSSDVLLSGLSSLSASDSPLETQIE-------------IL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1258 LSDE----AIK----YKDKIKTLEKNQEILDDTAKNLRVmlesereQNVKNQDLI-----SENKksiEKLKDVISMNASE 1324
Cdd:COG3206 91 KSRPvlerVVDklnlDEDPLGEEASREAAIERLRKNLTV-------EPVKGSNVIeisytSPDP---ELAAAVANALAEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1325 FSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEDWSKLH--AELSEQIKSFEKSQKDLEVALTHKDDNI 1402
Cdd:COG3206 161 YLEQNLELRREEARKALE-----FLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1403 NALTNCITQLnllecesESEGQNKGGNDSDELANGEVGGDRNE--KMKNQIKQMM--------DVSRTQTAISVVEEDLK 1472
Cdd:COG3206 236 AEAEARLAAL-------RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSarytpnhpDVIALRAQIAALRAQLQ 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1022433638 1473 LLQLKLRASvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKT----------LRQKVEILNELYQQkemaLQKKL 1538
Cdd:COG3206 309 QEAQRILAS------LEAELEALQAREASLQAQLAQLEARLAElpeleaelrrLEREVEVARELYES----LLQRL 374
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1217-1586 |
2.38e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1217 SEKLKTIM-KENTELVQ-KLSNYEQKIKESKKHVQETRKQ--NMILSDEAIK-YKDKIKTLEKNQEILDDTAKNLRVMLE 1291
Cdd:PTZ00440 832 DEELKQLLqKFPTEDENlNLKELEKEFNENNQIVDNIIKDieNMNKNINIIKtLNIAINRSNSNKQLVEHLLNNKIDLKN 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 --SEREQNVKNQDLISENKKSIekLKDVISmnaSEFSEVQIALNEAKLSEEKVKSEC------HRVQEENARLKKKKEQL 1363
Cdd:PTZ00440 912 klEQHMKIINTDNIIQKNEKLN--LLNNLN---KEKEKIEKQLSDTKINNLKMQIEKtleyydKSKENINGNDGTHLEKL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1364 QQEIEDWSKLHAELSEQIKSFEKSQKDL-EVALTHKDDNINALTNCITQLNLlecESESEGQNKGGNDSDELA------- 1435
Cdd:PTZ00440 987 DKEKDEWEHFKSEIDKLNVNYNILNKKIdDLIKKQHDDIIELIDKLIKEKGK---EIEEKVDQYISLLEKMKTklssfhf 1063
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1436 NGEVGGDRNEKMKNQIKQMMDVSRTQTAiSVVEEDLKLLQLKLRAS---VSTKCNLEDQVKKLEDDRNSLQAAKAGLEDE 1512
Cdd:PTZ00440 1064 NIDIKKYKNPKIKEEIKLLEEKVEALLK-KIDENKNKLIEIKNKSHehvVNADKEKNKQTEHYNKKKKSLEKIYKQMEKT 1142
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1022433638 1513 CKTLRQKVEILNELYQQKEMALQKKLsqeeYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERS 1586
Cdd:PTZ00440 1143 LKELENMNLEDITLNEVNEIEIEYER----ILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERND 1212
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1229-1392 |
2.44e-03 |
|
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: 41.83 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1229 ELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQ--NVKNQDLISE 1306
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1307 NKKSIEKLKDVISmnasEFSEVQIALNEaklseekvksechRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEK 1386
Cdd:COG1579 94 LQKEIESLKRRIS----DLEDEILELME-------------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 1022433638 1387 SQKDLE 1392
Cdd:COG1579 157 ELEELE 162
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1582 |
2.52e-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: 43.03 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1212 TEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsdeaiKYKDKIKTLEKNQEILDDTAKNLRVMLE 1291
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1292 SER-EQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 1370
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1371 SKLHAElsEQIKSFEKSQKDLEVALTHKDDNINAltnciTQLNLLECESESEGQNKGGNDSDELangevggdrnEKMKNQ 1450
Cdd:TIGR00618 379 QHIHTL--QQQKTTLTQKLQSLCKELDILQREQA-----TIDTRTSAFRDLQGQLAHAKKQQEL----------QQRYAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1451 IKQMMDVSRTQTAISVVEEDLKLLQ-----LKLRASVSTKCNLEDQVKKLEDDRNSLQAakaglEDECKTLRQKVEILNE 1525
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQslkerEQQLQTKEQIHLQETRKKAVVLARLLELQ-----EEPCPLCGSCIHPNPA 516
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1022433638 1526 LYQQKEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQK 1582
Cdd:TIGR00618 517 RQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1199-1373 |
2.55e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1199 RTVLVVKDRVYQVTEQQISEKLKTIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMilsdeaikykdkiKTLEKNQEI 1278
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-------------KLLEYITEL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1279 lddtaKNLRVMLESEREQNVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEA-----KLSEEKVKSECHRVQEEN 1353
Cdd:pfam15905 232 -----SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcklleSEKEELLREYEEKEQTLN 306
|
170 180
....*....|....*....|
gi 1022433638 1354 ARLKKKKEQLQQEIEDWSKL 1373
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1320-1506 |
2.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1320 MNASEFSEVQIALNEAKLSEEkvksECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQ--KDLEVALTH 1397
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1398 KDDNINALTNCITQLNLL--ECESESEGQNKGGNDSDELANgevggDRNEKMKNQIKQMM-DVSRTQTAISVVEEDLKLL 1474
Cdd:COG4717 144 LPERLEELEERLEELRELeeELEELEAELAELQEELEELLE-----QLSLATEEELQDLAeELEELQQRLAELEEELEEA 218
|
170 180 190
....*....|....*....|....*....|..
gi 1022433638 1475 QLKLRAsvstkcnLEDQVKKLEDDRNSLQAAK 1506
Cdd:COG4717 219 QEELEE-------LEEELEQLENELEAAALEE 243
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1224-1378 |
3.10e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1224 MKENTELVQKLSNYE--QKIKESKKHVQETRKQNMILSDEAI-KYKDKIKTL-EKNQEILDDTAKNLRVMLESEREQNVK 1299
Cdd:smart00787 122 VKTFARLEAKKMWYEwrMKLLEGLKEGLDENLEGLKEDYKLLmKELELLNSIkPKLRDRKDALEEELRQLKQLEDELEDC 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1300 NQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ-EIEDWSKLHAELS 1378
Cdd:smart00787 202 DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKLKEQLK 281
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1232-1528 |
3.16e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1232 QKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKnlrvMLESEREQNvKNQDLISENKKSI 1311
Cdd:PRK10929 65 ERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQ----LLEKSRQAQ-QEQDRAREISDSL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1312 EKLkdvismnASEFSEVQIALNEAK------------LSEEKVKSechrVQEENARLKKKKEQLQ---------QEIedw 1370
Cdd:PRK10929 140 SQL-------PQQQTEARRQLNEIErrlqtlgtpntpLAQAQLTA----LQAESAALKALVDELElaqlsannrQEL--- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1371 SKLHAELseqiksFEKSQKDLevalthkDDNINALTNcitQLNLL---ECESESEGQNKGGNDSDELANG---EVGGDRN 1444
Cdd:PRK10929 206 ARLRSEL------AKKRSQQL-------DAYLQALRN---QLNSQrqrEAERALESTELLAEQSGDLPKSivaQFKINRE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1445 -EKMKNQIKQMMDV-------SRTQT-----AISVVEE------DLKLLQLKLRASVST--------------------K 1485
Cdd:PRK10929 270 lSQALNQQAQRMDLiasqqrqAASQTlqvrqALNTLREqsqwlgVSNALGEALRAQVARlpempkpqqldtemaqlrvqR 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1022433638 1486 CNLEDQVKKLEDDRNSLQAAKAGLEDECK-----TLRQKVEILNELYQ 1528
Cdd:PRK10929 350 LRYEDLLNKQPQLRQIRQADGQPLTAEQNrildaQLRTQRELLNSLLS 397
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1214-1345 |
3.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1214 QQISEKLKTIMKENTE----LVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEildDTAKN 1285
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEklneLIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE---KEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1022433638 1286 LRVMLESEREQNVKNQDLISENKKSIEKLKDVIsmnasefsEVQIALNEA--KLSEEKVKSE 1345
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELI--------EARKRLNKAneKKEKKKKKQK 631
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1225-1386 |
3.84e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1225 KENtELVQKLSNYEQKIK------ESKKHVQETRKQNMILSDEAIKYKDKIKTLeknqeilddtaknlrvmleSEREQNV 1298
Cdd:COG1340 134 EEK-ELVEKIKELEKELEkakkalEKNEKLKELRAELKELRKEAEEIHKKIKEL-------------------AEEAQEL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1299 KNQdlISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED--WSKLHAE 1376
Cdd:COG1340 194 HEE--MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEE 271
|
170
....*....|
gi 1022433638 1377 LSEQIKSFEK 1386
Cdd:COG1340 272 IFEKLKKGEK 281
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1637-1916 |
4.43e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1637 QEEPVIVKPMPGKPNTQNPPrrGPLSQNGSF-------GPSPVSGGECSPPLTVEPPVRPLSATLNRRDMPRSEFGSVDG 1709
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPP--GPAAARQASpalpaapAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1710 PLPHP---RWSAEASGKPSPSDPGSGTATMMNSSS---RGSSPTRVLDEGKQTVLQEPEVPSVPSITSLaerPVAVNMAP 1783
Cdd:PHA03247 2782 RLTRPavaSLSESRESLPSPWDPADPPAAVLAPAAalpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL---PLGGSVAP 2858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1784 KGP-----PPFPGVPLMSTPMGGPVPPPIRYGPPPQLC---------GPFGPRPLPPPFGPGMRPPLGLREFAPGVPPGR 1849
Cdd:PHA03247 2859 GGDvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfalppdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1850 RDLPLHPR------GFLPGHAPFRPLGSLGPREYFIPGTRLPPP-----------------------------------T 1888
Cdd:PHA03247 2939 PQPPLAPTtdpagaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPapsreapasstppltghslsrvsswasslalheetD 3018
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1022433638 1889 HGP-----------------------------------------------QEYPPPPAVRDLLPSGSRDEPPPAS 1916
Cdd:PHA03247 3019 PPPvslkqtlwppddtedsdadslfdsdsersdlealdplppephdpfahEPDPATPEAGARESPSSQFGPPPLS 3093
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1217-1390 |
4.44e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1217 SEKLKTIMKENTELVQKLSNYEqkikeSKKHVQETRKQNMilsdeaikyKDKIKTLEKNQEILDDtaknlrvmlesEREQ 1296
Cdd:smart00787 108 SPDVKLLMDKQFQLVKTFARLE-----AKKMWYEWRMKLL---------EGLKEGLDENLEGLKE-----------DYKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1297 NVKNQDLISENKKSIEKLKDVISMNASEFSEVQIALNEAKLSE-----EKVKSECHRVQEEN---ARLKKKKEQLQQEIE 1368
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTEldrakEKLKKLLQEIMIKVkklEELEEELQELESKIE 242
|
170 180
....*....|....*....|..
gi 1022433638 1369 DWSKLHAELSEQIKSFEKSQKD 1390
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1230-1591 |
5.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1230 LVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKYKDKIKTLEKNQEILDDTAKNLRVMLESEREQnvknqdlISENKK 1309
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1310 SIEKLKDVISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDwsklHAELSEQIKSFEKSQk 1389
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE----AEALLEAGKCPECGQ- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1390 DLE-----VALTHKDDNINALTncitqLNLLECESESEGQNKGGNDSDELANGEVGGDRNEKMKNQIKQMMDVSRTQTAi 1464
Cdd:PRK02224 460 PVEgsphvETIEEDRERVEELE-----AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1465 svvEEDLKLLQLKLRAS-----------VSTKCNLE-----DQVKKLEDDRN-------------SLQAAKAGLEDECKT 1515
Cdd:PRK02224 534 ---EKRERAEELRERAAeleaeaeekreAAAEAEEEaeearEEVAELNSKLAelkerieslerirTLLAAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1516 LRQKVEILNELY-QQKEMALQKKLSQEEYERQEREHRLSAADEK---AVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 1591
Cdd:PRK02224 611 LREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDkerAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1442-1640 |
6.84e-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: 40.90 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1442 DRNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQVKKLEDDRNSLQAAKAGLEDECKTL 1516
Cdd:COG4942 23 AEAEAELEQLQQEIAelekeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1517 RQKVEILNELYQQKEMALQKK------------------------LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRR 1572
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1022433638 1573 IEEMEDELQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEP 1640
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1202-1574 |
9.11e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1202 LVVKDRVYQVTEQqiSEKLKTIMKEntelvqkLSNYEQKIKESKKHVQETRKQnmILSD-EAIKYKDKIKTLEKNQEILD 1280
Cdd:PTZ00440 1169 ILIDHIVEQINNE--AKKSKTIMEE-------IESYKKDIDQVKKNMSKERND--HLTTfEYNAYYDKATASYENIEELT 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1281 DTAKNLRVmlESEREQNVKN------------QDLISENKKSIEKLKDVISMNA---SEFSEVQIA--LNEAKLSEEKVK 1343
Cdd:PTZ00440 1238 TEAKGLKG--EANRSTNVDElkeiklqvfsylQQVIKENNKMENALHEIKNMYEfliSIDSEKILKeiLNSTKKAEEFSN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1344 SECHRVQEENARLKKKKEQLQQEIEDWSKLHAELS-EQIKSFEKSQKDLEVALTHKDDNINaltNCITQL--NLLECESE 1420
Cdd:PTZ00440 1316 DAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEdKQIDDEIKKIEQIKEEISNKRKEIN---KYLSNIksNKEKCDLH 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1022433638 1421 SEGQNKGGNDSDELANGEV--GGDRNEKMKNQIKQMMDVSRTqtaisvVEEDLKLLQLKLRASVSTKCNLEDQVKKLEDD 1498
Cdd:PTZ00440 1393 VRNASRGKDKIDFLNKHEAiePSNSKEVNIIKITDNINKCKQ------YSNEAMETENKADENNDSIIKYEKEITNILNN 1466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1022433638 1499 rNSLQAAKAGLE---DECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIE 1574
Cdd:PTZ00440 1467 -SSILGKKTKLEkkkKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLGRVK 1544
|
|
| |
