|
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 |
9.29e-45 |
|
Src Homology 3 domain of Melanoma Inhibitory Activity 3 protein; MIA3, also called TANGO or TANGO1, acts as a tumor suppressor of malignant melanoma. It is downregulated or lost in melanoma cells lines. Unlike other MIA family members, MIA3 is widely expressed except in hematopoietic cells. MIA3 is an ER resident transmembrane protein that is required for the loading of collagen VII into transport vesicles. SNPs in the MIA3 gene have been associated with coronary arterial disease and myocardial infarction. MIA3 contains an N-terminal SH3-like domain, similar to MIA. It is a member of the recently identified family that also includes MIA, MIAL, and MIA2. MIA is a single domain protein that adopts a SH3 domain-like fold; it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands.
Pssm-ID: 212826 Cd Length: 73 Bit Score: 156.16 E-value: 9.29e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387212238 37 LCADEECSMLMYRGEALEDFTGPDCRFVNFKKGDTVYVYYKLAGGSPEVWAGSVGHTFGYFPKDLIQVVHEYT 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 |
4.95e-37 |
|
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: 134.15 E-value: 4.95e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212238 37 LCADEECSMLMYRGEALEDFTGPDCRFVNFKKGDTVYVYYKLAGGSPEVWAGSVGH---TFGYFPKDLIQVVHEYT 109
Cdd:cd11760 1 LCADAECSNPISRARALEDYHGPDCRFLNFKKGDTIYVYSKLAGERQDLWAGSVGGdagLFGYFPKNLVQELKVYE 76
|
|
| SH3_MIA2 |
cd11892 |
Src Homology 3 domain of Melanoma Inhibitory Activity 2 protein; MIA2 is expressed ... |
38-109 |
1.04e-26 |
|
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: 104.92 E-value: 1.04e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 38 CADEECSMLMYRGEALEDFTGPDCRFVNFKKGDTVYVYYKLAGGSPEVWAGSVGHTFGYFPKDLIQVVHEYT 109
Cdd:cd11892 2 CGDPECERLMSRVQAIRDYRGPDCRYLSFKKGDEIIVYYKLSGKREDLWAGSTGKEFGYFPKDAVKVEEVYI 73
|
|
| MIA |
cd11890 |
Melanoma Inhibitory Activity protein; MIA is a single domain protein that adopts a Src ... |
36-124 |
1.88e-20 |
|
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: 88.01 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 36 KLCADEECSMLMYRGEALEDFTGPDCRFVNFKKGDTVYVYYKLAGGSPEVWAGSVGHTF--------GYFPKDLIQVVHE 107
Cdd:cd11890 2 KLCADQECSHPISIAVALQDYMAPDCRFIPIQRGQVVYVFSKLKGRGRLFWGGSVQGDYygeqaarlGYFPSSIVQEDQY 81
|
90
....*....|....*..
gi 1387212238 108 YTQEELQVPTDETDFVC 124
Cdd:cd11890 82 LKPGKVEVKTDKWDFYC 98
|
|
| MIAL |
cd11891 |
Melanoma Inhibitory Activity-Like protein; MIAL is specifically expressed in the cochlea and ... |
37-108 |
9.08e-19 |
|
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: 82.60 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 37 LCADEECSMLMYRGEALEDFTGPDCRFVNFKKGDTVYVYYKLA--GGSPEVWAGSVGH--------TFGYFPKDLIQVVH 106
Cdd:cd11891 1 LCADEECVYAISLARAEDDYNAPDCRFINIKKGQLIYVYSKLVkeNGAGEFWSGSVYSeryvdqmgIVGYFPSNLVKEQT 80
|
..
gi 1387212238 107 EY 108
Cdd:cd11891 81 VY 82
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1209-1588 |
1.05e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.06 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1209 TEQQISEKLKNIMKENAELVQK------LSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIkslEETNEILGDTAKS 1282
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLESerEQNAKNQdlISENKKSIEKLKDVISVNASEFSEVQIALNEakLSEEKVKSECHRVQEENARLKKKKEQLQQ 1362
Cdd:TIGR04523 255 LNQLKDE--QNKIKKQ--LSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1363 EIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcESESEDQNKGGSESdelangevggdRSE 1442
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLES-----------QIN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1443 KVKNQIKQMMDVSRT-QTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILN 1521
Cdd:TIGR04523 395 DLESKIQNQEKLNQQkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212238 1522 ELYQQKEMALQKKlsqeEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTErSFKNQI 1588
Cdd:TIGR04523 475 RSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-SEKKEK 536
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1209-1593 |
1.89e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.91 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1209 TEQQISEKLKNIMKENAELVQKLSSYEQKIK----ESKKHVQETKKQNMILSDEAIKFKDKIKSLEetNEILGDTAKSLR 1284
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1285 AMLESEREQ--NAKNQdlISENKKSIEKLKDVISV-------NASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 1355
Cdd:TIGR04523 314 SELKNQEKKleEIQNQ--ISQNNKIISQLNEQISQlkkeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1356 KKEQLQQEIKDWSKSHAELSEQIRSF-------EKSQKDLEVALTHKDDNINALTNCITQLNRL--DCESESEDQNKggs 1426
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLET--- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1427 esdelaNGEVGGDRSEKVKNQIKQmmdvsrTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVL 1506
Cdd:TIGR04523 469 ------QLKVLSRSINKIKQNLEQ------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1507 EDECKTLRQKVEILN-----ELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTE 1581
Cdd:TIGR04523 537 ESKISDLEDELNKDDfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
410
....*....|..
gi 1387212238 1582 RSFKNQIATHEK 1593
Cdd:TIGR04523 617 KELEKAKKENEK 628
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1215-1533 |
6.73e-13 |
|
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: 74.24 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1215 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKK---------------QNMILSDEAIKFKDKIKSLEETNEILGDT 1279
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1280 AKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 1359
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1360 LQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKddninaltncITQLNRLDCESESEDQNKGGSESD-----ELANG 1434
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----------EQLEEELLAKKKLESERLSSAAKLkeeelELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1435 EVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLR 1514
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*....
gi 1387212238 1515 QKVEILNELYQQKEMALQK 1533
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQK 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1198-1518 |
9.87e-13 |
|
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: 73.94 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1198 VLAVKSRVYQVTEQ--QISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEI 1275
Cdd:TIGR02168 672 ILERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1276 LGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 1355
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1356 KKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKggseSDELANGE 1435
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1436 vgGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTkcNLEDQIKKLEEDRSSLQSAktvlEDECKTLRQ 1515
Cdd:TIGR02168 908 --SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLEN 979
|
...
gi 1387212238 1516 KVE 1518
Cdd:TIGR02168 980 KIK 982
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1203-1597 |
1.74e-12 |
|
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: 72.83 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1203 SRVYQVTEQQISEKLKNIMKENAELVQKlssyEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKS 1282
Cdd:pfam05483 77 SRLYSKLYKEAEKIKKWKVSIEAELKQK----ENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECH-RVQEENARLKKKKEQLQ 1361
Cdd:pfam05483 153 TRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1362 QEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTncitQLNRLDCESESEDQNKGGSESDELangevggdrs 1441
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDENLKELIEKKDHLTKEL---------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1442 EKVKnqikqmMDVSRTQTAISVVEEDLKLlqcklraSMSTKCNL----EDQIKKLEEDRSS-------LQSAKTVLEDEC 1510
Cdd:pfam05483 299 EDIK------MSLQRSMSTQKALEEDLQI-------ATKTICQLteekEAQMEELNKAKAAhsfvvteFEATTCSLEELL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1511 KTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADE-KAVLAAEEVKTY-KRRIEEMEDELQKTERSFKNQI 1588
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDeKKQFEKIAEELKGKEQELIFLL 445
|
....*....
gi 1387212238 1589 ATHEKKAHD 1597
Cdd:pfam05483 446 QAREKEIHD 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1209-1522 |
4.04e-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: 68.12 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1209 TEQQISE---KLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRA 1285
Cdd:TIGR04523 333 NNKIISQlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1286 MLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIK 1365
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1366 DWSKSHAELSEQIRSFEKSQKDLEvalthkdDNINALTNCITQLNRLDCESESEDQNKggseSDELANGEVGGDRS--EK 1443
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDL----EDELNKDDFELKKEnlEK 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1444 VKNQIKQMMD-VSRTQTAISVVEEDLKLLQCKLRAS-----------MSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECK 1511
Cdd:TIGR04523 562 EIDEKNKEIEeLKQTQKSLKKKQEEKQELIDQKEKEkkdlikeieekEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
330
....*....|.
gi 1387212238 1512 TLRQKVEILNE 1522
Cdd:TIGR04523 642 KLKQEVKQIKE 652
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1644-1891 |
9.72e-11 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.66 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1644 PGRPNTQNPPRRGPLSqNGSFGPSPVSGGECSPPLTADPPA-RPLSATLNRREMPRSEFDPE---SGAAPTVNSSSRSSS 1719
Cdd:PHA03247 2748 PATPGGPARPARPPTT-AGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPaavLAPAAALPPAASPAG 2826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1720 PSKVMDEGKQTVPQEPEGPSVPSIP---SLAE-HPVSVSMAAKGPPPFPGT-----------PLMSSPVGGPLLPPIRYG 1784
Cdd:PHA03247 2827 PLPPPTSAQPTAPPPPPGPPPPSLPlggSVAPgGDVRRRPPSRSPAAKPAAparppvrrlarPAVSRSTESFALPPDQPE 2906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1785 PPPQlcgpfgpRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLPLDPR-----EFLPPGHAPFRPLGSLGPREYFFPGTRL 1859
Cdd:PHA03247 2907 RPPQ-------PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTtdpagAGEPSGAVPQPWLGALVPGRVAVPRFRV 2979
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387212238 1860 PPPNHG-PQDYPPSSAARDLPPSG-----------SRDEPPPAS 1891
Cdd:PHA03247 2980 PQPAPSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1200-1594 |
1.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1200 AVKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKqnmilSDEAIKFKDKIKSLEETNEILGDT 1279
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEA 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1280 AKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKK 1357
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1358 EQLQQEIKDWSKSHAELSEQIRSFEKSQKdLEVALTHKDDNINALTNciTQLNRLDCESESEDQNKGGSESDELANGEVG 1437
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKK-AEEAKKAEEDKNMALRK--AEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1438 GDRSEKVK-NQIKQMMDVSRTQTAISVVEEDLKLLQCKLR-ASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDEcktlRQ 1515
Cdd:PTZ00121 1614 KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KK 1689
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387212238 1516 KVEILNELYQQKEMALQkkLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKK 1594
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKE 1765
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1642-1906 |
3.37e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 65.73 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1642 PMPGRPNTQNPPRRGPLSQNGSFGPSPVsgGECSPPLTADPPA-RPLSATL-NRREMPRSEFDPESGAAPTVNSSSRSSS 1719
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRPRRARRLGRAA--QASSPPQRPRRRAaRPTVGSLtSLADPPPPPPTPEPAPHALVSATPLPPG 2724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1720 PSkvmdEGKQTVPQEPEGPSVPSIPSLAEHPVSVsmAAKGPPPFPGTPLMSSPVGGPLLPPIRYGPPPQLCGPFGPRPLP 1799
Cdd:PHA03247 2725 PA----AARQASPALPAAPAPPAVPAGPATPGGP--ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL 2798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1800 PPFGPGMRPPLGLREYAPGVPPGKRDLPLDPREFLPPGHAPFRPLGSLGPRE----YFFPG---TRLPPpnhgPQDYPPS 1872
Cdd:PHA03247 2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggSVAPGgdvRRRPP----SRSPAAK 2874
|
250 260 270
....*....|....*....|....*....|....
gi 1387212238 1873 SAARDLPPSGSRDEPPPASQGASQDCSPALKQSP 1906
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERP 2908
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1642-1894 |
6.60e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.96 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1642 PMPGRPNTQNPPrrgPLSQNGSFGPSPVSGGECSPPLTADPPARP------LSATLNRREMPRSEFDPESGAAPTVNSSS 1715
Cdd:PHA03247 2702 PPPPPTPEPAPH---ALVSATPLPPGPAAARQASPALPAAPAPPAvpagpaTPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1716 RSSSPSKvmdegKQTVPQEPEGPSVPSIPSLAEHPVSVSMAAKGPPPF--PGTPLMSSPVGGPLLPPIRYGPPPQ----- 1788
Cdd:PHA03247 2779 PPRRLTR-----PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAasPAGPLPPPTSAQPTAPPPPPGPPPPslplg 2853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1789 --------LCGPFGPRPLPPPFGPGMRPPLGlREYAPGVPPGKRDLPL--DPREFLPPGHAPFRPLGSlgPREYFFPGTR 1858
Cdd:PHA03247 2854 gsvapggdVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALppDQPERPPQPQAPPPPQPQ--PQPPPPPQPQ 2930
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387212238 1859 LPPPNHGPQDYPPSSAARDLPPSGSRDEPPPASQGA 1894
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1238-1581 |
1.96e-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: 63.15 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1238 IKESKKHVQETKKQnmilSDEAIKFKDKIKSLEETN-EILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVIS 1316
Cdd:TIGR02168 195 LNELERQLKSLERQ----AEKAERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1317 VNASEFSEVQIALNEAKlseekvkSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKD 1396
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1397 DNINALTNCItqlnrldcESESEDQNKGGSESDELANgevggdRSEKVKNQIKQMmdvsrtQTAISVVEEDLKLLQCKLR 1476
Cdd:TIGR02168 344 EKLEELKEEL--------ESLEAELEELEAELEELES------RLEELEEQLETL------RSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1477 ASMSTKCNLEDQIKKLEEDRSSLQSAKTvlEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQEREQRLSAADEKA 1556
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEE----LQEELERLEEALEELREELEEAEQAL 477
|
330 340
....*....|....*....|....*
gi 1387212238 1557 VLAAEEVKTYKRRIEEMEDELQKTE 1581
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1210-1533 |
2.65e-09 |
|
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: 62.35 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLKNIMKE--NAELVQK-----LSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETneilgdtAKS 1282
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD-------LSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 1362
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1363 EIKD-----------------WSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRL--------- 1412
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLkdeqnkikk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1413 ---DCESESEDQNKGGSE-SDELANGEVggdRSEKVKNQIKQMMDvSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQ 1488
Cdd:TIGR04523 268 qlsEKQKELEQNNKKIKElEKQLNQLKS---EISDLNNQKEQDWN-KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1387212238 1489 IKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 1533
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1210-1581 |
2.98e-09 |
|
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: 62.39 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKqnmilsdeaikfkdKIKSLEETNEILGDTAKSLRAMLES 1289
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR--------------KIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALN--EAKLSEEKVksechrvqeenarlkkkkEQLQQEIKDW 1367
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlEARLSHSRI------------------PEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1368 SKSHAELSEQIRSFEKSqkdlevalthkddninaltncitqLNRLDCESESEDqnkggsesDELANGEVGGDRSEKVKNQ 1447
Cdd:TIGR02169 804 EEEVSRIEARLREIEQK------------------------LNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1448 IKQMMDVSRTQtaISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQK 1527
Cdd:TIGR02169 852 IEKEIENLNGK--KEELEEELEELEAALR-------DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1528 EMALQKKLSQEEYERQEREQRLSAADEKAVLaaeevKTYKRRIEEMEDELQKTE 1581
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDVQAELQRVEEEIRALE 971
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1213-1636 |
1.03e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1213 ISEKLKNIMKENAELVQKLSSYEQKIKESKKhVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLEsERE 1292
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1293 QNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIKdwsksh 1371
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1372 aELSEQIRSFEKSQKDLEvalthkdDNINALTN----CITQLNRLDCESESEDQNKGGSESDELANG-EVGGDRSEKVKN 1446
Cdd:PRK03918 409 -KITARIGELKKEIKELK-------KAIEELKKakgkCPVCGRELTEEHRKELLEEYTAELKRIEKElKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1447 QIKQMMDVSRTQTAISVVEEDLKLLQcKLRASMStKCNLEDqIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQ 1526
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLK-ELEEKLK-KYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1527 KEmALQKKLSqeeyerqereqrlSAADEKAVLAAEEVKTYKRRIEEMEDELQKTErsfknqiathekKAHDNWLKARAAE 1606
Cdd:PRK03918 558 LA-ELEKKLD-------------ELEEELAELLKELEELGFESVEELEERLKELE------------PFYNEYLELKDAE 611
|
410 420 430
....*....|....*....|....*....|
gi 1387212238 1607 RAIAEEKREAANLRhklLELTQKMAMMQEE 1636
Cdd:PRK03918 612 KELEREEKELKKLE---EELDKAFEELAET 638
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1209-1649 |
2.55e-08 |
|
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: 58.96 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1209 TEQQISEKLKNIMKE-NAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAiKFKDKIKSLEETNEILGDTAKSLRAML 1287
Cdd:pfam05483 367 TEQQRLEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE-KLLDEKKQFEKIAEELKGKEQELIFLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1288 ESeREQNAKNQDLISENKKSIEKLKdvisvnASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQL------- 1360
Cdd:pfam05483 446 QA-REKEIHDLEIQLTAIKTSEEHY------LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkh 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1361 QQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNInaltncITQLNRLDCESESEDQNKGGSESDELANGEVGGDR 1440
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF------IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1441 SEKVKNQIKQMMDVSRTqtaISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDrssLQSAKTVLEDECKTLRQKVEIl 1520
Cdd:pfam05483 593 ENKCNNLKKQIENKNKN---IEELHQENKALKKKGSAENKQLNAYEIKVNKLELE---LASAKQKFEEIIDNYQKEIED- 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1521 nelyqqkemalqKKLSQEEYERQEREQRLSAaDEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEKKAHDNWL 1600
Cdd:pfam05483 666 ------------KKISEEKLLEEVEKAKAIA-DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1387212238 1601 KARAAERAIAEEKREAANLRHKLLELTQKMAMMQEEPVIVKpMPGRPNT 1649
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLK-MEAKENT 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1210-1636 |
6.30e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEkLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILsDEAIKFKDKIKSLEETNEILGDTAKSLRAMLES 1289
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREqnaknqdlISENKKSIEKLKDvisvnasEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWS 1368
Cdd:COG4717 155 LEE--------LRELEEELEELEA-------ELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1369 KSHAELSEQIRSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNRLDCESESEDQNK 1423
Cdd:COG4717 220 EELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1424 GGSESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAK 1503
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1504 TVLEDEckTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAA-EEVKTYKRRIEEMEDELQKTER 1582
Cdd:COG4717 380 GVEDEE--ELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1583 SFKNQIATHEKkahdnwlkaraaeraiaeeKREAANLRHKLLELTQKMAMMQEE 1636
Cdd:COG4717 457 ELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1196-1582 |
8.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1196 RTVLAVKSRVYQVTEQQISEKlknimkENAELVQKLSSYEQKIKESK---KHVQETKKQ--------NMILS-------- 1256
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerree 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1257 ----DEAI-KFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNE 1331
Cdd:PRK02224 253 letlEAEIeDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1332 AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALthkDDNINALTNCITQLNR 1411
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1412 LDCESESEDQNKGGSESDElANGEVGGDRSEKVKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQcKLRASMSTk 1482
Cdd:PRK02224 410 AEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1483 cnLEDQIKKLEEDRSSLQSAKTvLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEK------- 1555
Cdd:PRK02224 487 --LEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaea 563
|
410 420 430
....*....|....*....|....*....|
gi 1387212238 1556 ---AVLAAEEVKTYKRRIEEMEDELQKTER 1582
Cdd:PRK02224 564 eeeAEEAREEVAELNSKLAELKERIESLER 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1213-1522 |
1.10e-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: 57.39 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1213 ISEKLKN-----IMKENAELVQKLSS----YEQKIKESKKHVQETKKQNMI-----LSDEAIKFKDKI----KSLEETNE 1274
Cdd:TIGR02169 193 IDEKRQQlerlrREREKAERYQALLKekreYEGYELLKEKEALERQKEAIErqlasLEEELEKLTEEIseleKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1275 ILGDTAKSLRAMleSEREQNAKNQDlISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK 1354
Cdd:TIGR02169 273 LLEELNKKIKDL--GEEEQLRVKEK-IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1355 KKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKggseSDELANG 1434
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL----SEELADL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1435 EVGGDRSEKVKNQIKQMMD-----VSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDE 1509
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEdkaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
330
....*....|...
gi 1387212238 1510 CKTLRQKVEILNE 1522
Cdd:TIGR02169 506 VRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1265-1578 |
1.36e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1265 KIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDvisvnasEFSEVQIALNEAKLSEEKVKSECH 1344
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1345 RVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDdninaltncitqlnrldcesESEDQNKG 1424
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE--------------------AELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1425 GSESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKllqcklrasmstkcNLEDQIKKLEEDRSSLQSAKT 1504
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE--------------ALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1505 VLEDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQ 1578
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
49-105 |
1.63e-07 |
|
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 49.52 E-value: 1.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212238 49 RGEALEDFTGPDCRFVNFKKGDTVYVYYKLAGGSpevWAGSVGHTFGYFPKDLIQVV 105
Cdd:pfam07653 1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGKDNDGW---WEGETGGRVGLVPSTAVEEI 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1211-1411 |
2.39e-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: 55.16 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEET-NEILGDTAKSLRAMLES 1289
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREQNAK---NQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKd 1366
Cdd:COG4942 117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA- 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387212238 1367 wskshaELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNR 1411
Cdd:COG4942 196 ------ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1214-1534 |
2.79e-07 |
|
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: 55.88 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1214 SEKLKNI---------MKENAELVQKLSSYEQKIKESKKHVQETKKQNMilsdeaiKFKDKIKSLEETNEILGDTAKSLR 1284
Cdd:pfam05483 482 KEKLKNIeltahcdklLLENKELTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1285 AMLESEREQNAKNQDLISENKKSIEklkdvisvnasefSEVQIALNEAKLSEEKvkseCHRVQEENARLKKKKEQLQQEI 1364
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIE-------------YEVLKKEKQMKILENK----CNNLKKQIENKNKNIEELHQEN 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1365 KDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCIT---QLNRLDCESESEDQNKGGSESDELANGEVGGDRs 1441
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK- 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1442 eKVKNQIKQM---MDVSRTQTAISVVEED--LKLLQCKLRASMSTKCNLEDQIKKLeedRSSLQSAKTVLEDEcktlRQK 1516
Cdd:pfam05483 697 -RCQHKIAEMvalMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI---KAELLSLKKQLEIE----KEE 768
|
330
....*....|....*...
gi 1387212238 1517 VEILNELYQQKEMALQKK 1534
Cdd:pfam05483 769 KEKLKMEAKENTAILKDK 786
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1361-1636 |
3.08e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1361 QQEIKDWSKSHAELSEQIRSFEKSQKDLEVALThkddninALTNCITQLNRLdcesesedqnkGGSESDELANGEVGGDR 1440
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELE-------ELEEELEQLRKE-----------LEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1441 SEKVKNQIKQMMDvsRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEIL 1520
Cdd:TIGR02168 738 LEAEVEQLEERIA--QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1521 NELYQQKEMA---LQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQkterSFKNQIATHEKKAHD 1597
Cdd:TIGR02168 816 NEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE----ALLNERASLEEALAL 891
|
250 260 270
....*....|....*....|....*....|....*....
gi 1387212238 1598 NWLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 1636
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1214-1595 |
6.49e-07 |
|
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: 55.06 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1214 SEKLKNIMKENAELVQKLSSYE------------QKIKESKKHV--QETK-----------KQNMILSDEAIKFKD---- 1264
Cdd:TIGR01612 1388 SEKLIKKIKDDINLEECKSKIEstlddkdideciKKIKELKNHIlsEESNidtyfknadenNENVLLLFKNIEMADnksq 1467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1265 ---KIKSLEET-------NEILGDTAKSLRAMLESEreqnaKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKl 1334
Cdd:TIGR01612 1468 hilKIKKDNATndhdfniNELKEHIDKSKGCKDEAD-----KNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAK- 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1335 seekVKSECHRVQEENARLKKK----KEQLQQEIKDWSKSHAELSEQIRSFEKSQK---DLEVALTHKDDNINALTNCIT 1407
Cdd:TIGR01612 1542 ----TKKDSEIIIKEIKDAHKKfileAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKaaiDIQLSLENFENKFLKISDIKK 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1408 QLNrlDCESESEdqnkggsesdelangevggdrseKVKNQIKQMmDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLED 1487
Cdd:TIGR01612 1618 KIN--DCLKETE-----------------------SIEKKISSF-SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1488 QIKKLEEDRSSLQSAKTVLEDECKTLRQK-VEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTY 1566
Cdd:TIGR01612 1672 KKKELDELDSEIEKIEIDVDQHKKNYEIGiIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEY 1751
|
410 420
....*....|....*....|....*....
gi 1387212238 1567 KRRIEEMEDELQKTERSFKNQIATHEKKA 1595
Cdd:TIGR01612 1752 NTEIGDIYEEFIELYNIIAGCLETVSKEP 1780
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1203-1576 |
7.94e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 54.31 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1203 SRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSleetneilgdtakS 1282
Cdd:COG5022 852 GRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSS-------------D 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLESEREQNAKNQDLISENKKSIEKLKDVISVnasefsEVQIALNEaklseekVKSECHRVQEENARLKKKKEQLQ- 1361
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL------PELNKLHE-------VESKLKETSEEYEDLLKKSTILVr 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1362 ------QEIKDWSKSHAELSEQIRSFEKSQKDLEVaLTHKDDNINALTNCITQlnrldcESESEDQNKGGSES---DELA 1432
Cdd:COG5022 986 egnkanSELKNFKKELAELSKQYGALQESTKQLKE-LPVEVAELQSASKIISS------ESTELSILKPLQKLkglLLLE 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1433 NGEVGG---------DRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQC--------KLRASMStKCNLEDQIKKleed 1495
Cdd:COG5022 1059 NNQLQArykalklrrENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkpanvlqFIVAQMI-KLNLLQEISK---- 1133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1496 rsSLQSAKTVLEDECKTLRQKVEILNELYQQKemALQKKLSQEEYERQEREQRLSAA--DEKAVLAAEEVKTYKRRIEEM 1573
Cdd:COG5022 1134 --FLSQLVNTLEPVFQKLSVLQLELDGLFWEA--NLEALPSPPPFAALSEKRLYQSAlyDEKSKLSSSEVNDLKNELIAL 1209
|
...
gi 1387212238 1574 EDE 1576
Cdd:COG5022 1210 FSK 1212
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1201-1528 |
8.27e-07 |
|
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: 54.30 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1201 VKSRVYQVTEQQISEKLKNIMKENAE-LVQKLSSYE--QKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILG 1277
Cdd:pfam05911 441 VPVSSKDISLGKSLSWLQSRISVILEsHVTQKSIGKilEDIRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1278 DTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVI---SVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK 1354
Cdd:pfam05911 521 VVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDFVeglSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLE 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1355 KKKEQLQqEIKDWSKSH-------AELSEQIRSFEKSQKD--LEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGG 1425
Cdd:pfam05911 601 DFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKVtlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLK 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1426 SESDELANGEVGGDRSEKVKNQIKQMMDVSRTQTAIS---VVEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSA 1502
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlqESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETR 759
|
330 340
....*....|....*....|....*..
gi 1387212238 1503 KTVLEDECKTLRQKVEIL-NELYQQKE 1528
Cdd:pfam05911 760 LTELEAELNELRQKFEALeVELEEEKN 786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1211-1601 |
1.12e-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: 53.97 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHV-------QETKKQNMILSDEAIKFKDKIKSLeetneiLGDTAKSL 1283
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1284 RAmLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 1358
Cdd:pfam15921 391 KE-LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1359 ------QLQQEIKDWSKSHAELSEQIRSFEKSQK---DLEVALTHKDDNINALTNCITQL-NRLDCE--------SESED 1420
Cdd:pfam15921 463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrSRVDLKlqelqhlkNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1421 QNKGGSESDELANGEVGGDRS-EKVKNQIKQMMDV----SRTQTAISV----VEEDLKLLQCKLRASMSTKCNLEDQIKK 1491
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1492 LEEDRSSLQSAKTVLEDECKtlrQKVEILNELYQQKEMALQkklsqeeyerqereqrlsaadekavlaaeEVKTYKRRIE 1571
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLN-----------------------------EVKTSRNELN 670
|
410 420 430
....*....|....*....|....*....|
gi 1387212238 1572 EMEDELQKTERSFKNQiaTHEKKAHDNWLK 1601
Cdd:pfam15921 671 SLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1230-1582 |
1.65e-06 |
|
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: 53.53 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1230 KLSSYEQKIKESKKHVQETKKQNMILSDE---AIKFKDKIKSLEETNeilgdtAKSLRAMLESEREQNAKNQDLISENKK 1306
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKREYE------GYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1307 SIEKLKDVISVNASEFSEVQIALNEA-----KLSEEK---VKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQI 1378
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELnkkikDLGEEEqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1379 RSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRLDCESESEDQnKGGSESDELANGEVggdRSEKVKNQIKQMmdv 1454
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDK-EFAETRDELKDYRE---KLEKLKREINEL--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1455 srtQTAISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILnelyqqkemalqkk 1534
Cdd:TIGR02169 405 ---KRELDRLQEELQRLSEELA-------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL-------------- 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1535 lsqeeyerqereqrlsaadeKAVLAAEEVKTYKRR--IEEMEDELQKTER 1582
Cdd:TIGR02169 461 --------------------AADLSKYEQELYDLKeeYDRVEKELSKLQR 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1222-1412 |
1.69e-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: 52.46 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1222 KENAELVQKLSSYEQKIKESKKHVQETKKQnmilsdeaikFKDKIKSLEETNEILGDTAKSLRAMlesEREQNAKNQDL- 1300
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE----------EKALLKQLAALERRIAALARRIRAL---EQELAALEAELa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1301 -----ISENKKSIEKLKDVIS------------------VNASEFSEVQI------ALNEAKLSE-EKVKSECHRVQEEN 1350
Cdd:COG4942 87 elekeIAELRAELEAQKEELAellralyrlgrqpplallLSPEDFLDAVRrlqylkYLAPARREQaEELRADLAELAALR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1351 ARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRL 1412
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1266-1586 |
1.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1266 IKSLEETNEILGDTAKSLRAM---LESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEA---KLSEEKV 1339
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRierLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1340 KSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEvalthkddNINALTNCITQLNRLDCESESE 1419
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1420 DQN--KGGSESDELANG--EVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQcKLRASMSTKCNLEDQIK----- 1490
Cdd:PRK03918 309 LREieKRLSRLEEEINGieERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpe 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1491 KLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQkKLSQEEYERQEREQRLSAADEKAVLA--AEEVKTYKR 1568
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-ELKKAKGKCPVCGRELTEEHRKELLEeyTAELKRIEK 466
|
330
....*....|....*...
gi 1387212238 1569 RIEEMEDELQKTERSFKN 1586
Cdd:PRK03918 467 ELKEIEEKERKLRKELRE 484
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1640-1906 |
3.59e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1640 VKPMPGRPNTQNPPRRGPlsqNGSFGPSPvsggecSPPLTADPPARPLSatlnRREMPRSEFDPESGAAPTVNSSSRSSS 1719
Cdd:PHA03247 2591 APPQSARPRAPVDDRGDP---RGPAPPSP------LPPDTHAPDPPPPS----PSPAANEPDPHPPPTVPPPERPRDDPA 2657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1720 PSKVMDEGKQTVPQEPEGPSVPS---IPSLAEHPVSVSMAAKGPPPFPGTPlmsspvgGPLLPPIRYGPPPQLCGPFGPR 1796
Cdd:PHA03247 2658 PGRVSRPRRARRLGRAAQASSPPqrpRRRAARPTVGSLTSLADPPPPPPTP-------EPAPHALVSATPLPPGPAAARQ 2730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1797 PLPPPFGPGMRPPLGLREYAPGVP--PGKRDLPLDP--------REFLPPGHAPFRPLGSLGPREYFFPGTRLPPPNHGP 1866
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGParPARPPTTAGPpapappaaPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387212238 1867 QDYPPSSAARDLPPSGSrdEPPPASqgaSQDCSPALKQSP 1906
Cdd:PHA03247 2811 VLAPAAALPPAASPAGP--LPPPTS---AQPTAPPPPPGP 2845
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1210-1636 |
3.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLKnimKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLES 1289
Cdd:PTZ00121 1313 EAKKADEAK---KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREQNAKNQDlISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEE---NARLKKKKEQLQQEIKD 1366
Cdd:PTZ00121 1390 KKKADEAKKK-AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkKAEEAKKAEEAKKKAEE 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1367 WSKSH--AELSEQIRSFEKSQKDLEVALTHKDdninaltncitQLNRLDCESESEDQNKGGSE---SDELANGEVGGDRS 1441
Cdd:PTZ00121 1469 AKKADeaKKKAEEAKKADEAKKKAEEAKKKAD-----------EAKKAAEAKKKADEAKKAEEakkADEAKKAEEAKKAD 1537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1442 EKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKlRASMSTKCNLE--DQIKKLEEDRsslqsAKTVLEDECKTLRQKVEI 1519
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKNMALRkaEEAKKAEEAR-----IEEVMKLYEEEKKMKAEE 1611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1520 LNELYQQKEMALQKKlsqEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQiATHEKKAHDNW 1599
Cdd:PTZ00121 1612 AKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKAEEDE 1687
|
410 420 430
....*....|....*....|....*....|....*..
gi 1387212238 1600 LKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 1636
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1202-1533 |
4.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1202 KSRVYQVTEQQISEKLKN-------IMKENAELVQKLSSYEQKIKESKKHVQETKKQNMI-------LSDE-----AIKF 1262
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEElekakeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrkelLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1263 KDKIKSLEETNEILGDTAKSLRAMLEsEREQNAKNQDLISENKKSIEKLKDV-----------ISVNASEFSEVQIALNE 1331
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKELAEQLKELeeklkkynleeLEKKAEEYEKLKEKLIK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1332 AKLSEEKVKSECHRVQEenarLKKKKEQLQQEIKDWSKSHAELSEQIRSFE-KSQKDLEVALTHKD---DNINALTNCIT 1407
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyNEYLELKDAEK 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1408 QLNRLDCESESEdQNKGGSESDELANGEvggDRSEKVKNQIKQ----------------MMDVSRtqtAISVVEEDLKLL 1471
Cdd:PRK03918 613 ELEREEKELKKL-EEELDKAFEELAETE---KRLEELRKELEElekkyseeeyeelreeYLELSR---ELAGLRAELEEL 685
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1472 QCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDeCKTLRQKVEILNELyqQKEMALQK 1533
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKAL--LKERALSK 744
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1234-1534 |
4.73e-06 |
|
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: 51.61 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1234 YEQKIKESKKHVQETKKQN---MILSDEAIKFKDKIKSLEETNeilgDTAKSLRAMLESERE--------------QNAK 1296
Cdd:pfam05622 85 YRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKkledlgdlrrqvklLEER 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1297 NQDLISENKKSIEKLKDVISVNAS-EFSEVQIALNEAKLSEEKVKS-----ECHRVQEENARLKKKKEQLQQEiKDWSKs 1370
Cdd:pfam05622 161 NAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKAdklefEYKKLEEKLEALQKEKERLIIE-RDTLR- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1371 haELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQ---------LNRLDCESESEDQNKGGSESDELANGEVGGDRS 1441
Cdd:pfam05622 239 --ETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEimpaeirekLIRLQHENKMLRLGQEGSYRERLTELQQLLEDA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1442 EKVKNQIKQMMDVSRTQtaISVVEEDLKLLQCKLRA-------SMSTKCNLEDQIKKLEEDRSSLQSAKTVLED-ECKTL 1513
Cdd:pfam05622 317 NRRKNELETQNRLANQR--ILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLEKLHEAQSELQKKKEQIEElEPKQD 394
|
330 340
....*....|....*....|.
gi 1387212238 1514 RQKVEILNELyqqkEMALQKK 1534
Cdd:pfam05622 395 SNLAQKIDEL----QEALRKK 411
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1211-1580 |
4.86e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKhvqetkKQNMILSDEAIKFKDKIKSLEETNeilGDTAKSLRAMLESE 1290
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRR------QLEIKKKEQREKEELKKLKLEAEE---LLADRVQEAQDKIN 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1291 REQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQialNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKS 1370
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1371 HAELSEQirsFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQnkggsesdELANGEVGGDRSEKVKNQIKQ 1450
Cdd:pfam02463 813 EAELLEE---EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE--------EEITKEELLQELLLKEEELEE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1451 MMDVSRTQTAISVVEEDLKLLQCKLRASmstkCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQ-KEM 1529
Cdd:pfam02463 882 QKLKDELESKEEKEKEEKKELEEESQKL----NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEE 957
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387212238 1530 ALQKKLSQEEYERQEREQRLSAADE----------------------KAVLAAEEVKTYKRRIEEMEDELQKT 1580
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEfeekeerynkdelekerleeekKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1644-1903 |
5.37e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1644 PGRPNTQNPPR-RGPLSQNGsfGPSPVSGGecsPPltaDPPARPlsatlnrremprsefdPESGAAPTVnsssrssspsk 1722
Cdd:PHA03247 2475 PGAPVYRRPAEaRFPFAAGA--APDPGGGG---PP---DPDAPP----------------APSRLAPAI----------- 2519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1723 vmdegkqtVPQEPEGPSVPS-----IPSLAEhpvSVSMAAKGPPPfPGTPLMSSPVGGPLLPPIRYGPPPqlcgpfGPRP 1797
Cdd:PHA03247 2520 --------LPDEPVGEPVHPrmltwIRGLEE---LASDDAGDPPP-PLPPAAPPAAPDRSVPPPRPAPRP------SEPA 2581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1798 LPPPFGPGMRPPLGLREYAPGVPPGKRDLPLDPREFLPPGHAPFRPLGSLGPR--EYFFPGTRLPPPNHGPQDYPPSSAA 1875
Cdd:PHA03247 2582 VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAanEPDPHPPPTVPPPERPRDDPAPGRV 2661
|
250 260
....*....|....*....|....*...
gi 1387212238 1876 RDLPPSGSRDEPPPASQGASQDCSPALK 1903
Cdd:PHA03247 2662 SRPRRARRLGRAAQASSPPQRPRRRAAR 2689
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1210-1401 |
6.47e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEaikfkdkiksLEETNEILGDTAkslRAMLES 1289
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----------IEERREELGERA---RALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREQ-------NAKN-QDLISenkkSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQ 1361
Cdd:COG3883 99 GGSVsyldvllGSESfSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387212238 1362 QEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINA 1401
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1292-1529 |
6.67e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1292 EQNAKNQDLISENK---KSIEKLKDVIsvnasefsEVQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIKDWS 1368
Cdd:PHA02562 167 EMDKLNKDKIRELNqqiQTLDMKIDHI--------QQQIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1369 KSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRL-----------DCESE-SEDQNKGGSESDELANGEV 1436
Cdd:PHA02562 234 AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcpTCTQQiSEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1437 GGDRSEKVKNQIKQMMDVSRTQTaisvveEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQK 1516
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|...
gi 1387212238 1517 VEILNELYQQKEM 1529
Cdd:PHA02562 388 LDKIVKTKSELVK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1302-1582 |
9.05e-06 |
|
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: 50.84 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1302 SENKKSIEKLKDVisvnasefsEVQIALNEAKLSEekVKSECHRVQEENAR------LKKKKEQLQQ-----EIKDWSKS 1370
Cdd:TIGR02169 170 RKKEKALEELEEV---------EENIERLDLIIDE--KRQQLERLRREREKaeryqaLLKEKREYEGyellkEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1371 HAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcesesedqnkggsESDELangevGGDRSEKVKNQIKQ 1450
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK---------------KIKDL-----GEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1451 M-MDVSRTQTAISVVEEDLKllqcklrasmstkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEM 1529
Cdd:TIGR02169 299 LeAEIASLERSIAEKERELE--------------DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387212238 1530 ALQKKLSQeeyerqereqrLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTER 1582
Cdd:TIGR02169 365 ELEDLRAE-----------LEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1212-1582 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1212 QISEKLKNIMKENAELVQKLSSYEqKIKESKKHVQETKKQNMILSDEaiKFKDKIKSLEETNEILGDTAKSLRAMLESER 1291
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1292 EQnaknqdlISENKKSIEKL---KDVISVNASEFSEVQIA--LNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKD 1366
Cdd:PRK03918 419 KE-------IKELKKAIEELkkaKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1367 WSK--SHAELSEQIRSFEKSQKDLEVALTHKDD---------------NINALTNCITQLNRLDCESEsEDQNKGGSESD 1429
Cdd:PRK03918 492 ESEliKLKELAEQLKELEEKLKKYNLEELEKKAeeyeklkekliklkgEIKSLKKELEKLEELKKKLA-ELEKKLDELEE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1430 ELAN-----GEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRasmSTKCNLEDQIKKLEEDRSSLQSAKT 1504
Cdd:PRK03918 571 ELAEllkelEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK---KLEEELDKAFEELAETEKRLEELRK 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1505 VLED-ECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADE-KAVLaaEEVKTYKRRIEEMEDELQKTER 1582
Cdd:PRK03918 648 ELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKlKEEL--EEREKAKKELEKLEKALERVEE 725
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1630-1895 |
1.65e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 50.07 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1630 MAMMQEEPVIVKPMPGRPNTQNPP------RRGPLSQNGSFGPSPVSGGECSPPLTADPPARPLSATLNRREMPRSEFDP 1703
Cdd:PHA03378 684 MLPIQWAPGTMQPPPRAPTPMRPPaappgrAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGR 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1704 ESGAAPTvnsssrssspskvmdEGKQTVPQEPEGPSVP-SIPSLAEHPVSvsmaakgPPPFPGTPLMSSPVGgpllPPIR 1782
Cdd:PHA03378 764 ARPPAAA---------------PGAPTPQPPPQAPPAPqQRPRGAPTPQP-------PPQAGPTSMQLMPRA----APGQ 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1783 YGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREYAPGVPP----GKRDLPLDPREFLPPGHAPFRPLGSLG---------- 1848
Cdd:PHA03378 818 QGPTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPspgsGTSDKIVQAPVFYPPVLQPIQVMRQLGsvraaaastv 897
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1849 ---PREYffPGTRLPPPNHGPQDYPPSSAARdlppSGSRDEPPPASQGAS 1895
Cdd:PHA03378 898 tqaPTEY--TGERRGVGPMHPTDIPPSKRAK----TDAYVESQPPHGGQS 941
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1200-1533 |
1.83e-05 |
|
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: 50.12 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1200 AVKSRVYQVTEQQISE-KLKNimkENAELVQKLSSYEQKIKES-KKHVQETKKQNMIL-------SDEAIKFKDKIKSLE 1270
Cdd:pfam15921 437 AMKSECQGQMERQMAAiQGKN---ESLEKVSSLTAQLESTKEMlRKVVEELTAKKMTLessertvSDLTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1271 ETN-EIlgdTAKSLRAMLESEREQNAKNQDlisENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHR---- 1345
Cdd:pfam15921 514 ATNaEI---TKLRSRVDLKLQELQHLKNEG---DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtaga 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1346 VQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLE---VALTH---------------KDDNINALTNCIT 1407
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekVKLVNagserlravkdikqeRDQLLNEVKTSRN 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1408 QLNRLDCESESEDQN-KGGSESDELANGEV------GGDRSEKVKNQIKQM-----------MDVSRTQTA----ISVVE 1465
Cdd:pfam15921 668 ELNSLSEDYEVLKRNfRNKSEEMETTTNKLkmqlksAQSELEQTRNTLKSMegsdghamkvaMGMQKQITAkrgqIDALQ 747
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387212238 1466 EDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 1533
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1204-1636 |
1.86e-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: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1204 RVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSL 1283
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1284 RAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSE------------EKVKSECHRVQEENA 1351
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleeleeelEELQEELERLEEALE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1352 RLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLE------VALTHKDDNINALTNCITQLNRLDCESE-------- 1417
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELISVDEGYEaaieaalg 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1418 -------SEDQNKGGSESDELANGEVG-----------GDRSEKVKNQIKQMMDVSRtQTAISVVEEDLKL--------- 1470
Cdd:TIGR02168 545 grlqavvVENLNAAKKAIAFLKQNELGrvtflpldsikGTEIQGNDREILKNIEGFL-GVAKDLVKFDPKLrkalsyllg 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1471 -------------LQCKLRASM------------------------STKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTL 1513
Cdd:TIGR02168 624 gvlvvddldnaleLAKKLRPGYrivtldgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1514 RQKVEILN-------------------------------ELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEE 1562
Cdd:TIGR02168 704 RKELEELEeeleqlrkeleelsrqisalrkdlarleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212238 1563 VKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHDNWLKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 1636
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1582 |
3.00e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1347 QEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldceseseDQNKGGS 1426
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--------ELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1427 ESDELANgevggdRSEKVKNQIKQMMDVSRTQTAISVVE-----EDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQS 1501
Cdd:COG4942 91 EIAELRA------ELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1502 AKTVLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTE 1581
Cdd:COG4942 165 LRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
.
gi 1387212238 1582 R 1582
Cdd:COG4942 241 E 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-1636 |
3.03e-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: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1348 EENARLKKKKEQLQQEIKdwsksHAELSEQIRsfeksQKDLEVALTH---KDDNINALTNCITQLNRlDCESESEDQNKG 1424
Cdd:TIGR02168 197 ELERQLKSLERQAEKAER-----YKELKAELR-----ELELALLVLRleeLREELEELQEELKEAEE-ELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1425 GSESDEL--ANGEVggdrsEKVKNQIKQmmDVSRTQTAISVVEEDLKLLQCKLRasmstkcNLEDQIKKLEEDRSSLQSA 1502
Cdd:TIGR02168 266 EEKLEELrlEVSEL-----EEEIEELQK--ELYALANEISRLEQQKQILRERLA-------NLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1503 KTVLEDECKTLRQKVEILNELYQqkemALQKKLSQEEYERQEREQRLSAADE-------KAVLAAEEVKTYKRRIEEMED 1575
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELE----SLEAELEELEAELEELESRLEELEEqletlrsKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1576 ELQKTERS---FKNQIATHEKKAHDNWLKarAAERAIAEEKREAANLRHKLLELTQKMAMMQEE 1636
Cdd:TIGR02168 408 RLERLEDRrerLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1272-1600 |
3.22e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1272 TNEILGDTAKSLRAMLESEREQNAKNQDL---ISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQE 1348
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLreeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1349 ENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSES 1428
Cdd:COG4372 102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1429 DELANGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQ------CKLRASMSTKCNLEdQIKKLEEDRSSLQSA 1502
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsleaklGLALSALLDALELE-EDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1503 KTVLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTER 1582
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|....*...
gi 1387212238 1583 SFKNQIATHEKKAHDNWL 1600
Cdd:COG4372 341 DLLQLLLVGLLDNDVLEL 358
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1283-1507 |
3.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLESEREQNAknQDLISENKKSIEklkdvisVNASEFSEVQIALNEAKLSEEkvksECHRVQEENARLKKKKEQLQQ 1362
Cdd:COG4717 43 IRAMLLERLEKEA--DELFKPQGRKPE-------LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1363 EIKDWSKSHAELSEQIRSFEKSQ--KDLEVALTHKDDNINALTNCITQLNRL--DCESESEDQNKGGSESDELANgevgg 1438
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELeeELEELEAELAELQEELEELLE----- 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1439 DRSEKVKNQIKQMM-DVSRTQTAISVVEEDLKLLQCKLRAsmstkcnLEDQIKKLEEDRSSLQSAKTVLE 1507
Cdd:COG4717 185 QLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEE-------LEEELEQLENELEAAALEERLKE 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1222-1631 |
4.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1222 KENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEilgdtAKSLRAMLESEREQNAKNQdli 1301
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE-----AAEKKKEEAKKKADAAKKK--- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1302 SENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEE-KVKSECHRVQEE---NARLKKKKEQLQQEIKDWSKSH--AELS 1375
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEakkKAEEAKKADEAKKKAEEAKKAEeaKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1376 EQIRSFEKSQKDLEVALTHKDDNINA--LTNCITQLNRLDCESESEDQNKGGSE---SDELANGEVGGDRSEKVKNQIKQ 1450
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEakkADEAKKAEEAKKADEAKKAEEKK 1546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1451 MMDVSRTQTAISVVEEDLKLLQCKlRASMSTKCNLE--DQIKKLEEDRSSLQSAKTVLEDECKT--LRQKVEILNELYQQ 1526
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAK-KAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEEAKIKAEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1527 KEMALQKK----LSQEEYERQEREQRLSAADEKAVLAAEEVKTY----KRRIEEM---EDELQKTERSFKNQiaTHEKKA 1595
Cdd:PTZ00121 1626 KKAEEEKKkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedKKKAEEAkkaEEDEKKAAEALKKE--AEEAKK 1703
|
410 420 430
....*....|....*....|....*....|....*.
gi 1387212238 1596 HDNWLKARAAERAIAEEKREAANLRHKLLELTQKMA 1631
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1201-1390 |
8.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1201 VKSRVYQVTEQQISekLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEET-NEILgd 1278
Cdd:PRK03918 530 LKEKLIKLKGEIKS--LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELEPFyNEYL-- 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1279 TAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLseEKVKSECHRVQEENARLKKKKE 1358
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELE 683
|
170 180 190
....*....|....*....|....*....|..
gi 1387212238 1359 QLQQEIKDWSKSHAELSEQIRSFEKSQKDLEV 1390
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1210-1376 |
1.17e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFkdkIKSLEETNEILGDTaKSLRAMLES 1289
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL---VMDIEDPSAALNKL-NTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1290 EREQNAK--------------NQDLISENKKsIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 1355
Cdd:PHA02562 270 KIEQFQKvikmyekggvcptcTQQISEGPDR-ITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIST 348
|
170 180
....*....|....*....|.
gi 1387212238 1356 KKEQLQQEIKDWSKSHAELSE 1376
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEE 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1278-1553 |
1.37e-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: 46.30 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1278 DTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVIsvnasEFSEVQIALNEAKLSEekVKSECHRVQEENARLKKKK 1357
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-----AALERRIAALARRIRA--LEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1358 EQLQQEIKdwsKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLdcesesedqnkggsesdelangevg 1437
Cdd:COG4942 93 AELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1438 gdrsekVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMStkcNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKV 1517
Cdd:COG4942 145 ------APARREQAEELRADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387212238 1518 EILnelyQQKEMALQKKLSQEEYERQEREQRLSAAD 1553
Cdd:COG4942 216 AEL----QQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1207-1582 |
1.52e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1207 QVTEQQISEKLKnimkENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKD---KIKSLEETNEILGDTAKSL 1283
Cdd:pfam05557 121 QRAELELQSTNS----ELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElefEIQSQEQDSEIVKNSKSEL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1284 RAMLESEREQnaknQDLISENKKSIEKLKDVisvnasEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQE 1363
Cdd:pfam05557 197 ARIPELEKEL----ERLREHNKHLNENIENK------LLLKEEVEDLKRKLEREE------KYREEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1364 IKDWSKSHAELSEQIRSFEksqkdlevalthkddninALTNCITQLNRLDCESESEdqnKGGSESDELANGEVGGDRSEK 1443
Cdd:pfam05557 261 LQSWVKLAQDTGLNLRSPE------------------DLSRRIEQLQQREIVLKEE---NSSLTSSARQLEKARRELEQE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1444 VKNQIKQMMDVSRTQTAISVVEEDL---KLLQCKLRASMstKCNLEDQIKKLEEDRSSLQSAKTVLEDEckTLRQKVEIL 1520
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLqrrVLLLTKERDGY--RAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAH 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387212238 1521 NELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLA-----AEEVKTYKRRIEEMEDELQKTER 1582
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAdpsysKEEVDSLRRKLETLELERQRLRE 462
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1225-1582 |
1.54e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1225 AELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNE--------------ILGDTAKSLRAMLESE 1290
Cdd:pfam01576 64 ARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaarqklqlekvTTEAKIKKLEEDILLL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1291 REQNAKnqdLISENKKSIEKLKDVISvNASEFSEVQIALNEAKLSEEKVKS--ECHRVQEENAR--LKKKKEQLQQEIKD 1366
Cdd:pfam01576 144 EDQNSK---LSKERKLLEERISEFTS-NLAEEEEKAKSLSKLKNKHEAMISdlEERLKKEEKGRqeLEKAKRKLEGESTD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1367 WSKSHAELSEQIR----SFEKSQKDLEVALTHKDDNINALTNCITQLNRL---------DCESESEDQNKG-------GS 1426
Cdd:pfam01576 220 LQEQIAELQAQIAelraQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiselqeDLESERAARNKAekqrrdlGE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1427 ESDEL------------ANGEVGGDRSEKVKNQIKQMMDVSRT---------QTAISVVEEDLKLLQCKLRASMS---TK 1482
Cdd:pfam01576 300 ELEALkteledtldttaAQQELRSKREQEVTELKKALEEETRSheaqlqemrQKHTQALEELTEQLEQAKRNKANlekAK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1483 CNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMA---LQKKLSQEEYERQEREQRLSAADEKAVLA 1559
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQraeLAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
410 420
....*....|....*....|...
gi 1387212238 1560 AEEVKTYKRRIEEMEDELQKTER 1582
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETR 482
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1187-1316 |
2.04e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.20 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1187 IVSFAV-------FFWRTVLAV-KSRvyqvtEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQEtkkqnmILsDE 1258
Cdd:cd06503 6 IINFLIllfilkkFLWKPILKAlDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------II-EE 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387212238 1259 AIKFKDKIKsleetNEILGDtakslrAMLESEREQNAKNQDLISENKKSIEKLKDVIS 1316
Cdd:cd06503 74 ARKEAEKIK-----EEILAE------AKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1195-1526 |
2.25e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1195 WRTVLAVKSRVYQVTEQQISEKLKNIMKENAelvqkLSSYEQKIK----ESKKHVQETKKQNMilsdEAIKFKDKIKSLE 1270
Cdd:TIGR01612 658 YSTIKSELSKIYEDDIDALYNELSSIVKENA-----IDNTEDKAKlddlKSKIDKEYDKIQNM----ETATVELHLSNIE 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1271 ETNEILGDTAKSLRAMLESE--REQNAKNQDLISENKKSIEKL------KDVISVNASEFSEVQIALNEaklseekvKSE 1342
Cdd:TIGR01612 729 NKKNELLDIIVEIKKHIHGEinKDLNKILEDFKNKEKELSNKIndyakeKDELNKYKSKISEIKNHYND--------QIN 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1343 CHRVQEENArlKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLevaLTHKDDNINALTNCitqlnrldceseSEDQN 1422
Cdd:TIGR01612 801 IDNIKDEDA--KQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDF---LNKVDKFINFENNC------------KEKID 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1423 KGGSESDELANgevggdrseKVKNQIKqmmdvsrtqtaisvvEEDLKLLQCKLRASMSTkcnLEDQIKKLEEDRSSLQSA 1502
Cdd:TIGR01612 864 SEHEQFAELTN---------KIKAEIS---------------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTL 916
|
330 340 350
....*....|....*....|....*....|...
gi 1387212238 1503 KTVLE---------DECKTLRQKVEILNELYQQ 1526
Cdd:TIGR01612 917 KKVDEyikicentkESIEKFHNKQNILKEILNK 949
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1663-1901 |
2.41e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1663 SFGPSPVSGGECSPPLTADPPARPLSATLNRREMPRSEFDPESGAAPTVNSSSrssspskvmdegkqTVPQEPEGPSVPS 1742
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAA--------------AARAVAAAPARRS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1743 iPSLAEHPVSVSMAAKGPPPFPGTPLMSSPVGGPLLPPIRYGPPPqlcgpfgpRPLPPPFGPGMRPPLGLREYAPGVPPG 1822
Cdd:PRK12323 428 -PAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRP--------VAAAAAAAPARAAPAAAPAPADDDPPP 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1823 KRDLPLDPREFLP--PGHAPFRPLGSLGPReyffPGTRLPPPNHGPQDYPPSSAARDLPPSGSRDEPPPASQGASQDCSP 1900
Cdd:PRK12323 499 WEELPPEFASPAPaqPDAAPAGWVAESIPD----PATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP 574
|
.
gi 1387212238 1901 A 1901
Cdd:PRK12323 575 D 575
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1235-1588 |
2.58e-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: 46.10 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1235 EQKIKESKKHVQETKKQNMI--LSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQDLISENKKsIEKLK 1312
Cdd:COG5185 174 QNLKKLEIFGLTLGLLKGISelKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELED-LAQTS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1313 DVISVNASEFSEvqiaLNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEI------KDWSKSHAELSEQIRSFEKSQK 1386
Cdd:COG5185 253 DKLEKLVEQNTD----LRLEKLGENAESSK--RLNENANNLIKQFENTKEKIaeytksIDIKKATESLEEQLAAAEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1387 dLEVALTHKDDNINALTNCITQLNrldcESESEDQNKGGSESDELAnGEVGGDRSEKVKNQIKQMMDVSRT--------- 1457
Cdd:COG5185 327 -LEESKRETETGIQNLTAEIEQGQ----ESLTENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnq 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1458 -----------QTAISVVEEDLKLLQCKLRASMStkcNLEDQIKKLEEDRSSLQSAKTVLEDECK------------TLR 1514
Cdd:COG5185 401 rgyaqeilatlEDTLKAADRQIEELQRQIEQATS---SNEEVSKLLNELISELNKVMREADEESQsrleeaydeinrSVR 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1515 QKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQI 1588
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1235-1596 |
2.67e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1235 EQKIKESKKHVQETKKQNMILSDEA--------IKFKD-KIKSLEETNEILGDTAKSLR--AMLESEREQnaknqdlisE 1303
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDPAktkalqtvIEMKDtKISSLERNIRDLEDEVQMLKtnGLLHTEDRE---------E 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1304 NKKSIEKLKdvisvNASEFSEVQIalneaklseEKVKSECHRVQEENARLKKKKEQLQQEIKDwSKSHAELseqirsfek 1383
Cdd:pfam10174 273 EIKQMEVYK-----SHSKFMKNKI---------DQLKQELSKKESELLALQTKLETLTNQNSD-CKQHIEV--------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1384 sqkdLEVALTHKDDNINALTNCITQLnRLDCESESEDQNKGGSESDELANgEVGGDRSEKvkNQIKQMMDVSRTQtaISV 1463
Cdd:pfam10174 329 ----LKESLTAKEQRAAILQTEVDAL-RLRLEEKESFLNKKTKQLQDLTE-EKSTLAGEI--RDLKDMLDVKERK--INV 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1464 VEEDLKLLQCKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDeckTLRQKVEILNELYQQKEMA------------- 1530
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERIIERLKEQREREdrerleeleslkk 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1531 ----LQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFkNQIATHEKKAH 1596
Cdd:pfam10174 476 enkdLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEC-SKLENQLKKAH 544
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1262-1377 |
2.83e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1262 FKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNQD-------LISENKKSIEKLKdvisvnaSEFSEVQIALNEAKL 1334
Cdd:pfam07926 6 LQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQnyerelvLHAEDIKALQALR-------EELNELKAEIAELKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387212238 1335 SEEKVKSEchrVQEENARLKKKKEQLQQEIKDWSKSHAELSEQ 1377
Cdd:pfam07926 79 EAESAKAE---LEESEESWEEQKKELEKELSELEKRIEDLNEQ 118
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1380 |
3.04e-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: 45.14 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1199 LAVKSRVYQVTEQQISE---KLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQN---MILSDEAikFKDKIKSLEet 1272
Cdd:COG4942 64 IAALARRIRALEQELAAleaELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplaLLLSPED--FLDAVRRLQ-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1273 neILGDTAKSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENAR 1352
Cdd:COG4942 140 --YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180
....*....|....*....|....*...
gi 1387212238 1353 LKKKKEQLQQEIKDWSKSHAELSEQIRS 1380
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1211-1435 |
3.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKI----KSLEETNEILGDTAkslRAM 1286
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeAEIEERREELGERA---RAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1287 LESEREQNAKNQDLISENkksiekLKDVIS-VNASEfsevQIALNEAKLSEEkvksechrVQEENARLKKKKEQLQQEIK 1365
Cdd:COG3883 96 YRSGGSVSYLDVLLGSES------FSDFLDrLSALS----KIADADADLLEE--------LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1366 DWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDELANGE 1435
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1212-1588 |
3.48e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1212 QISEKLKNIMKENAELvqkLSSYEQKIKESKkhvQETKKQNMILSDEAIKFKDKI--KSLEETNEI-----LGDTAKSLR 1284
Cdd:PTZ00440 400 YFISKYTNIISLSEHT---LKAAEDVLKENS---QKIADYALYSNLEIIEIKKKYdeKINELKKSInqlktLISIMKSFY 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1285 AMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVksechrvqEENARLKKKKEQLQQEI 1364
Cdd:PTZ00440 474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYY--------ITIEGLKNEIEGLIELI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1365 KDWSKSHAELSEQirsfEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKV 1444
Cdd:PTZ00440 546 KYYLQSIETLIKD----EKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1445 KNQIKQMMDvsrtqtaiSVVEEDLKLLQcklrASMSTkcNLEDQiKKLEEDRSSLQSAKTVL---EDECKTLRQKV---- 1517
Cdd:PTZ00440 622 QEKVKYILN--------KFYKGDLQELL----DELSH--FLDDH-KYLYHEAKSKEDLQTLLntsKNEYEKLEFMKsdni 686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1518 -EILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAVlaaEEVKTYKRRIEEMEDELQKTErSFKNQI 1588
Cdd:PTZ00440 687 dNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYT---IKYNDLKSSIEEYKEEEEKLE-VYKHQI 754
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1453-1587 |
3.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1453 DVSRTQTAISVVEEDLKllqcKLRASMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQ 1532
Cdd:COG4913 662 DVASAEREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1533 KKLSQEEYERQER-EQRLSAADEKAVLA------AEEVKTYKRRIEEMEDELQKTERSFKNQ 1587
Cdd:COG4913 738 AAEDLARLELRALlEERFAAALGDAVERelrenlEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1212-1383 |
5.29e-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: 44.24 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1212 QISEKLKNIMKENAELVqklssyeqkiKESKKHVqeTKKQNmILSDEAIKFKDKIKSLEETNEILgdtakslramLESER 1291
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL--MKELE-LLNSIKPKLRDRKDALEEELRQL----------KQLED 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1292 EQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQlqqeIKDWSKSH 1371
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ----CRGFTFKE 272
|
170
....*....|...
gi 1387212238 1372 AE-LSEQIRSFEK 1383
Cdd:smart00787 273 IEkLKEQLKLLQS 285
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1263-1403 |
5.50e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1263 KDKIKSLEETneilgdtAKSLRAmlESEREQNAKNQDLISENKKSIEKLKdvisvnaSEF-SEVQIALNEAKLSEEKVKS 1341
Cdd:PRK12704 30 EAKIKEAEEE-------AKRILE--EAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1342 ECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALthkdDNINALT 1403
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1207-1586 |
5.57e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1207 QVTEQQISEKLKNIMKENAELV---------QKLSSYEQKiKESKKHVQETKKQNMILSdEAIKFKDKIKSLE------- 1270
Cdd:TIGR01612 443 NIFKDDFDEFNKPIPKSKLKALekrffeifeEEWGSYDIK-KDIDENSKQDNTVKLILM-RMKDFKDIIDFMElykpdev 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1271 -ETNEILGDTAKSLRAMLESEREQNAK----------------NQDLISENKKSIeKLKDVISVNASEFSEV---QIALN 1330
Cdd:TIGR01612 521 pSKNIIGFDIDQNIKAKLYKEIEAGLKesyelaknwkkliheiKKELEEENEDSI-HLEKEIKDLFDKYLEIddeIIYIN 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1331 EAKLS-EEKVK--SECHRVQEENARLKKKKEQLQQEIKDWSK-SHAELSEQIRSFEKSQKDLEVALTH-KDDNINALTN- 1404
Cdd:TIGR01612 600 KLKLElKEKIKniSDKNEYIKKAIDLKKIIENNNAYIDELAKiSPYQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNe 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1405 --CITQLNRLDcesESEDQNKggseSDELANgevggdRSEKVKNQIkQMMDVSRTQTAISVVEEDL-KLLQCKLRASMST 1481
Cdd:TIGR01612 680 lsSIVKENAID---NTEDKAK----LDDLKS------KIDKEYDKI-QNMETATVELHLSNIENKKnELLDIIVEIKKHI 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1482 KCNLEDQIKKLEEDRSSLQsaktvledecKTLRQKVeilNELYQQKEM--ALQKKLSQEEYERQEREQRLSAADEKAVLA 1559
Cdd:TIGR01612 746 HGEINKDLNKILEDFKNKE----------KELSNKI---NDYAKEKDElnKYKSKISEIKNHYNDQINIDNIKDEDAKQN 812
|
410 420
....*....|....*....|....*..
gi 1387212238 1560 AEEVKTYKRRIEEMEDELQKTERSFKN 1586
Cdd:TIGR01612 813 YDKSKEYIKTISIKEDEIFKIINEMKF 839
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1221-1534 |
6.08e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1221 MKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIK-SLEETNEILGDTAKSLRAMLESEREQNAKNQD 1299
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINvKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1300 LISENKKSI-------EKLKDVISVNASEFSEVQIALNEaklseekVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHA 1372
Cdd:PRK01156 449 LNGQSVCPVcgttlgeEKSNHIINHYNEKKSRLEEKIRE-------IEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1373 ELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDeLANGEVGGDRSEKVKNQIKQMM 1452
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS-LIDIETNRSRSNEIKKQLNDLE 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1453 D------------VSRTQTAISVVEEDLKLLQCKL---------------------------------RASMSTKCN-LE 1486
Cdd:PRK01156 601 SrlqeieigfpddKSYIDKSIREIENEANNLNNKYneiqenkilieklrgkidnykkqiaeidsiipdLKEITSRINdIE 680
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1387212238 1487 DQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKK 1534
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1211-1378 |
6.30e-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: 43.37 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETneiLGD--TAKSLRAM-- 1286
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvrNNKEYEALqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1287 -LESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKlseekvksechrvqeenARLKKKKEQLQQEIK 1365
Cdd:COG1579 97 eIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK-----------------AELDEELAELEAELE 159
|
170
....*....|...
gi 1387212238 1366 DWSKSHAELSEQI 1378
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1215-1629 |
8.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1215 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEIlgDTAKSLRAMLESEREQN 1294
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA--EEARKAEDARKAEEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1295 AKNQDLISENKKSIEKLKDVISVNASEFSEVQialnEAKLSEEKVKSECHRVQEENARLK--KKKEQLQQEIKDWSKSHA 1372
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEARKAEDAKKAE----AARKAEEVRKAEELRKAEDARKAEaaRKAEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1373 ELSEQIRSFEKSQKDLEVALTHKDDNINALTNC-----ITQLNRLDCESESEDQNKggseSDELANGEvggdrSEKVKNQ 1447
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeearMAHFARRQAAIKAEEARK----ADELKKAE-----EKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1448 IKQMMDVSRTQTAISVVEEDLKLLQCKLRAsmstkcnlEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQK 1527
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKA--------EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1528 EMALQKKlsqeeyerQEREQRLSAADEKA--VLAAEEVKTYKRRIEEMEDELQKTERSfknqiathEKKAHDnwLKARAA 1605
Cdd:PTZ00121 1367 EAAEKKK--------EEAKKKADAAKKKAeeKKKADEAKKKAEEDKKKADELKKAAAA--------KKKADE--AKKKAE 1428
|
410 420
....*....|....*....|....
gi 1387212238 1606 ERAIAEEKREAANLRHKLLELTQK 1629
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKK 1452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1275-1522 |
9.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1275 ILGDTAKSLRAMLESEREQNAKN----QDLISENKKSIEKLKDVISV--NASEFSEVQIALNEAKLSEEKVKSECHRVQE 1348
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEElaeaEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1349 EN---ARLKKKKEQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGG 1425
Cdd:COG4913 683 SSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1426 SESDELAN--GEVGGDRSEKVKNQ---IKQM--------MDVSRTQTAISVVEEDLKLLQcKLRASmstkcNL---EDQI 1489
Cdd:COG4913 763 VERELRENleERIDALRARLNRAEeelERAMrafnrewpAETADLDADLESLPEYLALLD-RLEED-----GLpeyEERF 836
|
250 260 270
....*....|....*....|....*....|....*...
gi 1387212238 1490 KKL-----EEDRSSLQSAktvLEDECKTLRQKVEILNE 1522
Cdd:COG4913 837 KELlnensIEFVADLLSK---LRRAIREIKERIDPLND 871
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
198-462 |
9.10e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 44.39 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 198 AELRERSEAQKSHPQV----------NSQTGHAQGErtsfesfgEMLQDKLKVPDSENNKTSNSSQVSHEQEKIDAYKLL 267
Cdd:PTZ00341 324 AEMKKRAEKPKKKKSKrrgwlccgggDIETVEPQQE--------EPVQDVGEHQINEYGDILPSLKASINNSAINYYDAV 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 268 KTEMTLDlktkfGSTADALVSDDEttrLVTSLEDD-FVEDLDpeyytvGKEEEENKEDFDELPLltftDGEDTKSPGHSG 346
Cdd:PTZ00341 396 KDGKYLD-----DDSSDALYTDED---LLFDLEKQkYMDMLD------GSEDESVEDNEEEHSG----DANEEELSVDEH 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 347 IEKHPTEKEQNSNKEHKVEETQPPGIKKGDKEIPKHREDTVFSDVMEgEENTDTDLESSDSKEEDDPLVMDSRLGKPRPE 426
Cdd:PTZ00341 458 VEEHNADDSGEQQSDDESGEHQSVNEIVEEQSVNEHVEEPTVADIVE-QETVDEHVEEPAVDENEEQQTADEHVEEPTIA 536
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387212238 427 DHTDPEKAADHLVNVEVPKADSDDDPEVGAGLHMKD 462
Cdd:PTZ00341 537 EEHVEEEISTAEEHIEEPASDVQQDSEAAPTIEIPD 572
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1222-1533 |
9.76e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.40 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1222 KENAELVQ---KLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILG---DTAKSLRAMLES-EREQN 1294
Cdd:pfam09728 1 KAARELMQllnKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQselSKAILAKSKLEKlCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1295 AKNQDLISENKKSIEKLKDvisvNASEFSE-VQIALNEAKLSEEKVKSECHRVQEENARLKKK-KEQLQQeikdwskshA 1372
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEE----KRKELSEkFQSTLKDIQDKMEEKSEKNNKLREENEELREKlKSLIEQ---------Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1373 ELSEQIrsFEK--SQKDLEVALthkddninaltnCITQLNRLDCESESEDQNKGGSESDELAngevggDRSEKVKNQIKQ 1450
Cdd:pfam09728 148 ELRELH--FEKllKTKELEVQL------------AEAKLQQATEEEEKKAQEKEVAKARELK------AQVQTLSETEKE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1451 MmdvsRTQtaISVVEEDLKLLQCKLRAS-------------MSTKCnledqiKKLEEDRSSLQS--------------AK 1503
Cdd:pfam09728 208 L----REQ--LNLYVEKFEEFQDTLNKSnevfttfkkemekMSKKI------KKLEKENLTWKRkweksnkallemaeER 275
|
330 340 350
....*....|....*....|....*....|
gi 1387212238 1504 TVLEDECKTLRQKVEILNELYQqkemALQK 1533
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLENLCR----ALQA 301
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1320-1562 |
1.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1320 SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKdwskshaELSEQIRSFEKSQKDLEVALTHKDDNI 1399
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-------ALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1400 NAltncitQLNRLdcesesedQNKGGSES--DELANGEVGGDRSEKVkNQIKQMMDvsRTQTAISVVEEDLKLLQCKLRA 1477
Cdd:COG3883 89 GE------RARAL--------YRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1478 SMSTKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREQRLSAADEKAV 1557
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 1387212238 1558 LAAEE 1562
Cdd:COG3883 232 AAAAA 236
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1210-1533 |
1.39e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.05 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1210 EQQISEKLkNIMKENAELVQ-KLSSYEQKIKESKKHVQE-TKKQNMIL-----SDEAIKFKDKIKSLEETNEILGDTAKS 1282
Cdd:PTZ00440 793 ENKISNDI-NILKENKKNNQdLLNSYNILIQKLEAHTEKnDEELKQLLqkfptEDENLNLKELEKEFNENNQIVDNIIKD 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1283 LRAMLES----EREQNAKNQDliSENKKSIEKLK----DVISVNASEFSEVQ----IALNEAKLSEEKVKSECHRVQEE- 1349
Cdd:PTZ00440 872 IENMNKNiniiKTLNIAINRS--NSNKQLVEHLLnnkiDLKNKLEQHMKIINtdniIQKNEKLNLLNNLNKEKEKIEKQl 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1350 -NARLKKKKEQLQQEIKDWSKSHAELS-------EQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRldcesesEDQ 1421
Cdd:PTZ00440 950 sDTKINNLKMQIEKTLEYYDKSKENINgndgthlEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIK-------KQH 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1422 NKGGSESDELANgEVGGDRSEKVKNQIKQM-------------MDVSRTQTAISvvEEDLKLLQCKlrasmstkcnLEDQ 1488
Cdd:PTZ00440 1023 DDIIELIDKLIK-EKGKEIEEKVDQYISLLekmktklssfhfnIDIKKYKNPKI--KEEIKLLEEK----------VEAL 1089
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1387212238 1489 IKKLEEDRSSLQSAKTVLEDECKTLRQKVEILNELYQQKEMALQK 1533
Cdd:PTZ00440 1090 LKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEK 1134
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1642-1906 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1642 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSP---PLTADPPARPlsATLNRREMPRSEFDPESGAAPTVNSSSRSS 1718
Cdd:pfam03154 243 PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPmphSLQTGPSHMQ--HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1719 SPSKVMDEGKQTVPQEPEGPSVPSIPslaehPVSVSMAAKGPPPFPGTPLMSSPVG----------GPLLPPIRYGPPPQ 1788
Cdd:pfam03154 321 SQQRIHTPPSQSQLQSQQPPREQPLP-----PAPLSMPHIKPPPTTPIPQLPNPQShkhpphlsgpSPFQMNSNLPPPPA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1789 LcgPFGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLP-LDPREFLPPGHAPFRPLGSL--GPREYFFPgTRLPPPNHG 1865
Cdd:pfam03154 396 L--KPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPvLTQSQSLPPPAASHPPTSGLhqVPSQSPFP-QHPFVPGGP 472
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387212238 1866 PQDYPPSSAARDLPPSGSRDEPPPASQGASQDCSPALKQSP 1906
Cdd:pfam03154 473 PPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCP 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1222-1521 |
1.42e-03 |
|
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: 43.57 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1222 KENAELVqkLSSYEQKIKESKKHVQET----KKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSlramlESEREQNAKN 1297
Cdd:pfam15921 73 KEHIERV--LEEYSHQVKDLQRRLNESnelhEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR-----ESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1298 Q----------------DLISENKKSIEKLKDVISVNASEFSEVQIAL---NEA---KLSEEKVKSECHrVQEENARLKK 1355
Cdd:pfam15921 146 QlqntvheleaakclkeDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEAsgkKIYEHDSMSTMH-FRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1356 KKEQLQQEIKDWSKSHAELSEQIRSFE-KSQKDLEVALTHKDDNINALTncitqlnrldceSESEDQNKGGSESDELANG 1434
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKsESQNKIELLLQQHQDRIEQLI------------SEHEVEITGLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1435 EvggdrSEKVKNQIKQMMDVSRTQTAISVveedlkllqcklrasmstkCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLR 1514
Cdd:pfam15921 293 Q-----ANSIQSQLEIIQEQARNQNSMYM-------------------RQLSDLESTVSQLRSELREAKRMYEDKIEELE 348
|
....*..
gi 1387212238 1515 QKVEILN 1521
Cdd:pfam15921 349 KQLVLAN 355
|
|
| DivIC |
pfam04977 |
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ... |
1338-1380 |
1.55e-03 |
|
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.
Pssm-ID: 428231 [Multi-domain] Cd Length: 69 Bit Score: 38.74 E-value: 1.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1387212238 1338 KVKSECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRS 1380
Cdd:pfam04977 10 QLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDPDYIEERARS 52
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1652-1901 |
1.63e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1652 PPRRGPLSQNGSFGPSPVSGgecSPPLTADPPARPLSATLNRREMPRSEFDPESGaaPTVNSSSRSSSPSKVMDEGKQTV 1731
Cdd:PHA03307 19 EFFPRPPATPGDAADDLLSG---SQGQLVSDSAELAAVTVVAGAAACDRFEPPTG--PPPGPGTEAPANESRSTPTWSLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1732 PQEPEG------PSVPSIPSLAEHPVSVSMAAKGPPPFPGTPLMSSPVGGPLLPPIRYGPPPQLCGPFGPRPLPPPFGPG 1805
Cdd:PHA03307 94 TLAPASparegsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1806 MRPPLGLREYAPGVPPGKRDLPLDPREFLPPG-HAPFRPL-------GSLGPREYFF--------------------PGT 1857
Cdd:PHA03307 174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRpPRRSSPIsasasspAPAPGRSAADdagasssdssssessgcgwgPEN 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387212238 1858 RLPPPNHGPQDYPPSSAARDLPPSGSRDEPPPASQGASQDCSPA 1901
Cdd:PHA03307 254 ECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPS 297
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
1735-1906 |
1.97e-03 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 41.90 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1735 PEGPS----VPSIPSLAEHPVSvsmaakgPPPFPGTPLMSSPVGGPLLPPIRYGPPPqlcgpfgprpLPPPFGPGMRPPL 1810
Cdd:pfam15822 59 PFGPAptgmYPSIPLTGPSPGP-------PAPFPPSGPSCPPPGGPYPAPTVPGPGP----------IGPYPTPNMPFPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1811 GLREYAPgvppgkrdlPLDPREFLPPGHAPFRPLGSLGPR---EYFFPGTRLPPPNHGPQDYPPSS--AARDLP----PS 1881
Cdd:pfam15822 122 LPRPYGA---------PTDPAAAAPSGPWGSMSSGPWAPGmggQYPAPNMPYPSPGPYPAVPPPQSpgAAPPVPwgtvPP 192
|
170 180
....*....|....*....|....*
gi 1387212238 1882 GSRDEPPPASQGASQDCSPALKQSP 1906
Cdd:pfam15822 193 GPWGPPAPYPDPTGSYPMPGLYPTP 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1226-1588 |
2.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1226 ELVQKLSSYEQKIKESKKHVQETKKQnmilsdeAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQnaknqdlISENK 1305
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1306 KSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK----------KKKEQLQ---------QEIKD 1366
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLeagkcpecgQPVEG 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1367 wsKSHA----ELSEQIRSFEKSQKDLEVALTHKDDNINALTNCI-------TQLNRLDCESESEDQNKGGSESDELA--- 1432
Cdd:PRK02224 464 --SPHVetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedrieRLEERREDLEELIAERRETIEEKRERaee 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1433 ----NGEVGGDRSEKVKNQIKQMMDVSRTQTAISVVEEDLKLLQC------KLRASMSTKCNLEDQIKKLEEDRSSLQSA 1502
Cdd:PRK02224 542 lrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1503 KTVLEDECKTLRQKVEILNELYQQK--EMALQKKlsqeeyerqereqrlsaadEKAVLAAEEVKTYKRRIEEMEDELQKT 1580
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEAriEEAREDK-------------------ERAEEYLEQVEEKLDELREERDDLQAE 682
|
....*...
gi 1387212238 1581 ERSFKNQI 1588
Cdd:PRK02224 683 IGAVENEL 690
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1278-1643 |
2.32e-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: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1278 DTAKSLRAMLESEREQNAKNQDLISENKKSiekLKDVISVNASEFSEVQIALNEAKLSEEKVKSEcHRVQEENARLKKKK 1357
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDT---YHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1358 EQLQQEIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKddninaltnCITQLNRLDCESESEDQNKGGSESDELAngevg 1437
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK---------AVTQIEQQAQRIHTELQSKMRSRAKLLM----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1438 gdrseKVKNQIKQMMDVSRTQTAISVVEEDLKLLQCKLRASMSTKCNLEDQiKKLEEDRSSLQSAKTVLEDECKTLRQKV 1517
Cdd:TIGR00618 329 -----KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1518 EILNELYQQ------KEMALQKKLSQEEYERQEREQRLSAADEKAVLAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 1591
Cdd:TIGR00618 403 DILQREQATidtrtsAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1387212238 1592 EKKAHdnwlKARAAERAIAEEKREAANLRHKLLELTQKMAMMQEEPVIVKPM 1643
Cdd:TIGR00618 483 LQETR----KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM 530
|
|
| SOBP |
pfam15279 |
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1732-1891 |
2.46e-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: 42.11 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1732 PQEPEGPSVPSIPSLAEHPVSVSMAAKGPPPfpGTPLMSSPVGGPLLPPIRYGPPPqlcgpfgprplpppfgpgmrpPLG 1811
Cdd:pfam15279 131 HEPPSLPPPPLPPKKGRRHRPGLHPPLGRPP--GSPPMSMTPRGLLGKPQQHPPPS---------------------PLP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1812 LREYAPGVPPGkrdlpldpreFLPPGHAPFRPLGSLGPReyffPGTRLPPPNHGPQDYPPSSAARDLPPSGSRDEPPPAS 1891
Cdd:pfam15279 188 AFMEPSSMPPP----------FLRPPPSIPQPNSPLSNP----MLPGIGPPPKPPRNLGPPSNPMHRPPFSPHHPPPPPT 253
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
1727-1895 |
2.77e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 40.24 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1727 GKQTVPQEPEGPSVPSIPSLAEHPVSVSmaakgPPPFPGTPLMSSPV---GGPLLPPirygPPPQLCGPFGPRPLPPPFG 1803
Cdd:pfam06346 8 GDSSTIPLPPGACIPTPPPLPGGGGPPP-----PPPLPGSAAIPPPPplpGGTSIPP----PPPLPGAASIPPPPPLPGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1804 PGMRPPLGLrEYAPGVPPGKRDLPLDPREFLPPghaPFRPLGslgpreyffPGTRLPPPNHGPQDYPPSSAARDLPPsgs 1883
Cdd:pfam06346 79 TGIPPPPPL-PGGAGIPPPPPPLPGGAGVPPPP---PPLPGG---------PGIPPPPPFPGGPGIPPPPPGMGMPP--- 142
|
170
....*....|..
gi 1387212238 1884 rdePPPASQGAS 1895
Cdd:pfam06346 143 ---PPPFGFGVP 151
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1215-1516 |
2.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1215 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEETNEILGDTAKSLRAMLESEREQ 1293
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1294 --NAKNQDLISENKKSIEKLKDVI---------------------------------------------SVNASEFSEVQ 1326
Cdd:COG4717 229 leQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllallflllarekASLGKEAEELQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1327 IALNEAKLSEEKVKSECHRVQ-------EENARLKKKKEQLQQEIKDWSKSHAELseQIRSFEKSQKDLevaLTHKD-DN 1398
Cdd:COG4717 309 ALPALEELEEEELEELLAALGlppdlspEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAAL---LAEAGvED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1399 INALTNCITQLNRL--------DCESESEDQNKGGSESDELANGEVGGDRSEKVKNQIKQ--------MMDVSRTQTAIS 1462
Cdd:COG4717 384 EEELRAALEQAEEYqelkeeleELEEQLEELLGELEELLEALDEEELEEELEELEEELEEleeeleelREELAELEAELE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387212238 1463 VVEEDLKLLQCKLRASMstkcnLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQK 1516
Cdd:COG4717 464 QLEEDGELAELLQELEE-----LKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
1226-1412 |
3.18e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 42.69 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1226 ELVQKLSSYEQKIkES---KKHVQETKKQNMILSDEAIK-FKDKIKSLEETNEILGDTAK-SLRAMLESereQNAKNQDL 1300
Cdd:PTZ00419 798 ELYQRLPNYLRKS-ESisiAKYPQPNPGWNNEALDEEMKiIMSIVKSIRSLIATLGIPNKtKPDCYVTA---KDAELIEL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1301 ISENKKSIEKLKDVISVNASEFSEVQIALNE--------AKLSEEKVKSECHRVQEENARLKKKKEQLQQEIKDWSKS-- 1370
Cdd:PTZ00419 874 IESAENLISTLAKIGSVSVIPPIEEEAEVPKgcgfdvvdNKVIIYLNLDEFIDLKKELAKLEKKLAKLQKSLESYLKKis 953
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212238 1371 ----HAELSEQIRSFEKSQKDlevALTHkddNINALTNCITQLNRL 1412
Cdd:PTZ00419 954 ipnyEDKVPEDVRKLNDEKID---ELNE---EIKQLEQAIEELKSL 993
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1211-1445 |
4.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAmlese 1290
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1291 reQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIKDWSK 1369
Cdd:COG4372 137 --QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212238 1370 SHAELSEQIRSFEKSQKDLEVALTHKDDNINALTNCITQLNRLDCESESEDQNKGGSESDELANGEVGGDRSEKVK 1445
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| ClyA-like |
cd21116 |
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ... |
1205-1394 |
4.22e-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: 40.86 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1205 VYQVTEQQiseklkNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIK-FKDKIKSLEET------NEILG 1277
Cdd:cd21116 15 VTAILNQP------NINLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgYNNTFQSYYPDlieladNLIKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1278 DTA--KSLRAMLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEKVKSECHRVQEENAR--- 1352
Cdd:cd21116 89 DQGakQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAaid 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387212238 1353 ----LKKKKEQLQQEIKDWSKShAELSEQIRSFEKSQKDLEVALTH 1394
Cdd:cd21116 169 alekLSNDWQTLDSDIKELITD-LEDAESSIDAAFLQADLKAAKAD 213
|
|
| SH3 |
cd00174 |
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
52-98 |
4.62e-03 |
|
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.
Pssm-ID: 212690 [Multi-domain] Cd Length: 51 Bit Score: 37.06 E-value: 4.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1387212238 52 ALEDFTGPDCRFVNFKKGDTVYVYYKLAGGspevWA-GSV-GHTFGYFP 98
Cdd:cd00174 4 ALYDYEAQDDDELSFKKGDIITVLEKDDDG----WWeGELnGGREGLFP 48
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1211-1310 |
4.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1211 QQISEKLKNIMKENAE----LVQKLSS----YEQKIKESKKHVQETKKQNMILSDEAIKFKDKIKSL-----EETNEILg 1277
Cdd:PRK00409 501 ENIIEEAKKLIGEDKEklneLIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAQQAI- 579
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1387212238 1278 DTAKS-----LRAMLESEREQNA--KNQDLIsENKKSIEK 1310
Cdd:PRK00409 580 KEAKKeadeiIKELRQLQKGGYAsvKAHELI-EARKRLNK 618
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1179-1381 |
5.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1179 VLITASLGIVSFAVFFWRtvlavKSRVYQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESKKhvQETKKQNMILSDE 1258
Cdd:PRK12705 10 LLLLIGLLLGVLVVLLKK-----RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQR--QEARREREELQRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1259 AIKFKDKIKSLEETNEILGDTAKSLramLESEREQNAKNQDLISENKKSIEKLKDVISVNASEFSEVQIALNEAKLSEEK 1338
Cdd:PRK12705 83 EERLVQKEEQLDARAEKLDNLENQL---EEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387212238 1339 VKSecHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSF 1381
Cdd:PRK12705 160 AQR--VKKIEEEADLEAERKAQNILAQAMQRIASETASDLSVS 200
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
1252-1382 |
6.40e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 39.78 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1252 NMILSDEAIKFKDKIKSLEETNEILGDTAKSLRAMLESEREQNAKNqdliSENKKSIEKLKdvISVNASEFSEVQIALNE 1331
Cdd:pfam14662 17 NQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKE----KLLEEELEDLK--LIVNSLEEARRSLLAQN 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1387212238 1332 AKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIKDWSKSHAELSEQIRSFE 1382
Cdd:pfam14662 91 KQLEKENQSllQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCE 143
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1206-1399 |
8.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1206 YQVTEQQISEKLKNIMKENAELVQKLSSYEQKIKESK-KHVQETKKQNMIlsdeaikfKDKIKSLEETNEILGDTAKSLR 1284
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdELKDYREKLEKL--------KREINELKRELDRLQEELQRLS 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1285 AMLEserEQNAKNQDLISENKKSIEKLKDVI-SVNASEFSEVQIALNEAKLSEE---------KVKSECHRVQEENARLK 1354
Cdd:TIGR02169 420 EELA---DLNAAIAGIEAKINELEEEKEDKAlEIKKQEWKLEQLAADLSKYEQElydlkeeydRVEKELSKLQRELAEAE 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387212238 1355 KKKEQLQQEIKDWSKS-----------HAELSEQIRSFEKSQKDLEVALTHKDDNI 1399
Cdd:TIGR02169 497 AQARASEERVRGGRAVeevlkasiqgvHGTVAQLGSVGERYATAIEVAAGNRLNNV 552
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
735-912 |
9.11e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 735 KQSKERSPEIQDKRLDVDLQNPEKPVSGAIKTDPETEKNKEETRHVSENERKNETAGKavdSLGRDAGGPVVEKEGSSPV 814
Cdd:PTZ00449 490 KKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGG---KPGETKEGEVGKKPGPAKE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 815 HQKVQRPSEGSDVPGKKQNQTPELGEASQK-KDPDYLKEDNHEGHPKTSGLMEKPGVEPSKEDDEHAEKFVDPgSRGSAS 893
Cdd:PTZ00449 567 HKPSKIPTLSKKPEFPKDPKHPKDPEEPKKpKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPP-QRPSSP 645
|
170
....*....|....*....
gi 1387212238 894 EDPDDDPFPWAPHAPVQPE 912
Cdd:PTZ00449 646 ERPEGPKIIKSPKPPKSPK 664
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1215-1601 |
9.64e-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: 41.19 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1215 EKLKNIMKENAELVQKLSSYEQKIKESKKHVQETKKQNMILSDEAIKF----KDKIKSLEETNEILGDTAKSLRAMLESE 1290
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKERELVDCQRE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1291 REQNAKNQDLISENKKSIEKLKDVISVNASEFSEvQIALNEAKLSEEKVKSECH--------RVQEENArLKKKKEQLQQ 1362
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVEQGRLQLQADRHQE-HIRARDSLIQSLATRLELDgfergpfsERQIKNF-HTLVIERQED 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1363 EIKDWSKSHAELSEQIRSFEKSQKDLEVALTHKDDNInaltncitqlnRLDCESESEDQNKGGSESDELANGEVGGDRSE 1442
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI-----------ELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1443 KVKNQIKqmmdvsRTQTAISVVEEDlKLLQCKLRASMS---TKCNLEDQIKKLEEDRSSLQSAKTVLEDECKTLRQKVEI 1519
Cdd:TIGR00606 475 ELDQELR------KAERELSKAEKN-SLTETLKKEVKSlqnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1520 LNELYQQKEMALQKKLSqeEYERQEREQRLSAADEKavlAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHDNW 1599
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTS--LLGYFPNKKQLEDWLHS---KSKEINQTRDRLAKLNKELASLEQN-KNHINNELESKEEQL 621
|
..
gi 1387212238 1600 LK 1601
Cdd:TIGR00606 622 SS 623
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1708-1904 |
9.65e-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: 40.91 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1708 APTVNSSSRSSSPSKVMDEGKQTVPQEPEGPSVPSIPslaehPVSVSMAAKGPPPFPGTPLMSSPVGGPLLPPIRYGPPP 1787
Cdd:pfam03154 150 SPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSP-----PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQST 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387212238 1788 QLCGPFGPRPLPPPFGPGMRPPLGLREYAPGVPPGKRDLPLDPReflPPGHAPFRPLG---SLGPREYFFPGTRLP---P 1861
Cdd:pfam03154 225 AAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQ---PSLHGQMPPMPhslQTGPSHMQHPVPPQPfplT 301
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387212238 1862 PNHGPQDYPPSSAARDLPPSGSRDEPPPaSQGASQDCSPALKQ 1904
Cdd:pfam03154 302 PQSSQSQVPPGPSPAAPGQSQQRIHTPP-SQSQLQSQQPPREQ 343
|
|
| |
