|
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 |
2.70e-44 |
|
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: 155.01 E-value: 2.70e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622828951 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWPEVWAGSVGRIFGYFPKDLIQVVHEYT 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 |
3.08e-38 |
|
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: 138.00 E-value: 3.08e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWPEVWAGSVG---RIFGYFPKDLIQVVHEYT 109
Cdd:cd11760 1 LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGgdaGLFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
38-109 |
1.12e-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: 1.12e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828951 38 CADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWPEVWAGSVGRIFGYFPKDLIQVVHEYT 109
Cdd:cd11892 2 CGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
37-108 |
1.15e-17 |
|
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: 79.51 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 37 LCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLAR--AWPEVWAGSVGR--------IFGYFPKDLIQVVH 106
Cdd:cd11891 1 LCADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVKenGAGEFWSGSVYSeryvdqmgIVGYFPSNLVKEQT 80
|
..
gi 1622828951 107 EY 108
Cdd:cd11891 81 VY 82
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
36-124 |
3.81e-17 |
|
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: 78.38 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 36 KLCADDECSMLMYRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWPEVWAGSV---------GRIfGYFPKDLIQVVH 106
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVqgdyygeqaARL-GYFPSSIVQEDQ 80
|
90
....*....|....*...
gi 1622828951 107 EYTKEELRVPADETDFVC 124
Cdd:cd11890 81 YLKPGKVEVKTDKWDFYC 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1288-1594 |
2.30e-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: 79.34 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1288 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLE------SE 1361
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleariEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKN-------------QDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:TIGR02169 770 LEEDLHKleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVG 1508
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1509 GDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV 1588
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
....*.
gi 1622828951 1589 EILNEL 1594
Cdd:TIGR02169 1010 EEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1280-1659 |
2.72e-13 |
|
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: 75.44 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1280 TEQQISEKLKIIMKENTELVQKLSNYEQKIK----ESKKHVQETRKQNMILSDEAIKFKDKIKTLekNNEILGDAAKNLR 1355
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1356 VMLESEREQNVKNQDLISENKKSIEKLKDAIS------MNA-SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkelTNSeSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAELSEQIKSF-------EKSQKDLEVALTHKDDNINALTNCITQL----NRLECESESEGQN---- 1493
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKeliiKNLDNTRESLETQlkvl 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1494 --KGGNDSDELANGEVGGDQNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQ 1571
Cdd:TIGR04523 474 srSINKIKQNLEQKQKELKSKEKELKKLNE--EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1572 A--AKAGLEDECKTLRQKVEIL---NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYK---RRIEE 1643
Cdd:TIGR04523 552 FelKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkenEKLSS 631
|
410
....*....|....*.
gi 1622828951 1644 MEDELQKTERSFKNQI 1659
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1282-1589 |
3.74e-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: 72.01 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESE 1361
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKL 1441
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1442 HAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKggndSDELANGEvggDQNEKMKNQIKQ 1521
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE---SKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1522 MMD-VSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQIKKLEDDRNSLQAAkaglEDECKTLRQKVE 1589
Cdd:TIGR02168 920 LREkLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1300-1645 |
5.39e-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: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1300 QKLSNYEQKIKESKKHVQETRKQnmilsdeaikfkdkIKTLEKNNEILGDAAKNLRVMLESEREQnvknqdlISENKKSI 1379
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKA--------------LAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1380 EKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDL 1459
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1460 EVALTHKDDNINALTN----CITQLNRLECESESEgqnkggNDSDELANGEVG--GDQNEKMKNQIKQMMDvsrtqtAIS 1533
Cdd:TIGR02168 816 NEEAANLRERLESLERriaaTERRLEDLEEQIEEL------SEDIESLAAEIEelEELIEELESELEALLN------ERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1534 VVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV----EILNELYQQKEMALQKKLSQE 1609
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKI 963
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622828951 1610 EYERQEREHRLSAADEK-----AV--SAAEEVKTYKRRIEEME 1645
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKikelgPVnlAAIEEYEELKERYDFLT 1006
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1281-1707 |
9.41e-11 |
|
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: 66.97 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKENTELVQKlsnyEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 1360
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1361 EREQNVKNQDL---ISENKKSIEKLKDAISMNASEFSEVQIALNeaklseeKVKSECHRVQEENARLKKKKEQLQQEIE- 1436
Cdd:TIGR04523 206 LKKKIQKNKSLesqISELKKQNNQLKDNIEKKQQEINEKTTEIS-------NTQTQLNQLKDEQNKIKKQLSEKQKELEq 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1437 ----------------------------DWSKlhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESE 1488
Cdd:TIGR04523 279 nnkkikelekqlnqlkseisdlnnqkeqDWNK---ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1489 SEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDR 1567
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1568 NSLQAAKAGLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 1647
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828951 1648 LQKTER---SFKNQIA--THEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEE 1707
Cdd:TIGR04523 512 VKDLTKkisSLKEKIEklESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1286-1604 |
4.92e-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: 64.99 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1286 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRK---------------QNMILSDEAIKFKDKIKTLEKNNEILGDA 1350
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1351 AKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 1430
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1431 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddniNALTNCITQLNRLECESESEGQnKGGNDSDELANGEVGGD 1510
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1511 QNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 1590
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330
....*....|....
gi 1622828951 1591 LNELYQQKEMALQK 1604
Cdd:pfam02463 488 LLLSRQKLEERSQK 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1349-1660 |
9.35e-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: 64.31 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1349 DAAKNLRVMLESEREQNVKNQDLISEnkkSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEE---KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRlECESESEG----QNKGGNDSDELAN 1504
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREAldelRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1505 GEVGGDQNEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTL 1584
Cdd:TIGR02168 822 LRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1585 RQKVEILN----ELYQQKEmALQKKLSQEEYE----RQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 1656
Cdd:TIGR02168 900 SEELRELEskrsELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....
gi 1622828951 1657 NQIA 1660
Cdd:TIGR02168 979 NKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1309-1652 |
7.65e-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: 61.23 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1309 IKESKKHVQETRKQnmilSDEAIKFKDKIKTLEknneilgDAAKNLRVM-LESEREQNVKNQDLISENKKSIEKLKDAIS 1387
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKELKAELR-------ELELALLVLrLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1388 MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD 1467
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1468 DNINALTNCITQLNRLECESESEGQNkggndsdelangevggdQNEKMKNQIKQMMDVSRtqtAISVVEEDLKLLQLKLR 1547
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEE-----------------LESRLEELEEQLETLRS---KVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1548 asvstkcNLEDQIKKLEDDRNSLQAAKAGLEDEcKTLRQKVEILNELYQQKEMA--LQKKLSQEEYERQEREHRLSAADE 1625
Cdd:TIGR02168 404 -------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*..
gi 1622828951 1626 KAVSAAEEVKTYKRRIEEMEDELQKTE 1652
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1281-1707 |
1.21e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEkLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 1360
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1361 EREqnvknqdlISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQEIEDWSK 1440
Cdd:COG4717 155 LEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1441 LHAELSEQIKSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNRLECESESEGQNKG 1495
Cdd:COG4717 221 ELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1496 GNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLqAAKA 1575
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1576 GLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTE 1652
Cdd:COG4717 380 GVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622828951 1653 RSFKNQIATHEKkahenwlkaraaeraiaeeKREAANLRHKLLELTQKMAMLQEE 1707
Cdd:COG4717 456 AELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1281-1604 |
1.61e-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: 59.65 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKE--NTELVQK-----LSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKN 1353
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1354 lrvmlesEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 1433
Cdd:TIGR04523 115 -------DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1434 EIED-----------------WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRLEcESESEGQ 1492
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLK-DEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1493 NKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQ----------TAISVVEEDLKLLQLKLRASVSTKCNLEDQIKK 1562
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622828951 1563 LEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQK 1604
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1281-1697 |
2.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKENtELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 1360
Cdd:PRK03918 175 KRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1361 ER--EQNVKN-QDLISENKKSIEKLKDaismNASEFSEVQ-IALNEAKLSE--EKVKSECHRVQEENARLKKKKEQLQQE 1434
Cdd:PRK03918 254 KRklEEKIRElEERIEELKKEIEELEE----KVKELKELKeKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1435 IEDWSKLHAELSEQIKSFEKSQKDLEVaLTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDEL--ANGEVGGDQN 1512
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELekAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1513 E------KMKNQIKQMMD-VSRTQTAISVV--------EEDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQAAKAGL 1577
Cdd:PRK03918 409 KitarigELKKEIKELKKaIEELKKAKGKCpvcgreltEEHRKELLEEYTAELK---RIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1578 EDECKTLRqKVEILNELYQQKEmALQKKLSQEEYErqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTErSFKN 1657
Cdd:PRK03918 486 EKVLKKES-ELIKLKELAEQLK-ELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKK 556
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622828951 1658 QIATHEKKAHEnwlkaraaeraiaeEKREAANLRHKLLEL 1697
Cdd:PRK03918 557 KLAELEKKLDE--------------LEEELAELLKELEEL 582
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1715-1985 |
3.08e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1715 PGRPNTQNPPRRGPL--SQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 1792
Cdd:PHA03247 2670 LGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1793 SPSDPGSGTAAMMNSSSRGSSPNRVIDEGKQTVLQEPEV-------PSVPSITSLAEHPVAVNM-----------APKGP 1854
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesrESLPSPWDPADPPAAVLApaaalppaaspAGPLP 2829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1855 PPFSGVPLMSTPMGGPIPPPIRYGPPP----QLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGKRDLPLHPREFLPG 1930
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVapggDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERP 2908
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622828951 1931 HTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQ 1985
Cdd:PHA03247 2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1293-1668 |
4.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1293 KENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLI 1372
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1373 SENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKKEQLQQEIEDWSKLHAELSEQIK 1450
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1451 SFEKSQKdLEVALTHKDDNINALTNCiTQLNRLEcESESEGQNKGGNDSDELANGEVGGDQNEKMK-NQIKQMMDVSRT- 1528
Cdd:PTZ00121 1559 KAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKv 1635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1529 -QTAISVVEEDLKLLQLKlRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQkkLS 1607
Cdd:PTZ00121 1636 eQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEE--LK 1708
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828951 1608 QEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSfKNQIAtHEKKAHE 1668
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIA-HLKKEEE 1767
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1345-1672 |
1.07e-07 |
|
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: 57.29 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1345 EILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKV-KSECHRVQEENAR 1423
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1424 LKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALtncITQLNRLECESESEGQNKGGNDSDELA 1503
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1504 NGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcNLEDQIKKLEDDRNSLQAAKAGLEDEcKT 1583
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ------LEEELLAKKKLESERLSSAAKLKEEE-LE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1584 LR----QKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 1659
Cdd:pfam02463 399 LKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330
....*....|...
gi 1622828951 1660 ATHEKKAHENWLK 1672
Cdd:pfam02463 479 LVKLQEQLELLLS 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1358-1625 |
1.86e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1358 LESEREQNVKNQDLIsenKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 1437
Cdd:COG1196 251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1438 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTnciTQLNRLECESESEGQNKggnDSDELANGEVGGDQNEKMKN 1517
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEEL---EELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1518 QIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQ 1597
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAE-------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|....*...
gi 1622828951 1598 KEMALQKKLSQEEYERQEREHRLSAADE 1625
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1277-1563 |
2.18e-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: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1277 YQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRV 1356
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1357 MLE-SEREQNVKNQD---LISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK---KKE 1429
Cdd:TIGR04523 483 NLEqKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1430 --QLQQEIEdwsklhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCItqlnrleceseSEGQNKGGNDSDELANGEv 1507
Cdd:TIGR04523 563 idEKNKEIE-------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-----------EEKEKKISSLEKELEKAK- 623
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1508 ggDQNEKMKNQIKQMmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKL 1563
Cdd:TIGR04523 624 --KENEKLSSIIKNI------KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1713-1984 |
2.41e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1713 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPrwSAEASGKP 1792
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--PPPPPGPP 2846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1793 SPSDPGSGTAAMMNSSSRGSSPnrvidegkQTVLQEPEVPSVPSITSLAEHPVAVNMAPKGPPPFSGVPLMSTPMGGPIP 1872
Cdd:PHA03247 2847 PPSLPLGGSVAPGGDVRRRPPS--------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1873 PPIRygpppqlcgpfgprplpppfgpgmrPPLGLREFAPGVPPGKRDLPLHPR---EFLPGHTPFRP---LGPLGPREYF 1946
Cdd:PHA03247 2919 PQPQ-------------------------PPPPPQPQPPPPPPPRPQPPLAPTtdpAGAGEPSGAVPqpwLGALVPGRVA 2973
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1947 IPGARLPPPTHG-PQDYPPPPAARDLPPSG-----------SRDDPPPAS 1984
Cdd:PHA03247 2974 VPRFRVPQPAPSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1281-1484 |
2.65e-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: 56.22 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKENTELV---QKLSNYEQKIKESKKHVQETRKQ----NMILSDEAIKFKDKIKTLEKNNEILGDAAKN 1353
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1354 LRVM---LESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 1430
Cdd:TIGR02168 840 LEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1431 LQQEIED----WSKLHAELSEQIKSF-EKSQKDLEVALTHKDDNINALTNCITQLNRLE 1484
Cdd:TIGR02168 920 LREKLAQlelrLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1284-1668 |
2.89e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1284 ISEKLKIIMKENTELVQKLSNYEQKIKESKKhVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLEsERE 1363
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1364 QNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLH 1442
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1443 AELSEQIKSFEKSQKDLEVA----------LT--HKDDNINALTnciTQLNRLECESE--SEGQNKGGNDSDELANGEVG 1508
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgreLTeeHRKELLEEYT---AELKRIEKELKeiEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1509 GDQNEKMKNQIKQMMDVSRTQTAISVVE--------EDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQA---AKAGL 1577
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEElekkaeeyEKLKEKLIKLKGEIK---SLKKELEKLEELKKKLAElekKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1578 EDECKTLRQK--------VEILNELYQQKEMALQK--KLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 1647
Cdd:PRK03918 569 EEELAELLKEleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420
....*....|....*....|.
gi 1622828951 1648 LQKTERSFKNQiaTHEKKAHE 1668
Cdd:PRK03918 649 LEELEKKYSEE--EYEELREE 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1281-1653 |
3.12e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKlkiimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KFKDK 1336
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1337 IKTLEKNNEILGDAAKNLRVM---LESEREQNVKNQDLISENKKSIEKLKDAISmnaSEFSEVQIALNEAKLSEEKVKSE 1413
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEAVEARREELE---DRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1414 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNRLECESESEGQN 1493
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1494 KGGNDSDElANGEVGGDQNEKMKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQlKLRASVSTkcnLEDQIKKLE 1564
Cdd:PRK02224 421 RDELRERE-AELEATLRTARERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1565 DDRNSLQAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSAAEEV 1634
Cdd:PRK02224 496 ERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEAREEV 574
|
410
....*....|....*....
gi 1622828951 1635 KTYKRRIEEMEDELQKTER 1653
Cdd:PRK02224 575 AELNSKLAELKERIESLER 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1282-1473 |
3.17e-07 |
|
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: 54.77 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKN-NEILGDAAKNLRVMLES 1360
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1361 EREQNVK---NQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 1437
Cdd:COG4942 117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622828951 1438 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 1473
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1294-1591 |
3.83e-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: 55.46 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1294 ENTELVQKLSNYEQKIKESKKHVQETRKQnmiLSDEAIKFKDKIKTLEKNNEILGDAakNLRVMLESEREQN-VKNQdlI 1372
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEEEQLrVKEK--I 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1373 SENKKSIEKLKDAISMNASEfsevqiaLNEAKLSEEKVKSECHRVQEEnarlkkkKEQLQQEIEDWSKLHAELSEQIKSF 1452
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1453 EKSQKDLEVALTHKDDNINALtncitqlnRLECESESEGQNKGGNDSDELaNGEVGGDQNEKMKNQIKQM---MDVSRTQ 1529
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAET--------RDELKDYREKLEKLKREINEL-KRELDRLQEELQRLSEELAdlnAAIAGIE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1530 TAISVVEEDLKLLQLKLRAS----VSTKCNLEDQIKKLEDDRNSLQAakagLEDECKTLRQKVEIL 1591
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEA 495
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1713-1999 |
4.72e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1713 PMPGRPNTQNPPRRGPLSQNGSFGPSPV-SGGECSPPLTVEPPVRPLSATLS----RRDMPRSEFGSV--------DGPL 1779
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDpAPGRVSRPRRARRLGRAAQASSPpqrpRRRAARPTVGSLtsladpppPPPT 2707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1780 PHPRWSAEASGKPSPSDPGSGtaammnsssRGSSPNRVIDEGKQTVLQEPEVP------SVPSITSLAEHPVAVNMAPKG 1853
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPAAA---------RQASPALPAAPAPPAVPAGPATPggparpARPPTTAGPPAPAPPAAPAAG 2778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1854 PPPFSGVPLMSTPMGGPIPPPIRYGPPPqlcGPFGPRPLPPPFGPGMRPplglrefAPGVPPGKRDLPLHPReflPGHTP 1933
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPAD---PPAAVLAPAAALPPAASP-------AGPLPPPTSAQPTAPP---PPPGP 2845
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1934 FRPLGPLGprEYFIPG---ARLPPPthgpQDYPPPPAARDLPPSgSRDDPPPASQSTSqdcSQALKQSP 1999
Cdd:PHA03247 2846 PPPSLPLG--GSVAPGgdvRRRPPS----RSPAAKPAAPARPPV-RRLARPAVSRSTE---SFALPPDQ 2904
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1283-1653 |
8.55e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1283 QISEKLKIIMKENTELVQKLSNYEqKIKESKKHVQETRKQNMILSDEaiKFKDKIKTLEKNNEILGDAAKNLRvmlesER 1362
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT-----AR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1363 EQNVKNQdlISENKKSIEKLKDA------ISMNASEFSEVQIaLNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIE 1436
Cdd:PRK03918 414 IGELKKE--IKELKKAIEELKKAkgkcpvCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1437 DWSKLHA--ELSEQIKSFEKSQKDLEVALTHKD--------DNINALTNCITQLNRlECESESEGQNKGGNDSDELANGE 1506
Cdd:PRK03918 491 KESELIKlkELAEQLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKK-ELEKLEELKKKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1507 vggdqnEKMKNQIKQMMdvSRTQTAISVVEEDLKLLQ------LKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDE 1580
Cdd:PRK03918 570 ------EELAELLKELE--ELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 1581 CKTLRQKVEILNELYQQKEMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 1653
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1273-1691 |
1.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1273 KSRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKFKDKIKtlEKNNEILGDAAK 1352
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDK--KKADELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1353 NLRVMLESEREQNVKNQDlisENKKSIEKLKDAISMNaSEFSEVQIALNEAKLSEEKVKSECHRVQEENAR----LKKKK 1428
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKAD---EAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKKKA 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAEL--SEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGE 1506
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1507 VGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEdQIKKLEDDRNSLQAAKAGLEDECKTLRQ 1586
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1587 kVEILNELYQQKEMALQKKlsqeEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEdELQKTERSFKNQIATHEKKA 1666
Cdd:PTZ00121 1652 -LKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAE 1725
|
410 420
....*....|....*....|....*
gi 1622828951 1667 HENWLKARAAERAIAEEKREAANLR 1691
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1280-1653 |
1.18e-06 |
|
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: 53.59 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1280 TEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILgdAAKNLRVMlE 1359
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1360 SEREQNVKNQD-LISENKKS-------IEKLKDAI-SMNA--SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:pfam05557 175 LEFEIQSQEQDsEIVKNSKSelaripeLEKELERLrEHNKhlNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAE----------LSEQIKSFEKSQkdlevaLTHKDDNiNALTNCITQLNRLECESESEGQNKGGND 1498
Cdd:pfam05557 255 EKLEQELQSWVKLAQDtglnlrspedLSRRIEQLQQRE------IVLKEEN-SSLTSSARQLEKARRELEQELAQYLKKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1499 SDElangevggdqNEKMKNQIKQmmdVSRTQTAISVVEEDLKLLQLKLR------ASVSTKCNLEDQIKKLEDDRNSLQA 1572
Cdd:pfam05557 328 EDL----------NKKLKRHKAL---VRRLQRRVLLLTKERDGYRAILEsydkelTMSNYSPQLLERIEEAEDMTQKMQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1573 AKAGLEDECKTLRQKVEILNELYQQKEMALQKKlsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 1652
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-------------RQQESLADPSYSKEEVDSLRRKLETLELERQRLR 461
|
.
gi 1622828951 1653 R 1653
Cdd:pfam05557 462 E 462
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1282-1672 |
1.36e-06 |
|
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: 53.58 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHV-------QETRKQNMILSDEAIKFKDKIKTLeknneiLGDAAKNL 1354
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1355 RvMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 1429
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1430 ------QLQQEIEDWSKLHAELSEQIKSFEKSQK---DLEVALTHKDDNINALTNCITQL-NRLECESESEGQNKggNDS 1499
Cdd:pfam15921 463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrSRVDLKLQELQHLK--NEG 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1500 DELANGEV----------GGDQN-EKMKNQIKQMMDV----SRTQTAISV----VEEDLKLLQLKLRASVSTKCNLEDQI 1560
Cdd:pfam15921 541 DHLRNVQTecealklqmaEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKI 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1561 KKLEDDRNSLQAAKAGLEDECKtlrQKVEILNELYQQKEMALQkklsqeeyerqerehrlsaadekavsaaeEVKTYKRR 1640
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLN-----------------------------EVKTSRNE 668
|
410 420 430
....*....|....*....|....*....|..
gi 1622828951 1641 IEEMEDELQKTERSFKNQiaTHEKKAHENWLK 1672
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1363-1600 |
1.70e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1363 EQNVKNQDLISENK---KSIEKLKDAIsmnasefsEVQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIEDWS 1439
Cdd:PHA02562 167 EMDKLNKDKIRELNqqiQTLDMKIDHI--------QQQIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1440 KLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLE-----------CESE-SEGQNKGGNDSDELANGEV 1507
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQiSEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1508 GGDQNEKMKNQIKQMMDVSRTQTaisvveEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQK 1587
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|...
gi 1622828951 1588 VEILNELYQQKEM 1600
Cdd:PHA02562 388 LDKIVKTKSELVK 400
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
49-105 |
2.69e-06 |
|
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: 46.05 E-value: 2.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 49 RGEALEDFTGPDCRFVNFKKGDPVYVYYKlarAWPEVWAGSVGRIFGYFPKDLIQVV 105
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGK---DNDGWWEGETGGRVGLVPSTAVEEI 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1418-1653 |
3.20e-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: 51.69 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1418 QEENARLKKKKEQLQQEIedwsklhAELSEQIKSFEKSQKDLEVALTHKDDNINALTNcitQLNRLECESESEGQNKGGN 1497
Cdd:COG4942 19 ADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1498 DSDELANGEVGGDQNEKMKNQIKQMMDVSRT--------QTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNS 1569
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1570 LQAAKAGLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 1649
Cdd:COG4942 162 LAALRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....
gi 1622828951 1650 KTER 1653
Cdd:COG4942 238 AAAE 241
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1713-1999 |
5.91e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1713 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 1792
Cdd:PHA03247 2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1793 SPSDPGSGTAAMMN---------SSSRGSSPNRVIDEGKQTVLQEPEV--------PSVPSITSLAE-HPVAVNMAPKGP 1854
Cdd:PHA03247 2634 AANEPDPHPPPTVPpperprddpAPGRVSRPRRARRLGRAAQASSPPQrprrraarPTVGSLTSLADpPPPPPTPEPAPH 2713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1855 PPFSGVPLMSTPMGGPIPPpirygpppqlcgpfgprplpppfgpgmrPPLGLREFAPGVPPGkrdlPLHPREFLPGHTPF 1934
Cdd:PHA03247 2714 ALVSATPLPPGPAAARQAS----------------------------PALPAAPAPPAVPAG----PATPGGPARPARPP 2761
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1935 RPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLP-PSGSRDDPPPASQSTSQDCSQALKQSP 1999
Cdd:PHA03247 2762 TTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPsPWDPADPPAAVLAPAAALPPAASPAGP 2827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1293-1482 |
6.84e-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: 50.53 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1293 KENTELVQKLSNYEQKIKESKKHVQETRKQnmilsdeAIKFKDKIKTLEKNneiLGDAAKNLRvmlESEREQNVKNQDL- 1371
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERR---IAALARRIR---ALEQELAALEAELa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1372 -----ISENKKSIEKLKDAIS------------------MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:COG4942 87 elekeIAELRAELEAQKEELAellralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622828951 1429 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNR 1482
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1712-1988 |
7.86e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.33 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1712 KPMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTVEPPVRPLSATLSRRDMPRSEfGSVDGPLPHPRWSAEASGK 1791
Cdd:PHA03307 83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1792 PSPSDPGSGTAAMMNSSSrGSSPNRVIDEGKqtvlqEPEVPSVPSI-TSLAEHPVAVNMAPKGPPPfSGVPLMSTPMGGP 1870
Cdd:PHA03307 161 AVASDAASSRQAALPLSS-PEETARAPSSPP-----AEPPPSTPPAaASPRPPRRSSPISASASSP-APAPGRSAADDAG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1871 IPPPIRYGPPPQLCGPfgprplpppfgpgmrpplGLREFAPGVPPGKRDLPLHPREFLPGHTPFRPLGPLGPREYFIPGA 1950
Cdd:PHA03307 234 ASSSDSSSSESSGCGW------------------GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622828951 1951 RLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTS 1988
Cdd:PHA03307 296 PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSS 333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-1599 |
7.88e-06 |
|
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: 51.21 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1286 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLekNNEIlgdAAKNLRVMLESEREQN 1365
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL--ANEI---SRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1366 VKNQ-----DLISENKKSIEKLKDAISMNASEFSEVQIALNEAklsEEKVKsECHRVQEEnarLKKKKEQLQQEIEDWSK 1440
Cdd:TIGR02168 314 LERQleeleAQLEELESKLDELAEELAELEEKLEELKEELESL---EAELE-ELEAELEE---LESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1441 LHAELSEQIKSFEKSQKDLEVALTHKDDNinaltncitqLNRLECESESEGQNKGGNDSDELangevggdqnekmknqik 1520
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDR----------RERLQQEIEELLKKLEEAELKEL------------------ 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1521 qmmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSlqaakagLEDECKTLRQKVEILNELYQQKE 1599
Cdd:TIGR02168 439 --------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-------AERELAQLQARLDSLERLQENLE 502
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1268-1647 |
8.08e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1268 TVLVVK-SRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLE-KNNE 1345
Cdd:COG5022 845 EVLIQKfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLE 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1346 ILGDAAKNLRVMLES------------EREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKlseeKVKSE 1413
Cdd:COG5022 925 FKTELIARLKKLLNNidleegpsieyvKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK----NFKKE 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1414 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELS--EQIKSFEKSQKDLevalthkDDNINALTnciTQLNRLECESESEG 1491
Cdd:COG5022 1001 LAELSKQYGALQESTKQLKELPVEVAELQSASKiiSSESTELSILKPL-------QKLKGLLL---LENNQLQARYKALK 1070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1492 QNKGGNDSDELangevggdqnekmknQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVST-------KCNLEDQIKKle 1564
Cdd:COG5022 1071 LRRENSLLDDK---------------QLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqmiKLNLLQEISK-- 1133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1565 ddrnSLQAAKAGLEDECKTLRQKVEILNELYQQKemALQKKLSQEEYERQEREHRLSAA--DEKAVSAAEEVKTYKRRIE 1642
Cdd:COG5022 1134 ----FLSQLVNTLEPVFQKLSVLQLELDGLFWEA--NLEALPSPPPFAALSEKRLYQSAlyDEKSKLSSSEVNDLKNELI 1207
|
....*
gi 1622828951 1643 EMEDE 1647
Cdd:COG5022 1208 ALFSK 1212
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1282-1651 |
1.02e-05 |
|
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: 50.74 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKkhvqetRKQNMILSDEAIKFKDKIKTLEKNNeilGDAAKNLRVMLESE 1361
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILR------RQLEIKKKEQREKEELKKLKLEAEE---LLADRVQEAQDKIN 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQialNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEdwskl 1441
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE----- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1442 hAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKggndsDELANGEVGGDQNEKMKNQIKQ 1521
Cdd:pfam02463 808 -EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL-----EEEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1522 MMDVSRTQTAISVVEEDLKLLQLKLRASV-----STKCNLEDQIKKLEDDRNSLQAAK-----AGLEDECKTLRQKVEIL 1591
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKLNlleekENEIEERIKEEAEILLKYEEEPEEllleeADEKEKEENNKEEEEER 961
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1592 NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVK---------TYKRRIEEMEDELQKT 1651
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKkliraiieeTCQRLKEFLELFVSIN 1030
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1385-1633 |
1.25e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1385 AISMNASEFSEVQIALNEAKLSEekvksechrVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 1464
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSE---------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1465 HKDDNINALTNCITQLNRLEcesesegQNKGGNDS--DELANGEVGGDQNEKMkNQIKQMMDvsRTQTAISVVEEDLKLL 1542
Cdd:COG3883 76 EAEAEIEERREELGERARAL-------YRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1543 QLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 1622
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|.
gi 1622828951 1623 ADEKAVSAAEE 1633
Cdd:COG3883 226 AAAAAAAAAAA 236
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1271-1606 |
1.27e-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: 50.34 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1271 VVKSRVYQVTEQQISEKLKIIMKENTELVQKLS-NYEQKIKESKKHVQETRKQNMILSDEAIKFKdkiKTLEKNNEILGD 1349
Cdd:COG5185 192 ISELKKAEPSGTVNSIKESETGNLGSESTLLEKaKEIINIEEALKGFQDPESELEDLAQTSDKLE---KLVEQNTDLRLE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1350 AAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNAS-EFSEVQIALNEAKLSEEKVKSEchrVQEENARLKKKK 1428
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRE---TETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEI-EDWSKLHAELSE--QIKSFEKSQKDLEVALTH----KDDNINALTNCITQLNRLEcesESEGQNKGGNDSD- 1500
Cdd:COG5185 346 EQGQESLtENLEAIKEEIENivGEVELSKSSEELDSFKDTiestKESLDEIPQNQRGYAQEIL---ATLEDTLKAADRQi 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1501 ELANGEVGGD--QNEKMKNQIKQMMDvSRTQTAISVVEEDLKLLQLKLRASVSTkcnLEDQIKKLEDDRNSLQAAKAGLE 1578
Cdd:COG5185 423 EELQRQIEQAtsSNEEVSKLLNELIS-ELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLK 498
|
330 340
....*....|....*....|....*...
gi 1622828951 1579 DECKTLRQKVEILNELYQQKEMALQKKL 1606
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1443-1707 |
1.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1443 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESEsegqnkggndsDELANGEvggdqnekmknqikqm 1522
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-----------RQISALR---------------- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1523 MDVSRTQTAISVVEEDLKLLQLKLRasvstkcNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVE-ILNELYQQKEM- 1600
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREAl 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1601 -ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEK--KAHENWLKARAAE 1677
Cdd:TIGR02168 806 dELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleSELEALLNERASL 885
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622828951 1678 RAIAEEKREAA--------NLRHKLLELTQKMAMLQEE 1707
Cdd:TIGR02168 886 EEALALLRSELeelseelrELESKRSELRRELEELREK 923
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1703-1999 |
1.44e-05 |
|
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: 50.15 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1703 MLQEEPVIVKPMPGRPNTQNPPRRGPlSQNGSFGPSPvsgGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSvdGPLPHP 1782
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGT-TQAATAGPTP---SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ--TPTLHP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1783 RwsaeasGKPSPSDPgsgtaamMNSSSRGSSPNRVIDEGKQTVLQEPEVPSVP----SITSLAEHPVAvnmapkgPPPFS 1858
Cdd:pfam03154 240 Q------RLPSPHPP-------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPhslqTGPSHMQHPVP-------PQPFP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1859 GVPLMSTPMGGPIPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrefapgvPPGKRDLP-LHPreflPGHTPFRPL 1937
Cdd:pfam03154 300 LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---------PPAPLSMPhIKP----PPTTPIPQL 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1938 gPLGPREYFIPGARLPPPTHGPQDYPPPPAARDL-------PPSGSrddpPPASQSTSQdcSQALKQSP 1999
Cdd:pfam03154 367 -PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLsslsthhPPSAH----PPPLQLMPQ--SQQLPPPP 428
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1381-1647 |
1.53e-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: 50.45 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1381 KLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE 1460
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1461 VALTHKDDNINALTNCITQLNrlecESESEGQNKGGNDSDELANGEVggDQNEKMKNQIKQmmDVSRTQTAISVVEEDLK 1540
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELE----EDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEE--EVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1541 LLQLKLRASVSTKCNLEDQIKKLEDDRNS-------LQAAKAGLEDECKTLRQKVEILNELYQ---------QKEM-ALQ 1603
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLrELE 902
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622828951 1604 KKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 1647
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1282-1707 |
1.66e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESE 1361
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKK-----SIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK---EQLQQ 1433
Cdd:TIGR02168 420 QQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1434 EIEDWSK--------------LHAELSEQIKSFEKSQKDLEVAL-------THKDDN-----INALT-NCITQLNRLECE 1486
Cdd:TIGR02168 500 NLEGFSEgvkallknqsglsgILGVLSELISVDEGYEAAIEAALggrlqavVVENLNaakkaIAFLKqNELGRVTFLPLD 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1487 SESEGQNKgGNDSDELAN--GEVG-GDQNEKMKNQIKQMMD--------VSRTQTAIsvveEDLKLLQLKLR-------- 1547
Cdd:TIGR02168 580 SIKGTEIQ-GNDREILKNieGFLGvAKDLVKFDPKLRKALSyllggvlvVDDLDNAL----ELAKKLRPGYRivtldgdl 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1548 ---------ASVSTKC----------NLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEM---ALQKK 1605
Cdd:TIGR02168 655 vrpggvitgGSAKTNSsilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKD 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1606 LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHENWLKARAAERAIAE 1682
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTL 814
|
490 500
....*....|....*....|....*
gi 1622828951 1683 EKREAANLRHKLLELTQKMAMLQEE 1707
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERR 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1284-1668 |
1.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1284 ISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsDEAIKFKDKIKTLEKNNEILG------DAAKNLRVM 1357
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEerhelyEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1358 LES--------EREQNVKNQDLISENKKSIE----KLKDAISMNASEFSEVQIALNEAKLSEEKVKSeCHRVQEENARlK 1425
Cdd:PRK03918 374 LERlkkrltglTPEKLEKELEELEKAKEEIEeeisKITARIGELKKEIKELKKAIEELKKAKGKCPV-CGRELTEEHR-K 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1426 KKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALThKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELAN- 1504
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKl 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1505 ----GEVGGDQnEKMKNQIKQMMDVSRTQTAISV----VEEDLKLLQLKLRA-SVSTKCNLEDQIKKLE----------D 1565
Cdd:PRK03918 531 keklIKLKGEI-KSLKKELEKLEELKKKLAELEKkldeLEEELAELLKELEElGFESVEELEERLKELEpfyneylelkD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1566 DRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMaLQKKLSQEEYERQEREHRlsAADEKAVSAAEEVKTYKRRIEEME 1645
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEE-LRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELE 686
|
410 420
....*....|....*....|....*.
gi 1622828951 1646 ---DELQKTERSFKNQIATHEKKAHE 1668
Cdd:PRK03918 687 krrEEIKKTLEKLKEELEEREKAKKE 712
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1342-1671 |
1.99e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1342 KNNEILGDAAKNLRVMLESEREQNVKNQDL---ISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQ 1418
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLreeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1419 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGND 1498
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1499 SDE-----LANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAA 1573
Cdd:COG4372 181 AEQaldelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1574 KAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 1653
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|....*...
gi 1622828951 1654 SFKNQIATHEKKAHENWL 1671
Cdd:COG4372 341 DLLQLLLVGLLDNDVLEL 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1282-1484 |
2.94e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESE 1361
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEV--QIALNEAKLSEEKVKSEchrvqeenaRLKKKKEQLQQEIEDWS 1439
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLelQIASLNNEIERLEARLE---------RLEDRRERLQQEIEELL 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622828951 1440 K--LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLE 1484
Cdd:TIGR02168 428 KklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1281-1472 |
3.26e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 1360
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1361 EreqNVknQDLISenkkSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 1440
Cdd:COG3883 112 E---SF--SDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|..
gi 1622828951 1441 LHAELSEQIKSFEKSQKDLEVALTHKDDNINA 1472
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1374-1707 |
3.36e-05 |
|
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: 49.20 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1374 ENKKSIEKLKDAISMNAS----EFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQI 1449
Cdd:pfam02463 174 ALKKLIEETENLAELIIDleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1450 KSFEKSQKDLE--VALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQmmdvSR 1527
Cdd:pfam02463 254 ESSKQEIEKEEekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----KE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1528 TQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLS 1607
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1608 QEEYERQEREHRLSAADEKA--VSAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHENWLKarAAERAIAEEKR 1685
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELeiLEEEEESIELKQGKLTEEKEELEKQEL-KLLKDELELKKSEDLLK--ETQLVKLQEQL 486
|
330 340
....*....|....*....|..
gi 1622828951 1686 EAANLRHKLLELTQKMAMLQEE 1707
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSG 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1306-1691 |
4.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1306 EQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEK-NNEILGDAAKNLRVMLESEREQNVKnqdliSENKKSIEKLKD 1384
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEeRNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKK 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1385 AismnasefSEVQIAlNEAKLSEEKVKSECHRVQEENARlkkKKEQLQQEIEDWSKLHAELSeqiKSFEKSQKDLEVAlt 1464
Cdd:PTZ00121 1286 A--------EEKKKA-DEAKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAA-- 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1465 hkddninaltncitqlnrlecesesegQNKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTaisvvEEDLKLLQL 1544
Cdd:PTZ00121 1349 ---------------------------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA-----EEKKKADEA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1545 KLRASVSTKcnLEDQIKKLEDDRNSLQAAKAGLEDECKT--LRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 1622
Cdd:PTZ00121 1397 KKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828951 1623 ADEKAVSA--AEEVKTYKRRIEEMEDELQKTERSFKNqiATHEKKAHEnwlKARAAERAIAEEKREAANLR 1691
Cdd:PTZ00121 1475 AKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEE---AKKADEAKKAEEAKKADEAK 1540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1286-1700 |
5.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1286 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEIL-GDAAKNLRVMLESEREQ 1364
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEeARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1365 NVKNQDLiseNKKSIEKLKDAISMNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLKK-KKEQLQQEIEDWSKLH- 1442
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAE----AARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEd 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1443 AELSEQIKSFEKSQKDLEVALTHKDDNINALTNC-----ITQLNRLECESESEGQNKggndSDELANGEvggdqNEKMKN 1517
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeearMAHFARRQAAIKAEEARK----ADELKKAE-----EKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1518 QIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQIKKLEDDRNSLQAAKAGLEDECKTL------------- 1584
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaekk 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1585 ----RQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIA 1660
Cdd:PTZ00121 1373 keeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622828951 1661 THEKKAHENWLKARAAERAIAEEKREAANLRhKLLELTQK 1700
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKK 1491
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1515-1668 |
6.08e-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: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1515 MKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 1594
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1595 ---YQQ--------KEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 1662
Cdd:COG1579 75 ikkYEEqlgnvrnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*.
gi 1622828951 1663 EKKAHE 1668
Cdd:COG1579 155 EAELEE 160
|
|
| PROL5-SMR |
pfam15621 |
Proline-rich submaxillary gland androgen-regulated family; SMR is a family of proteins found ... |
1927-1999 |
9.65e-05 |
|
Proline-rich submaxillary gland androgen-regulated family; SMR is a family of proteins found in eukaryotes. The family of SMR proteins is expressed in the submaxillary gland. SMR members may play a role in protection or detoxification.
Pssm-ID: 434817 [Multi-domain] Cd Length: 103 Bit Score: 43.26 E-value: 9.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1927 FLPGHTPFRPLGPLGPREY---FIPGArlPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTSQDCSQALKQSP 1999
Cdd:pfam15621 25 GPRGHDPRRPLPPSQPPPNgpqIGPPP--PPPPYGPGRIPPPPPPPFGPGRIPPPPPPPYGPGRILSQSFPPPPDP 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1624 |
1.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1350 AAKNLRVMLESEREQNVKNqdlISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKE 1429
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1430 QLQQEIEdwsKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLecesesegqnkggndsdelangevgg 1509
Cdd:COG4942 94 ELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1510 dqNEKMKNQIKQMMdvsRTQTAISVVEEDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVE 1589
Cdd:COG4942 145 --APARREQAEELR---ADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|....*
gi 1622828951 1590 ILnelyQQKEMALQKKLSQEEYERQEREHRLSAAD 1624
Cdd:COG4942 217 EL----QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1282-1603 |
1.42e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIimKENTELVQKLSNYEQKIKESKKHVQETrkqnmilsdeaikfKDKIKTLEKNNEILGDAAKNLRVMLESE 1361
Cdd:COG1196 216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEEL--------------EAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKKSIEKLkdaismnasefsEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEIEDWSKL 1441
Cdd:COG1196 280 ELELEEAQAEEYELLAELARL------------EQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1442 HAELSEQIKSFEKSQKDLEVALTHKDDNINALtncITQLNRLEcESESEGQNKGGNDSDELANGEvgGDQNEKMKNQIKQ 1521
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELA-EELLEALRAAAELAAQLEELE--EAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1522 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDEcktLRQKVEILNELYQQKEMA 1601
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA---LAELLEELAEAAARLLLL 496
|
..
gi 1622828951 1602 LQ 1603
Cdd:COG1196 497 LE 498
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1753-1982 |
1.45e-04 |
|
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: 44.09 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1753 PPVRPLSATLSRRDMPRSEFGSVDGPLPhprwsaeASGKPSPSDPGSGTAAMmnsssrgSSPnrvidegkqtvlqePEVP 1832
Cdd:pfam06346 1 PPPPPLPGDSSTIPLPPGACIPTPPPLP-------GGGGPPPPPPLPGSAAI-------PPP--------------PPLP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1833 SVPSITSLAEHPVAVNMAPkgPPPFSGVPLMSTPmggpipppirygpppqlcgpfgprplpppfgpgmrPPLglrEFAPG 1912
Cdd:pfam06346 53 GGTSIPPPPPLPGAASIPP--PPPLPGSTGIPPP-----------------------------------PPL---PGGAG 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1913 VPPgkrdlPLHPREFLPGHTPFRPLGPLGPreyfipGARLPPPTHGPQDYPPPPAARDLPPsgsrddPPP 1982
Cdd:pfam06346 93 IPP-----PPPPLPGGAGVPPPPPPLPGGP------GIPPPPPFPGGPGIPPPPPGMGMPP------PPP 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1369-1664 |
1.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1369 QDLISENKKSIEKLKDAISmnASEFSEVQIALNEAKLseEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSE- 1447
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIK--RTENIEELIKEKEKEL--EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEl 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1448 --QIKSFEKSQKDLEVALTHKDDNINaltncitqlnrlECESESEGQNKGGNDSDELangEVGGDQNEKMKNQIKQMMDV 1525
Cdd:PRK03918 244 ekELESLEGSKRKLEEKIRELEERIE------------ELKKEIEELEEKVKELKEL---KEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1526 SRTqtaisvVEEDLKLLQLKLRasvstkcNLEDQIKKLEDDRNSLQAakagLEDECKTLRQKVEILNELYQQKEMALQKK 1605
Cdd:PRK03918 309 LRE------IEKRLSRLEEEIN-------GIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828951 1606 LSQEEYERQEREHRLsaadEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEK 1664
Cdd:PRK03918 372 EELERLKKRLTGLTP----EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1538-1707 |
1.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1538 DLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELY---QQKEMALQKKLSQEEYERQ 1614
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1615 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 1691
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170
....*....|....*.
gi 1622828951 1692 HKLLELTQKMAMLQEE 1707
Cdd:COG1196 386 EELLEALRAAAELAAQ 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1388-1602 |
1.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1388 MNASEFSEVQIALNEAKLSEEkvksECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQ--KDLEVALTH 1465
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1466 KDDNINALTNCITQLNRLEcesesegqnkggndsDELANGEvggDQNEKMKNQIKQMMDVSRTQTaisvvEEDLKLLQLK 1545
Cdd:COG4717 144 LPERLEELEERLEELRELE---------------EELEELE---AELAELQEELEELLEQLSLAT-----EEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 1546 LRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMAL 1602
Cdd:COG4717 201 LEE-------LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
1935-1994 |
1.96e-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: 46.30 E-value: 1.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828951 1935 RPLGPLGPREYF----IPGARL-PPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTSQDCSQA 1994
Cdd:pfam15685 143 RPLLPLLPRQLIekdpAPGAPApPPPTPLEPRKPPPLPPSDRQPPNRGITPALATSATSPTDSQA 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1298-1659 |
2.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1298 LVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQnvknqdlISENKK 1377
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1378 SIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK----------KKKEQLQ---------QEIEDW 1438
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLeagkcpecgQPVEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1439 SKLHA--ELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI---TQLNRLECESESEGQ----NKGGNDSDELA------ 1503
Cdd:PRK02224 465 PHVETieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEEliaeRRETIEEKRERaeelre 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1504 -NGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKllqlklrasvstkcNLEDQIKKLEDDRNSLqAAKAGLEDECK 1582
Cdd:PRK02224 545 rAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA--------------ELKERIESLERIRTLL-AAIADAEDEIE 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1583 TLRQKVEILNELY-QQKEMALQKKLSQEEYERQEREHRLSAADEK---AVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 1658
Cdd:PRK02224 610 RLREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDkerAEEYLEQVEEKLDELREERDDLQAEIGAVENE 689
|
.
gi 1622828951 1659 I 1659
Cdd:PRK02224 690 L 690
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1278-1580 |
2.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1278 QVTEQQISEKLKIIMKENTELVQKLSNYEQ-KIK-ESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLR 1355
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1356 VMLESEREQNVKNQDLISENKKSIEKL-------KDAISMNASEFSEVQIAlNEAKLSEEKVKSECHRVQEENARLKKKK 1428
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeaKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1429 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHkddninaltncitQLNRLECESESEGQNKGGNDSDELANGEVG 1508
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-------------ELDEEDEKRRMEVDKKIKDIFDNFANIIEG 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1509 GDQNEKMKNQIKQMMDVSRTQTAIS---VVEEDLKLLQLKLRA-------------SVSTKCNLEDQIKKLEDDRNSLQA 1572
Cdd:PTZ00121 1814 GKEGNLVINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKnnengedgnkeadFNKEKDLKEDDEEEIEEADEIEKI 1893
|
....*...
gi 1622828951 1573 AKAGLEDE 1580
Cdd:PTZ00121 1894 DKDDIERE 1901
|
|
| SH3_p40phox |
cd11869 |
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil ... |
49-105 |
2.30e-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: 40.94 E-value: 2.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 49 RGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWPEvwaGSVGRIFGYFPKDLIQVV 105
Cdd:cd11869 1 RAEALFDFTGNSKLELNFKAGDVIFLLSRVNKDWLE---GTVRGATGIFPLSFVKII 54
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1309-1599 |
2.41e-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: 46.21 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1309 IKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKD---A 1385
Cdd:pfam05911 481 IRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDfveG 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1386 ISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQqEIEDWSKLH-------AELSEQIKSFEKSQKD 1458
Cdd:pfam05911 561 LSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKV 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1459 --LEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAIS--- 1533
Cdd:pfam05911 640 tlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlq 719
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 1534 VVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL-NELYQQKE 1599
Cdd:pfam05911 720 ESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALeVELEEEKN 786
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1359-1474 |
2.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1359 ESEREQNVKNQDLISENKKSIEKLKdaismnaSEF-SEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 1437
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE 118
|
90 100 110
....*....|....*....|....*....|....*..
gi 1622828951 1438 WSKLHAELSEQIKSFEKSQKDLEVALthkdDNINALT 1474
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1259-1659 |
4.27e-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: 45.33 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1259 VSFAVFFWRTVLVVKSRVYqVTEQQISEKLKIIMKENTELVQKlsnyeQKIKESKKHVQETrkqnmilsdEAIKFKDKIK 1338
Cdd:COG5185 148 DIEASYGEVETGIIKDIFG-KLTQELNQNLKKLEIFGLTLGLL-----KGISELKKAEPSG---------TVNSIKESET 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1339 TLEKNNEILGDAAKNLRVMLESEREQNVKNQDLisenkKSIEKLKDAISMNASEFSEvqiaLNEAKLSEEKVKSEchRVQ 1418
Cdd:COG5185 213 GNLGSESTLLEKAKEIINIEEALKGFQDPESEL-----EDLAQTSDKLEKLVEQNTD----LRLEKLGENAESSK--RLN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1419 EENARLKKKKEQLQQEIE------DWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCITQLNrlecESESEGQ 1492
Cdd:COG5185 282 ENANNLIKQFENTKEKIAeytksiDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQ----ESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1493 NKGGNDSDELAnGEVGGDQNEKMKNQIKQMMDVSRT--------------------QTAISVVEEDLKLLQLKLRASVST 1552
Cdd:COG5185 357 EAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQIEELQRQIEQATSS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1553 KCNLEDQIKKLED-----DRNSLQAAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAA 1623
Cdd:COG5185 436 NEEVSKLLNELISelnkvMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622828951 1624 DEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 1659
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1270-1605 |
4.43e-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: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1270 LVVKSRVYQVTEQQISEKLKIIMKE-------NTELVqklSNYEQKIKESKKHVQETRKQNMIL---SDEAIKFKDKIKT 1339
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTElekeklkNIELT---AHCDKLLLENKELTQEASDMTLELkkhQEDIINCKKQEER 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1340 LEKNNEILGDAAKNLRVMLESEREQNVKNQDlisENKKSIEKlkdaiSMNASEFSEVQIALNEAKLSEEKVKSECHRVQE 1419
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGD---EVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1420 ENArlKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNciTQLNRLECESESEGQNKGgnds 1499
Cdd:pfam05483 604 ENK--NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID--NYQKEIEDKKISEEKLLE---- 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1500 dELANGEVGGDQNEKMKNQIKQ-----------MMDVSRTQTAISVVEED--LKLLQLKLRASVSTKCNLEDQIKKLedd 1566
Cdd:pfam05483 676 -EVEKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI--- 751
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622828951 1567 RNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQKK 1605
Cdd:pfam05483 752 KAELLSLKKQLEIE----KEEKEKLKMEAKENTAILKDK 786
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1297-1454 |
5.84e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1297 ELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQ--NVKN----QD 1370
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNnkeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1371 LISE---NKKSIEKLKDAIS--MNASEFSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEdwsKLHAEL 1445
Cdd:COG1579 94 LQKEiesLKRRISDLEDEILelMERIEELEEELAELEAELAELEA-----ELEEKKAELDEELAELEAELE---ELEAER 165
|
....*....
gi 1622828951 1446 SEQIKSFEK 1454
Cdd:COG1579 166 EELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1332-1707 |
6.27e-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: 45.06 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1332 KFKDKIKTLEKN---NEILGDAAKNLRVMLESEREQNVKNQDLISENKKSieklkdaismnasEFSEVQIALNEAKLSEE 1408
Cdd:TIGR02169 174 KALEELEEVEENierLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------------EGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1409 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKsfeKSQKDLEVALTHKddnINALTNCITQLNRLECESE 1488
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEK---IGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1489 segqnkggndsdelangevggDQNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDR 1567
Cdd:TIGR02169 315 ---------------------RELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1568 NSLQAAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKtykrRIEEMEDE 1647
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA----GIEAKINE 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1648 LQKTERSFKNQIATHEKKAHENwlkaraaERAIAEEKREAANLRHKLLELTQKMAMLQEE 1707
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQL-------AADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1286-1463 |
6.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1286 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIK-FKDKIKTLEK-NNEI--LGDAAKNLRVM---L 1358
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEE-------LGFESVEeLEERLKELEPfYNEYleLKDAEKELEREekeL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1359 ESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQialnEAKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIE 1436
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE----YEELREEYLElsRELAGLRAELEELEKRREEIKKTLE 697
|
170 180
....*....|....*....|....*..
gi 1622828951 1437 dwsKLHAELsEQIKSFEKSQKDLEVAL 1463
Cdd:PRK03918 698 ---KLKEEL-EEREKAKKELEKLEKAL 720
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1283-1446 |
8.06e-04 |
|
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: 43.85 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1283 QISEKLKIIMKENTELVqklsnyeqkiKESKKHVqetRKQNMILSDEAIKFKDKIKTLEKNneilgdaaknLRVMLESER 1362
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL---MKELELLNSIKPKLRDRKDALEEE----------LRQLKQLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1363 EQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ-EIEDWSKL 1441
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKL 276
|
....*
gi 1622828951 1442 HAELS 1446
Cdd:smart00787 277 KEQLK 281
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1510-1708 |
9.30e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1510 DQNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTL 1584
Cdd:COG4942 23 AEAEAELEQLQQEIAelekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1585 RQKV-EILNELYQQK-----EMALQKKLSQEEYERQEREHRLSAADEKAVSA-----------AEEVKTYKRRIEEMEDE 1647
Cdd:COG4942 103 KEELaELLRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElradlaelaalRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828951 1648 LQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEP 1708
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1305-1663 |
1.11e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1305 YEQKIKESKKHVQETRKQN---MILSDEAIKFKDKIKTLEKNNeilgDAAKNLRVMLESEREQ-----NVKNQDLISENK 1376
Cdd:pfam05622 85 YRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKKledlgDLRRQVKLLEER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1377 KSI---------EKLKDAISMNAS-EFSEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQE----IEDWSKLH 1442
Cdd:pfam05622 161 NAEymqrtlqleEELKKANALRGQlETYKRQVQELHGKLSEESKKAD--KLEFEYKKLEEKLEALQKEkerlIIERDTLR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1443 aELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQ---------LNRLECESESEGQNKGGNDSDELANGEVGGDQNE 1513
Cdd:pfam05622 239 -ETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEimpaeirekLIRLQHENKMLRLGQEGSYRERLTELQQLLEDAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1514 KMKNQIKQMMDVSRTQtaISVVEEDLKLLQLKLRA-------SVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQ 1586
Cdd:pfam05622 318 RRKNELETQNRLANQR--ILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDS 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1587 KVeilnelyQQKEMALQKKLSQEEYERQEREHRLSAADEKA------------VSAAEEVKTYKRRIEEMEDELQKTERS 1654
Cdd:pfam05622 396 NL-------AQKIDELQEALRKKDEDMKAMEERYKKYVEKAksviktldpkqnPASPPEIQALKNQLLEKDKKIEHLERD 468
|
....*....
gi 1622828951 1655 FKNQIATHE 1663
Cdd:pfam05622 469 FEKSKLQRE 477
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1379-1631 |
1.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1379 IEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEI----EDWSKLHAELSEQIKSFEK 1454
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1455 SQKD---LEVALTHKDdninaLTNCITQLNRLECESESegqnkggndsdelangevggdQNEKMKNQIKQMMDVSRTQTA 1531
Cdd:COG3883 98 SGGSvsyLDVLLGSES-----FSDFLDRLSALSKIADA---------------------DADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1532 ISVVEEDLKLLQLKlrasvstkcnLEDQIKKLEDDRNSLQAAKAGLE-DECKTLRQKVEILNELYQQKEMALQKKLSQEE 1610
Cdd:COG3883 152 LEAKLAELEALKAE----------LEAAKAELEAQQAEQEALLAQLSaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250 260
....*....|....*....|.
gi 1622828951 1611 YERQEREHRLSAADEKAVSAA 1631
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAA 242
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1792-1999 |
1.61e-03 |
|
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: 43.60 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1792 PSPSDpgsgtaammNSSSRGSSPNRVIDEGKQTVLQEPEVPSVP---------SITSLAEHPVAVNMAPKGPPPFSGVPL 1862
Cdd:pfam03154 149 PSPQD---------NESDSDSSAQQQILQTQPPVLQAQSGAASPpsppppgttQAATAGPTPSAPSVPPQGSPATSQPPN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1863 MSTPMGgpipppirygpppqlcgpfgprplpppfgpgmrPPLGLREFAPgvppgkrdlPLHPREFLPGHTPFRPLGPLGP 1942
Cdd:pfam03154 220 QTQSTA---------------------------------APHTLIQQTP---------TLHPQRLPSPHPPLQPMTQPPP 257
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828951 1943 REYFIPGARLPPPTHGPQ--------------DYPPPPAARDLPPSGSRDDPPPASQSTSQDCSQALKQSP 1999
Cdd:pfam03154 258 PSQVSPQPLPQPSLHGQMppmphslqtgpshmQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTP 328
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1301-1594 |
1.66e-03 |
|
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: 43.89 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1301 KLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEI---------------LGDAAKNLRV----MLESE 1361
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeckskiestlddkdIDECIKKIKElknhILSEE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNV--KNQDlisENKKSIEKLKDAISM--NASEF----------SEVQIALNEAKLSEEKVKSeCHRVQEENAR-LKK 1426
Cdd:TIGR01612 1436 SNIDTyfKNAD---ENNENVLLLFKNIEMadNKSQHilkikkdnatNDHDFNINELKEHIDKSKG-CKDEADKNAKaIEK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1427 KKEQLQQEIEDWSKLHAELSE-QIKS-FEKSQKDLEVALTHKDDNINALTncitqlnrLECESESEGQNKGGND----SD 1500
Cdd:TIGR01612 1512 NKELFEQYKKDVTELLNKYSAlAIKNkFAKTKKDSEIIIKEIKDAHKKFI--------LEAEKSEQKIKEIKKEkfriED 1583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1501 ELANGEVGG----DQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRA-SVSTKcnlEDQIKKLEDDRNSLQAAKA 1575
Cdd:TIGR01612 1584 DAAKNDKSNkaaiDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQ---DTELKENGDNLNSLQEFLE 1660
|
330
....*....|....*....
gi 1622828951 1576 GLEDECKTLRQKVEILNEL 1594
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELDEL 1679
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1248-1606 |
1.67e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1248 KPVLITAFLGIVSFAVFFwrtvLVVKSRVYQVTEQ-QI-SEKLKIIMKENTELVQKLSNYEQKIKeskkhvqetrkqnMI 1325
Cdd:COG3206 28 KWLILLVFLLVLALALLY----ALLLPPVYEASATlLVePQSSDVLLSGLSSLSASDSPLETQIE-------------IL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1326 LSDE----AIK----FKDKIKTLEKNNEILGDAAKNLRVmlesereQNVKNQDLI-----SENKKSIEKLKDAIsmnASE 1392
Cdd:COG3206 91 KSRPvlerVVDklnlDEDPLGEEASREAAIERLRKNLTV-------EPVKGSNVIeisytSPDPELAAAVANAL---AEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1393 FSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEDWSKLH--AELSEQIKSFEKSQKDLEVALTHKDDNI 1470
Cdd:COG3206 161 YLEQNLELRREEARKALE-----FLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1471 NALTNCITQLNRLECESESEGQNKGGNDS-----DELANGEV--------GGDQNEKMKNQIKQMMDV-----SRTQTAI 1532
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAelaelsarYTPNHPDVIALRAQIAALraqlqQEAQRIL 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828951 1533 SVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDecktLRQKVEILNELYQQkemaLQKKL 1606
Cdd:COG3206 316 ASLEAELEALQAREAS-------LQAQLAQLEARLAELPELEAELRR----LEREVEVARELYES----LLQRL 374
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1287-1458 |
1.82e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1287 KLKIIMKENTELVQKLSNYEQKIKESKKHVQE---------TRKQNMI--LSDEAIKFK-------DKIKTLEKNNEILG 1348
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEqrkkngeniARKQNKYdeLVEEAKTIKaeieeltDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1349 DAAKNLR-----------------VM-------------LESEREQNVKNQDLISENKKSIEKLKDAI---SMNASEFSE 1395
Cdd:PHA02562 255 AALNKLNtaaakikskieqfqkviKMyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIdelEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 1396 VQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEI----EDWSKLHAELSEQIKSFEKSQKD 1458
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnaEELAKLQDELDKIVKTKSELVKE 401
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1253-1392 |
1.82e-03 |
|
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: 40.50 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1253 TAFLGIVSFAV-------FFWRTVL-VVKSRvyqvtEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 1324
Cdd:cd06503 1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828951 1325 ILsDEAIKFKDKIKtleknNEILGDAAKnlrvmlESEREQNVKNQDLISENKKSIEKLKD---AISMNASE 1392
Cdd:cd06503 70 II-EEARKEAEKIK-----EEILAEAKE------EAERILEQAKAEIEQEKEKALAELRKevaDLAVEAAE 128
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1293-1454 |
2.03e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1293 KENtELVQKLSNYEQKIKESKKhvqetrkqnmilsdeAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLI 1372
Cdd:COG1340 134 EEK-ELVEKIKELEKELEKAKK---------------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1373 SENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED--WSKLHAELSEQIK 1450
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLK 277
|
....
gi 1622828951 1451 SFEK 1454
Cdd:COG1340 278 KGEK 281
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1715-1989 |
2.62e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1715 PGRPNTQNPPR-RGPLSQNGsfGPSPVSGGECSPPlTVEPPVRPLSATLSrrDMPRSEfgsvdgPLpHPR---W------ 1784
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGGPPDPD-APPAPSRLAPAILP--DEPVGE------PV-HPRmltWirglee 2542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1785 -SAEASGKPSPSDPGSGTAAMMNSSSRGSSPnrvidegkqtvlqEPEvPSVPSITSLAEHPVAvnmapkgpppfsgvplm 1863
Cdd:PHA03247 2543 lASDDAGDPPPPLPPAAPPAAPDRSVPPPRP-------------APR-PSEPAVTSRARRPDA----------------- 2591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1864 stpmggpipppirygpppqlcgpfgprplpppfgpgmrPPLGLREFAPGVPPGKRDLPLHPREFLPGHTPFRPLGPLG-- 1941
Cdd:PHA03247 2592 --------------------------------------PPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPsp 2633
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622828951 1942 -PREYFIPGARLPPPTHGPQDYPPPPAARdLPPSGSRDDPPPASQSTSQ 1989
Cdd:PHA03247 2634 aANEPDPHPPPTVPPPERPRDDPAPGRVS-RPRRARRLGRAAQASSPPQ 2681
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1280-1650 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1280 TEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsdeaiKFKDKIKTLEKNNEILGDAAKNLRVMLE 1359
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1360 SER-EQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 1438
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1439 SKLHAElsEQIKSFEKSQKDLEVALTHKDDNINAltnciTQLNRLECESESEGQnkggndsdeLANGEvGGDQNEKMKNQ 1518
Cdd:TIGR00618 379 QHIHTL--QQQKTTLTQKLQSLCKELDILQREQA-----TIDTRTSAFRDLQGQ---------LAHAK-KQQELQQRYAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1519 IKQMMDVSRTQTAISVVEEDLKLLQ-----LKLRASVSTKCNLEDQIKKLEDDRNSLQAakaglEDECKTLRQKVEILNE 1593
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQslkerEQQLQTKEQIHLQETRKKAVVLARLLELQ-----EEPCPLCGSCIHPNPA 516
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828951 1594 LYQQKEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQK 1650
Cdd:TIGR00618 517 RQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1280-1462 |
2.80e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1280 TEQQISEKLKIIMKENTELVQKLsnyeqkikesKKHVQETRKQNMILSDEAIKFKDKIKTLE------KNNEILGDAAK- 1352
Cdd:pfam05557 370 TMSNYSPQLLERIEEAEDMTQKM----------QAHNEEMEAQLSVAEEELGGYKQQAQTLErelqalRQQESLADPSYs 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1353 -----NLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKK 1427
Cdd:pfam05557 440 keevdSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRL 519
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622828951 1428 KEQLQQEIEDWSKLHAELSE-QIKSFEKSQKDLEVA 1462
Cdd:pfam05557 520 LKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESA 555
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1341-1654 |
3.00e-03 |
|
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: 42.85 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1341 EKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAIsmnasefsEVQIALNEAKLSEEKVK--SECHRVQ 1418
Cdd:pfam01576 291 EKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL--------EEETRSHEAQLQEMRQKhtQALEELT 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1419 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEvaltHKDDNINAltncitQLNRLEC---ESE---SEGQ 1492
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE----HKRKKLEG------QLQELQArlsESErqrAELA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1493 NKGGNDSDELANgeVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEdlkLLQLKLRAsvstKCNLEDQIKKLEDDRNSLQA 1572
Cdd:pfam01576 433 EKLSKLQSELES--VSSLLNEAEGKNIKLSKDVSSLESQLQDTQE---LLQEETRQ----KLNLSTRLRQLEDERNSLQE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1573 AkagLEDECKTlRQKVEILNELYQQKEMALQKKLSQEEYErqerehrLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 1652
Cdd:pfam01576 504 Q---LEEEEEA-KRNVERQLSTLQAQLSDMKKKLEEDAGT-------LEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
..
gi 1622828951 1653 RS 1654
Cdd:pfam01576 573 KT 574
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1698-1993 |
3.33e-03 |
|
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: 42.45 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1698 TQKMAMLQEEPVIVKPMPGRPNTQNPPRRGPLSQNGSFGPSPvSGGECSPPLTVEPPVRPLSATLS-------RRDMPRS 1770
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQG-SPATSQPPNQTQSTAAPHTLIQQtptlhpqRLPSPHP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1771 EFGSVDGPLPHPRWSAEASGKPS-----------------------PSDPGSGTAAMMNSSSRGSSPNRVIDEGKQTVLQ 1827
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLPQPSlhgqmppmphslqtgpshmqhpvPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1828 EPEVPSVPSITSLAEHPVA---VNMAPKGPPPFSGVPLMSTPMGGPIPPPIRYGPPPQL--------CGPFGPRPLPPPF 1896
Cdd:pfam03154 328 PPSQSQLQSQQPPREQPLPpapLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMnsnlppppALKPLSSLSTHHP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1897 GPGMRPPLGLREFAPGVPPGkrdlPLHPreflPGHTPFRPLGPLG----PREYFIPGARLPP-PTHGPQDYPPPPAardL 1971
Cdd:pfam03154 408 PSAHPPPLQLMPQSQQLPPP----PAQP----PVLTQSQSLPPPAashpPTSGLHQVPSQSPfPQHPFVPGGPPPI---T 476
|
330 340
....*....|....*....|..
gi 1622828951 1972 PPSGsrddpPPASQSTSQDCSQ 1993
Cdd:pfam03154 477 PPSG-----PPTSTSSAMPGIQ 493
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1267-1441 |
3.36e-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: 41.72 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1267 RTVLVVKSRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMilsdeaikfkdkiKTLEKNNEI 1346
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-------------KLLEYITEL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1347 lgdaaKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEA-----KLSEEKVKSECHRVQEEN 1421
Cdd:pfam15905 232 -----SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcklleSEKEELLREYEEKEQTLN 306
|
170 180
....*....|....*....|
gi 1622828951 1422 ARLKKKKEQLQQEIEDWSKL 1441
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
|
|
| SH3 |
smart00326 |
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
48-103 |
3.78e-03 |
|
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: 37.52 E-value: 3.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828951 48 YRGEALEDFTGPDCRFVNFKKGDPVYVYYKLARAWpevWAGSVGR-IFGYFPKDLIQ 103
Cdd:smart00326 3 PQVRALYDYTAQDPDELSFKKGDIITVLEKSDDGW---WKGRLGRgKEGLFPSNYVE 56
|
|
| DUF3824 |
pfam12868 |
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ... |
1914-1985 |
3.89e-03 |
|
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.
Pssm-ID: 372351 [Multi-domain] Cd Length: 145 Bit Score: 39.72 E-value: 3.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828951 1914 PPGKRDLPLHPREFLPGHTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAArdLPPSGSRDDPPPASQ 1985
Cdd:pfam12868 62 PPSPAGPYASQGQYYPETNYFPPPPGSTPQPPVDPQPNAPPPPYNPADYPPPPGA--APPPQPYQYPPPPGP 131
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1758-1982 |
4.23e-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: 41.72 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1758 LSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKPSPSdpgsgTAAMMNSSSRGSSPnrvidegKQTVLQEPEVPSVPSI 1837
Cdd:pfam15279 75 LSDCRRKSASPASTRSESVSPGPSSSASPSSSPTSSNS-----SKPLISVASSSKLL-------APKPHEPPSLPPPPLP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1838 TSLAEHPVAVNMAPKGPPPfsGVPLMSTPMGGPIPPPIRYGPPPQLcgpfgprpLPPPFGPGMRPPLgLREFAPGVPPGK 1917
Cdd:pfam15279 143 PKKGRRHRPGLHPPLGRPP--GSPPMSMTPRGLLGKPQQHPPPSPL--------PAFMEPSSMPPPF-LRPPPSIPQPNS 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1918 RDLPLHPREFLPGHTPFRPLGPLGPREYFIP-GARLPPPTHGPqdYPPPPAardLPPSGSRDDPPP 1982
Cdd:pfam15279 212 PLSNPMLPGIGPPPKPPRNLGPPSNPMHRPPfSPHHPPPPPTP--PGPPPG---LPPPPPRGFTPP 272
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
1902-1995 |
4.79e-03 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 41.48 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1902 PPLGLRE-FAPGVPPGKRDLPLHPREFLPghtpfrPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDP 1980
Cdd:PHA03291 195 PRLGPADvFVPATPRPTPRTTASPETTPT------PSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPAPPTPGGGEAP 268
|
90
....*....|....*
gi 1622828951 1981 PPASQSTSQDCSQAL 1995
Cdd:PHA03291 269 PANATPAPEASRYEL 283
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1271-1458 |
5.04e-03 |
|
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: 40.47 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1271 VVKSRVYQVTEQQIseklkiIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK--------FKDKIKTLEK 1342
Cdd:cd21116 10 LVQAYVTAILNQPN------INLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgynntfqsYYPDLIELAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1343 N-NEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEEN 1421
Cdd:cd21116 84 NlIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQI 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622828951 1422 ARLKKKKEQLQQeieDWSKLHAELSEQIKSFEKSQKD 1458
Cdd:cd21116 164 DAAIDALEKLSN---DWQTLDSDIKELITDLEDAESS 197
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1288-1619 |
5.04e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1288 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQ-----------NMILSDEAI--KFKDKIKTLEKNNEILG---DAA 1351
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesaKVCLTDVTImeRFQMELKDVERKIAQQAaklQGS 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1352 KNLRVMLESEREQNVK-------------NQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQ 1418
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKqheldtvvskielNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1419 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNRLECESESEGQNKGGND 1498
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1499 SDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQ-----AA 1573
Cdd:TIGR00606 976 ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQvlqmkQE 1055
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622828951 1574 KAGLEDECKTL-RQKVEILNEL--YQQKEMALQKKLSQEEYERQEREHR 1619
Cdd:TIGR00606 1056 HQKLEENIDLIkRNHVLALGRQkgYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1282-1516 |
5.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1282 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLrvmlese 1361
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1362 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 1440
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828951 1441 LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMK 1516
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1285-1458 |
6.77e-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: 40.77 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1285 SEKLKIIMKENTELVQKLSNYEqkikeSKKHVQETRKQNMilsdeaikfKDKIKTLEKNNEILgdaaknlrvmlESEREQ 1364
Cdd:smart00787 108 SPDVKLLMDKQFQLVKTFARLE-----AKKMWYEWRMKLL---------EGLKEGLDENLEGL-----------KEDYKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1365 NVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSE-----EKVKSECHRVQEEN---ARLKKKKEQLQQEIE 1436
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTEldrakEKLKKLLQEIMIKVkklEELEEELQELESKIE 242
|
170 180
....*....|....*....|..
gi 1622828951 1437 DWSKLHAELSEQIKSFEKSQKD 1458
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1281-1525 |
8.34e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1281 EQQISEKLKIIMKENTELVQKLSnyEQKIKESKKHVQETRK--QNMILSDEAIKFKDKIKTLEKN-----NEILGDAAKN 1353
Cdd:PTZ00440 1030 DKLIKEKGKEIEEKVDQYISLLE--KMKTKLSSFHFNIDIKkyKNPKIKEEIKLLEEKVEALLKKidenkNKLIEIKNKS 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1354 LRVMLESEREQNvKNQDLISENKKSIEKLKDAISMNASEFSEVQIAL------NEAKLSEEKVKSE--CHRVQEENARLK 1425
Cdd:PTZ00440 1108 HEHVVNADKEKN-KQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDitlnevNEIEIEYERILIDhiVEQINNEAKKSK 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1426 KKKEQLQQEIEDWSKLHAELSEQIKS----FEKSQKDLEvaLTHKDDNINALtncITQLNRLECESESEGQNK--GGNDS 1499
Cdd:PTZ00440 1187 TIMEEIESYKKDIDQVKKNMSKERNDhlttFEYNAYYDK--ATASYENIEEL---TTEAKGLKGEANRSTNVDelKEIKL 1261
|
250 260
....*....|....*....|....*.
gi 1622828951 1500 DELANGEVGGDQNEKMKNQIKQMMDV 1525
Cdd:PTZ00440 1262 QVFSYLQQVIKENNKMENALHEIKNM 1287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1297-1411 |
9.44e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1297 ELVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTL-----EKNNEILGDA----AKNLRVMLESERE 1363
Cdd:PRK00409 520 ELIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAQQAIKEAkkeaDEIIKELRQLQKG 599
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622828951 1364 Q--NVKNQDLIsENKKSIEKLKDAISMNASEFSEVQIALNEAklseEKVK 1411
Cdd:PRK00409 600 GyaSVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVG----DEVK 644
|
|
| LPD_N |
smart00638 |
Lipoprotein N-terminal Domain; |
910-1083 |
9.69e-03 |
|
Lipoprotein N-terminal Domain;
Pssm-ID: 214755 [Multi-domain] Cd Length: 574 Bit Score: 40.79 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 910 HTSVEPEYSYKREDLLIisSFFKE--QQSLQRFKRYLNAYEMEALLQEMSSKLKSAQQESLPYNMEKVLDKVFRASESQI 987
Cdd:smart00638 251 PSSPPPGEPRNRGSLVY--EFESTnqQLPIRLLKAPSNEVQIVEVLKHLVQDIASDVQEPAAAKFLRLVRLLRTLSEEQL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828951 988 LSIAEKMldayvdEHRDMGMQVIFEEAAVLDD----IQDLIYFVRYKHSTAEETATLV-----MAP-PVEEglggAMEEM 1057
Cdd:smart00638 329 EQLWRQL------YEKKKKARRIFLDAVAQAGtppaLKFIKQWIKNKKITPLEAAQLLavlphTARyPTEE----ILKAL 398
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622828951 1058 QPLHEDNFSQEN-----TAELN-------VQVSEEPTH 1083
Cdd:smart00638 399 FELAESPEVQKQpylreSALLAygslvrrYCVNTPSCP 436
|
|
| |
