|
Name |
Accession |
Description |
Interval |
E-value |
| ANTH |
pfam07651 |
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ... |
3-241 |
6.63e-69 |
|
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Pssm-ID: 400137 Cd Length: 272 Bit Score: 231.80 E-value: 6.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 3 HKAKEAKTFWMIISRQPLMQSRFTAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWG-LLQDDIGCCIQAYSKLL 81
Cdd:pfam07651 31 SSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRISSfSLSWDYGAFIRAYAKYL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 82 ATKLNFHDKNRMFPGTLNISFTELFIAVDRDLNYCfqLCVEIFDYLEDIIALQLTIFSSME-KYRMSSMTpqGQCRLAPI 160
Cdd:pfam07651 111 DERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY--LTMSMEDLLDSIPKLQKLLFRLLKcRPTGNALS--NECIIAAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 161 VCLIQDSNALYDLSVRLMFKLHDGVPY------DVVSGHRDRFHGLFLKLKSFYNNVRPLQYFKDLItIPELPDSSPNFK 234
Cdd:pfam07651 187 ILLVKESFGLYRAINEGIINLLEKFFElskpdaDRALGIYKRFVKQFERLKEFYEVCKNLGYFRSLE-IPKLPHIPPNLL 265
|
....*..
gi 24663450 235 SQNDFTS 241
Cdd:pfam07651 266 EALEEYL 272
|
|
| ILWEQ |
smart00307 |
I/LWEQ domain; Thought to possess an F-actin binding function. |
887-1085 |
9.95e-57 |
|
I/LWEQ domain; Thought to possess an F-actin binding function.
Pssm-ID: 214607 [Multi-domain] Cd Length: 200 Bit Score: 194.51 E-value: 9.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 887 TNLEVNGKIVDACTTLMECVKALIQKSRLLQHEIVASQKGNASANEFYRRNSQWSDGLISASKSVAKAANYLVEAANKAI 966
Cdd:smart00307 2 VELEVDESILEAAKAITKAIAALVKAATNAQREIVAQGRGGASPGEFYKKNSRWTEGLISAAKAVAAATNVLVEAADGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 967 EsESGKNFELIVAAQEIAACTTQMVIASKVKAERNSQKLTDLTKASRSVTQATGTLVATVKDCNSQ-LEQQSEIELSKLT 1045
Cdd:smart00307 82 T-GKGSEEELIVAAKEVAASTAQLVAASRVKADKDSQAQDRLQAASKAVTNATANLVAAVKSGMIFdEEQEEEEDFSKLS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24663450 1046 PSQIKTMEMEIHVKVLEIEQALQMQRLKLSSFRKEHYKNA 1085
Cdd:smart00307 161 LHEGKTQEMEQQVEILKLENELEAARKKLAEIRKQHYELA 200
|
|
| I_LWEQ |
pfam01608 |
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from ... |
936-1083 |
6.46e-50 |
|
I/LWEQ domain; I/LWEQ domains bind to actin. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin. I/LWEQ domains can be placed into four major groups based on sequence similarity: (1) Metazoan talin; (2) Dictyostelium TalA/TalB and SLA110; (3) metazoan Hip1p; and (4) yeast Sla2p. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks.
Pssm-ID: 460265 [Multi-domain] Cd Length: 149 Bit Score: 173.15 E-value: 6.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 936 RNSQWSDGLISASKSVAKAANYLVEAANKAIESeSGKNFELIVAAQEIAACTTQMVIASKVKAERNSQKLTDLTKASRSV 1015
Cdd:pfam01608 1 KNNRWTEGLISAAKAVAAATNLLVEAADGVVQG-QGSEEELIVAAKEVAASTAQLVAASRVKADPNSKTQQRLEAASKAV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 1016 TQATGTLVATVKDCNSQLEQQ--SEIELSKLTPSQIKTMEMEIHVKVLEIEQALQMQRLKLSSFRKEHYK 1083
Cdd:pfam01608 80 TDATKNLVAAVKSAAELQEEEieEEMDFSKLSLHQAKRQEMEAQVEILKLEKELEEARKKLAEIRKAHYH 149
|
|
| ANTH_N_HIP1_like |
cd17006 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
1-88 |
2.75e-42 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.
Pssm-ID: 340803 Cd Length: 114 Bit Score: 150.13 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 1 MIHKAKEAKTFWMIISRQPLMQSRFTAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWGLLQDDIGCCIQAYSKL 80
Cdd:cd17006 27 GTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRSRLKELGKLWGHLKDGYGKLIAQYCKL 106
|
....*...
gi 24663450 81 LATKLNFH 88
Cdd:cd17006 107 LITKLEFH 114
|
|
| ANTH_N_HIP1R |
cd17014 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
3-88 |
2.45e-22 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.
Pssm-ID: 340811 Cd Length: 114 Bit Score: 93.01 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 3 HKAKEAKTFWMIISRQPLMQSRFTAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWGLLQDDIGCCIQAYSKLLA 82
Cdd:cd17014 29 HHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRSNIRETGSLWGHLHDRYGQLVSLYTKLLC 108
|
....*.
gi 24663450 83 TKLNFH 88
Cdd:cd17014 109 TKIEFH 114
|
|
| ANTH_N_HIP1 |
cd17013 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ... |
3-88 |
1.48e-20 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.
Pssm-ID: 340810 Cd Length: 114 Bit Score: 88.17 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 3 HKAKEAKTFWMIISRQPLMQSRFTAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWGLLQDDIGCCIQAYSKLLA 82
Cdd:cd17013 29 HHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKNELSDMSRMWGHLSEGYGQLCSIYLKLLI 108
|
....*.
gi 24663450 83 TKLNFH 88
Cdd:cd17013 109 TKMEFH 114
|
|
| ENTH |
smart00273 |
Epsin N-terminal homology (ENTH) domain; |
3-95 |
5.46e-14 |
|
Epsin N-terminal homology (ENTH) domain;
Pssm-ID: 214594 Cd Length: 127 Bit Score: 69.58 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 3 HKAKEAKTFWMIISRQPLMQSRF--TAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWGLLQD--DIGCCIQAYS 78
Cdd:smart00273 31 HNEKSSFAEIMAVLWRRLNDTKNwrVVYKALILLHYLLRNGSPRVILEALRNRNRILNLSDFQDIDSRgkDQGANIRTYA 110
|
90
....*....|....*..
gi 24663450 79 KLLATKLNFHDKNRMFP 95
Cdd:smart00273 111 KYLLERLEDDRRLKEER 127
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-746 |
9.71e-12 |
|
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: 69.28 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 275 QQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNDlvlaremcatfRMQNDDLEMQLNQ 354
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN-----------NKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 355 npilLQKAMEEEEKHKlSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEE 434
Cdd:TIGR04523 293 ----LKSEISDLNNQK-EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 435 KEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAES 514
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 515 QINAK----------TEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSE------AQNAQLQEIMDNLEQKDKEFNEVKL 578
Cdd:TIGR04523 448 QDSVKeliiknldntRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelkklnEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 579 QLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLGIEhKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNqLRQEN 658
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD-LIKEI 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 659 ASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQIcstdLSELRKLVIKTVKEICNSKlsgseqqpldavPNIIREME 738
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK----LKQEVKQIKETIKEIRNKW------------PEIIKKIK 669
|
....*...
gi 24663450 739 TILNKFNN 746
Cdd:TIGR04523 670 ESKTKIDD 677
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
433-688 |
5.38e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 433 EEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNA 512
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 513 ESQINAKTEDIEkmlkafEAEKALLltQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKAL 592
Cdd:COG1196 301 EQDIARLEERRR------ELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 593 EIQNNLKAFEAEKSVLLTKIEQLgIEHKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLRQENASAGQRNEDLQSKL 672
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250
....*....|....*.
gi 24663450 673 SLTEVKLTQATQQIDA 688
Cdd:COG1196 452 AELEEEEEALLELLAE 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
272-615 |
7.71e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 272 SQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNT---VLSNDLVLAREMCATFRMQNDDL 348
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 349 EMQLNQnpilLQKAMEEEEKHkLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKI 428
Cdd:TIGR02169 771 EEDLHK----LEEALNDLEAR-LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 429 KVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEK 508
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 509 LSNAESQinaktediekmLKAFEAEKAllltqieqqSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLqLSSAESQIS 588
Cdd:TIGR02169 926 LEALEEE-----------LSEIEDPKG---------EDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM-LAIQEYEEV 984
|
330 340
....*....|....*....|....*...
gi 24663450 589 LKAL-EIQNNLKAFEAEKSVLLTKIEQL 615
Cdd:TIGR02169 985 LKRLdELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-649 |
2.92e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 361 KAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLlletKELTNEISKIKVNVEEKEKTNL 440
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 441 ILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKT 520
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 521 EDIEKMLKAFEAEKALLLTQIEQQSVESK--SHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQNNL 598
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24663450 599 KAFEAEKSVLLTKIEQLGIEHKnNSEAQNAQLQLTLNNLEQNESALQQTQE 649
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAA-LLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-688 |
3.58e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 414 LLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDvvKQKEIQELDIistsenlrlncl 493
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE--AQAEEYELLA------------ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 494 KVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQsveskshsEAQNAQLQEIMDNLEQKDKEF 573
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL--------EEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 574 NEVKLQLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSEAQNAQLQLtLNNLEQNESALQQTQEIVNQ 653
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL-EEALAELEEEEEEEEEALEE 446
|
250 260 270
....*....|....*....|....*....|....*
gi 24663450 654 LRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDA 688
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-704 |
4.91e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 407 EKQVNSqlLLETKELTNEISKIKVNVEEKEKTnlILQKQIEEHKEKIAHLEAVKNEMKEKFDDvvKQKEIQELDiistse 486
Cdd:TIGR02168 199 ERQLKS--LERQAEKAERYKELKAELRELELA--LLVLRLEELREELEELQEELKEAEEELEE--LTAELQELE------ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 487 nlrlncLKVEELN---GNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESkshsEAQNAQLQEIM 563
Cdd:TIGR02168 267 ------EKLEELRlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL----EELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 564 DNLEQKDKEFNEVKLQLSSAESQISLKALEIQNnLKAFEAEKSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNLEQNESA 643
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEE-LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24663450 644 LQQTQEIVNQLRQENASA------------GQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELR 704
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
417-695 |
1.75e-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: 62.00 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 417 ETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIqeldiistsenLRLNCLKVE 496
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-----------LEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 497 ELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNAqLQEIMDNLEQkdkEFNEV 576
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNE---EAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 577 KLQLSSAESQISLKALEIQNNLKAFE-------------AEKSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNLEQNESA 643
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEelsedieslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24663450 644 LQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLtqaTQQIDAVTSSYQI 695
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRI---DNLQERLSEEYSL 951
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
224-735 |
5.44e-09 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 60.69 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 224 PELPDSSPNFKSQNDFTSYVPP-----VVHVPQEPDPVVEDL-VDTNNHELEAFSQAQQQLSMLEGIISEKEASIEELSF 297
Cdd:PLN02939 56 PKQRSSNSKLQSNTDENGQLENtslrtVMELPQKSTSSDDDHnRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 298 KLDAMQKNFDALQQSyrhDVQELQQNNTVLSNDLVLAREMcatfrmqnDDLEMQLNQNPILLQKAMEEEEKHKLSSEKFN 377
Cdd:PLN02939 136 MIQNAEKNILLLNQA---RLQALEDLEKILTEKEALQGKI--------NILEMRLSETDARIKLAAQEKIHVEILEEQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 378 KLktlytkiRDEHIQLLREQSDCNKSLNKEKQVnsqLLLETKELTNEISKIK---VNVEEKEKTNLILQKQIeehkekiA 454
Cdd:PLN02939 205 KL-------RNELLIRGATEGLCVHSLSKELDV---LKEENMLLKDDIQFLKaelIEVAETEERVFKLEKER-------S 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 455 HLEAVKNEMKEKFddVVKQKEIQELDiistseNLRLNCL--KVEelngNLNDTLEKLSNaesqinaktediekmlkafEA 532
Cdd:PLN02939 268 LLDASLRELESKF--IVAQEDVSKLS------PLQYDCWweKVE----NLQDLLDRATN-------------------QV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 533 EKALLLTQieqqsveskshseaQNAQLQEIMDNLEQKDKEFNEVKLqlssaesqiSLKALEI-QNNLKAFEAEksvlltk 611
Cdd:PLN02939 317 EKAALVLD--------------QNQDLRDKVDKLEASLKEANVSKF---------SSYKVELlQQKLKLLEER------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 612 ieqlgieHKNNSEAQNAQLQLTlnnleqnESALQQTQEIVNQLRQE------NASAGQRNEDLQSKLSLTevkltqatqq 685
Cdd:PLN02939 367 -------LQASDHEIHSYIQLY-------QESIKEFQDTLSKLKEEskkrslEHPADDMPSEFWSRILLL---------- 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24663450 686 IDAVTSSYQICSTDLSELRKLVIKTVKEICNSKLSGSEQQPLDAVPNIIR 735
Cdd:PLN02939 423 IDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGKNEREAVENFLK 472
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
316-637 |
5.81e-09 |
|
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: 60.84 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 316 DVQELQQNNTVLSNdLVLAREMCATFRMQNDDlemQLNQNPILLQKAME---EEEKHKLSSEKFNKlktlyTKIRDEHIQ 392
Cdd:TIGR01612 1416 DIDECIKKIKELKN-HILSEESNIDTYFKNAD---ENNENVLLLFKNIEmadNKSQHILKIKKDNA-----TNDHDFNIN 1486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 393 LLREQSDCNKSLNKEKQVNSQLLLETKELTNEISK-------------IKVNVEEKEKTNLILQKQIEEHKEKIAhLEAV 459
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKdvtellnkysalaIKNKFAKTKKDSEIIIKEIKDAHKKFI-LEAE 1565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 460 KNEMK------EKF---DDVVKQKEIQE--LDIISTSENLRLNCLKVEELNGNLNDTLEklsnaesqinaKTEDIEKMLK 528
Cdd:TIGR01612 1566 KSEQKikeikkEKFrieDDAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLK-----------ETESIEKKIS 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 529 AFeaekallltQIEQQSVESKSHSEAQNAqLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQNNLKAFEAEksvL 608
Cdd:TIGR01612 1635 SF---------SIDSQDTELKENGDNLNS-LQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIG---I 1701
|
330 340
....*....|....*....|....*....
gi 24663450 609 LTKIEQLGIEHKNNSEAQNAQLQLTLNNL 637
Cdd:TIGR01612 1702 IEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-674 |
6.11e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 442 LQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTE 521
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 522 DIEKMLKA------FEAEKALLLTQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQ 595
Cdd:COG4942 105 ELAELLRAlyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 596 NNLKAFEAEKSVLLTKIEQLgiehknnsEAQNAQLQLTLNNLEQNESALQQTQE--IVNQLRQENASAGQRNEDLQSKLS 673
Cdd:COG4942 185 EERAALEALKAERQKLLARL--------EKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGKLP 256
|
.
gi 24663450 674 L 674
Cdd:COG4942 257 W 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
325-644 |
1.17e-08 |
|
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: 59.31 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 325 TVLSNDLVLAREMCATFRMQNDDLEmqlnqnpiLLQK--AMEEEEKHKLSSEKFN-KLKTLYTKIRDEHIQLLREQSDCN 401
Cdd:TIGR02169 623 TLVVEDIEAARRLMGKYRMVTLEGE--------LFEKsgAMTGGSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQ 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 402 KSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDI 481
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 482 isTSENLRLNCLKVEELNG---NLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIeQQSVESKSHSEAQNAQ 558
Cdd:TIGR02169 775 --HKLEEALNDLEARLSHSripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-QELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 559 LQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLGIEhKNNSEAQNAQLQLTLNNLE 638
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALE 930
|
....*.
gi 24663450 639 QNESAL 644
Cdd:TIGR02169 931 EELSEI 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-617 |
1.18e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 274 AQQQLSMLEGIISEKEASIEELSFKLDAMQKnfdalQQSYRHDVQELQQnnTVLSNDLVLAREMCATFRMQNDDLEMQLN 353
Cdd:TIGR02168 184 TRENLDRLEDILNELERQLKSLERQAEKAER-----YKELKAELRELEL--ALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 354 QNPILLQKAMEEEEKHKLsseKFNKLKTLYTKIRDEHIQLLREQSDCNKSL----NKEKQVNSQLLLETKELTNEISKI- 428
Cdd:TIGR02168 257 ELTAELQELEEKLEELRL---EVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKLd 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 429 --KVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTL 506
Cdd:TIGR02168 334 elAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 507 EKLSNAESQINaktEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQ 586
Cdd:TIGR02168 414 DRRERLQQEIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350
....*....|....*....|....*....|..
gi 24663450 587 I-SLKALEiQNNLKAFEAEKSVLLTKIEQLGI 617
Cdd:TIGR02168 491 LdSLERLQ-ENLEGFSEGVKALLKNQSGLSGI 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-705 |
1.91e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 257 VEDLVDTNNHELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQsyrhDVQELQQNNTVLSNDLVLARE 336
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK----ELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 337 MCATFRMQNDDLEMQLNQNPILLQKAMEEEEKHKLSSE---KFNKLKTLYTKIRDEHIQLLREQSDCNKslnKEKQVNsQ 413
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyldELREIEKRLSRLEEEINGIEERIKELEE---KEERLE-E 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 414 LLLETKELTNEISKIKVNVEEKEKTnLILQKQIEEHKEKIAHLEavKNEMKEKFDDVVKQKEIQELDIISTSEnlRLNCL 493
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITA--RIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 494 KVEElnGNLNDTLEKLSNAE--------------------------SQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVE 547
Cdd:PRK03918 418 KKEI--KELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 548 SKSHSEAQnaQLQEI--------MDNLEQKDKEFNEVKLQLSSAESQISLKALEIqNNLKAFEAEKSVLLTKIEQLgieH 619
Cdd:PRK03918 496 IKLKELAE--QLKELeeklkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDEL---E 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 620 KNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLrQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTD 699
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
....*.
gi 24663450 700 LSELRK 705
Cdd:PRK03918 649 LEELEK 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
265-714 |
2.50e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 265 NHELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNDLVLAREMCATFRMQ 344
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 345 NDDLEMQLNQNPILLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNE 424
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 425 ISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELngnlnD 504
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA-----A 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 505 TLEKLSNAESQINAKTEDIEKMLKAFEAEKA------LLLTQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKL 578
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 579 QLSSAESQISLKALEIQNNLKAFEAE---------------------KSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNL 637
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRlrevtlegeggsaggsltggsRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24663450 638 EQNESALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVIKTVKEI 714
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
273-609 |
3.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 273 QAQQQLSMLEGIISEKEASIEELsfKLDAMQ-KNFDALQQSYR--------HDVQELQQNNTVLSNDLVLAREMCATFRM 343
Cdd:COG1196 183 ATEENLERLEDILGELERQLEPL--ERQAEKaERYRELKEELKeleaelllLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 344 QNDDLEMQLNqnpillqkamEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTN 423
Cdd:COG1196 261 ELAELEAELE----------ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 424 EISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVV---KQKEIQELDIISTSENLRlncLKVEELNG 500
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEeelEELAEELLEALRAAAELA---AQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 501 NLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSvESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQL 580
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340
....*....|....*....|....*....
gi 24663450 581 SSAESQISLKALEIQNNLKAFEAEKSVLL 609
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-685 |
3.66e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 333 LAREMcATFRMQNDDLE------MQLNQNPILLQKAMEEEEKHKLSSEKFNK-LKTLYTKIRDEHIQLLREQSDCNK--- 402
Cdd:pfam15921 446 MERQM-AAIQGKNESLEkvssltAQLESTKEMLRKVVEELTAKKMTLESSERtVSDLTASLQEKERAIEATNAEITKlrs 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 403 SLNKEKQVNSQLLLETKELTN---EISKIKVNVEEKEKTNLILQKQIE-------EHKEKIAHLEAVKNEMKEKFDDvvK 472
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIEnmtqlvgQHGRTAGAMQVEKAQLEKEIND--R 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 473 QKEIQELDIISTSENLrlnclKVEELNGNLND-TLEKLSnaesQINAKTEDIeKMLKAFEAEKALLLTQIEQQSVESKSH 551
Cdd:pfam15921 603 RLELQEFKILKDKKDA-----KIRELEARVSDlELEKVK----LVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSL 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 552 SEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQI-----SLKALE------------IQNNLKAFEAEKSVLLTKIEQ 614
Cdd:pfam15921 673 SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSKIQF 752
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24663450 615 LGiEHKNNSEAQNAQLQLTLNNLEQNESALQQTQeivNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQ 685
Cdd:pfam15921 753 LE-EAMTNANKEKHFLKEEKNKLSQELSTVATEK---NKMAGELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
275-684 |
4.18e-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: 57.42 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 275 QQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNdlvLAREMcatfrmqnDDLEMQLnQ 354
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH---LTKEL--------EDIKMSL-Q 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 355 NPILLQKAMEEE------------EKHKLSSEKFNKLKTLYTKIRDEHI-------QLLR-EQSDCNKSLNKEKQVNSQL 414
Cdd:pfam05483 307 RSMSTQKALEEDlqiatkticqltEEKEAQMEELNKAKAAHSFVVTEFEattcsleELLRtEQQRLEKNEDQLKIITMEL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 415 LLETKELtNEISKIKVNVE-EKEKTNLIL---QKQIEEHKEkiahLEAVKNEMKEKFDDVV-----KQKEIQELDI---- 481
Cdd:pfam05483 387 QKKSSEL-EEMTKFKNNKEvELEELKKILaedEKLLDEKKQ----FEKIAEELKGKEQELIfllqaREKEIHDLEIqlta 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 482 ISTSENLRLNclKVEELNGNLNDtlEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSE----AQNA 557
Cdd:pfam05483 462 IKTSEEHYLK--EVEDLKTELEK--EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 558 QLQE----IMDNLEQKDKEF----NEVKLQLSSAESQISLKALEIQ-------------NNLKAFEAEKSVLLTKIEQLG 616
Cdd:pfam05483 538 NLEEkemnLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLkkekqmkilenkcNNLKKQIENKNKNIEELHQEN 617
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24663450 617 IEHKNNSEAQNAQL---QLTLNNLE-QNESALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQ 684
Cdd:pfam05483 618 KALKKKGSAENKQLnayEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
345-678 |
9.93e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 345 NDDLEMQLNQNPILLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNE 424
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 425 ISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKfdDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLND 504
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 505 TLEKLSNAESQINAKTEDIEK---MLKAFEAEKALLLTQIEQQsvesKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLS 581
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEkqnEIEKLKKENQSYKQEIKNL----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 582 SAESQIS-LKALEIQNN--LKAFEAEKSVLLTKIEQLGI---EHKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLR 655
Cdd:TIGR04523 423 LLEKEIErLKETIIKNNseIKDLTNQDSVKELIIKNLDNtreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
330 340
....*....|....*....|...
gi 24663450 656 QENASAGQRNEDLQSKLSLTEVK 678
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEK 525
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
357-1086 |
2.27e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 357 ILLQKAMEEEEKHKLsSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKqvnsQLLLETKELTNEISKIKVNVEEKE 436
Cdd:pfam02463 164 GSRLKRKKKEALKKL-IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ----LKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 437 KTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVV-----KQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSN 511
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 512 AESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVEskshsEAQNAQLQEIMDNLEQKdKEFNEVKLQLSSAESQISLKA 591
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE-----EEEEEELEKLQEKLEQL-EEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 592 LEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSEAQNA-------QLQLTLNNLEQNESALQQTQEIVNQLRQENASAGQR 664
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELeileeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 665 NEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVIKTVKEICNSKLSGSEQQPLDAVPNIIREMETILNKF 744
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 745 NNASAINYVASTEGLQNV--MYLGYVFIKLYDQCDVIYKTTTAIETGQEIFSKTNLLCTDICQLFQYLLNNETKEPERQK 822
Cdd:pfam02463 553 VSATADEVEERQKLVRALteLPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 823 TITDIQTKLRDIE-----------KLIEKIKASFEQKIDLDKLLEIELREMDAAIDDAASKI---------TDLLAKARE 882
Cdd:pfam02463 633 ELTKLKESAKAKEsglrkgvsleeGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIlrrqleikkKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 883 KDNQTNLEV--NGKIVDACTTLMECVKALIQKSRLLQHEIVASQKGNASANEFYRRNSQWSDGLI-SASKSVAKAANYLV 959
Cdd:pfam02463 713 KKLKLEAEEllADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAeEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 960 EAANKAIESESGKNFEL----IVAAQEIAACTTQMVIASKVKAERNSQKLTDLTKASRSVTQATGTLVA--TVKDCNSQL 1033
Cdd:pfam02463 793 EEKLKAQEEELRALEEElkeeAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEeiTKEELLQEL 872
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 24663450 1034 EQQSEIELSKLTPSQIKTMEMEIHVKVLEIEQALQMQRLKLSSFRKEHYKNAD 1086
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
472-705 |
5.44e-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: 53.91 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 472 KQKEIQELDIISTSENL-RLNCLkVEELNGNLNdTLEKLSNAESQINAKTEDIEkmlkafEAEKALLLTQIEQQsVESKS 550
Cdd:TIGR02168 172 ERRKETERKLERTRENLdRLEDI-LNELERQLK-SLERQAEKAERYKELKAELR------ELELALLVLRLEEL-REELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 551 HSEAQNAQLQEIMDNLE----QKDKEFNEVKLQLSSAESQIslkaLEIQNNLKAFEAEKSVLLTKIEQLGiEHKNNSEAQ 626
Cdd:TIGR02168 243 ELQEELKEAEEELEELTaelqELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILR-ERLANLERQ 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24663450 627 NAQLQLTLnnlEQNESALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRK 705
Cdd:TIGR02168 318 LEELEAQL---EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
267-687 |
7.97e-07 |
|
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: 53.43 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 267 ELEAFSQAQQQLSMLEGII-------SEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNT-------------- 325
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQelqqryaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlqetrkkavvla 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 326 VLSNDLVLAREMCATFRMQNddLEMQLNQNPILLQKAMEE-EEKHKLSSEKFNKLKTLYTKIRdEHIQLLREQSdcnKSL 404
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIHPN--PARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVYHQLTSER-KQRASLKEQM---QEI 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 405 NKEKQVNSQLLLETKELTNEISKIKVNVEEkektnlILQKQIEEHKEKIAHLEAVKNEMKEKFDDvvkQKEIQELDIIST 484
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNITVRLQD------LTEKLSEAEDMLACEQHALLRKLQPEQDL---QDVRLHLQQCSQ 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 485 SENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKallltqieQQSVESKSHSEAQNAQLQEIMD 564
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK--------EQLTYWKEMLAQCQTLLRELET 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 565 NLEQKDKEFNEVKLQLSSAESQISLKALEIQNNLKAFEAEKSvllTKIEQLGIEHKNNSEAQNAQLQL--TLNNLEQN-E 641
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR---TVLKARTEAHFNNNEEVTAALQTgaELSHLAAEiQ 788
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 24663450 642 SALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQID 687
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
358-714 |
1.88e-06 |
|
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: 51.94 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 358 LLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDehiqLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEK 437
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKI----LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 438 TNLILQKQIEEHKEKIA-------HLEAVKNEMKEKFDDVVKQKEIQE----------LDIISTSENLRLNCLKVEELNG 500
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELEnelnllekekLNIQKNIDKIKNKLLKLELLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 501 NL------NDTLE-KLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNaQLQEIMDNLEQKDKEF 573
Cdd:TIGR04523 205 NLkkkiqkNKSLEsQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK-QLSEKQKELEQNNKKI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 574 NEVKLQLSSAESQIS-LKALEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSEAQN------AQLQLTLNNLEQNESALQ- 645
Cdd:TIGR04523 284 KELEKQLNQLKSEISdLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqiSQLKKELTNSESENSEKQr 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24663450 646 ---QTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQ-------QIDAVTSSYQICSTDLSELRKLVIKTVKEI 714
Cdd:TIGR04523 364 eleEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqqkdeQIKKLQQEKELLEKEIERLKETIIKNNSEI 442
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
402-690 |
1.98e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 402 KSLNKEKQVNSQLLLETKELTNEISKIKvNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQkeiqeldi 481
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 482 istsenlRLNCLKVEELNGNLNDTLEKLSNAESQinaktediekmlkafeaekallLTQIEQQSVESKSHSE-AQNA--- 557
Cdd:PRK11281 117 -------TLSTLSLRQLESRLAQTLDQLQNAQND----------------------LAEYNSQLVSLQTQPErAQAAlya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 558 ---QLQEI---MDNLEQKDKEFNEVKLQLSSAEsqisLKALEIQNNLKAFEAEKSVLLTKIEQLGIEHKNnseAQNAQLQ 631
Cdd:PRK11281 168 nsqRLQQIrnlLKGGKVGGKALRPSQRVLLQAE----QALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLT---ARIQRLE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24663450 632 LTLNNLEQ--NESALQQTQEIVNQLR-QENASAGQRNEDLQSKLS----LTEvKLTQATQQIDAVT 690
Cdd:PRK11281 241 HQLQLLQEaiNSKRLTLSEKTVQEAQsQDEAARIQANPLVAQELEinlqLSQ-RLLKATEKLNTLT 305
|
|
| ANTH_N_Sla2p |
cd17007 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ... |
6-88 |
2.18e-06 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.
Pssm-ID: 340804 Cd Length: 115 Bit Score: 47.69 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 6 KEAKTFWMIISRQPLMQSRFTAWKFSHLLHKVLREGHESAIRHSQSHKKMILEVGKMWGL-LQDDIGCCIQAYSKLLATK 84
Cdd:cd17007 32 KSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWLESLGRQSSGsGAKGYGRLIKEYVRYLLDK 111
|
....
gi 24663450 85 LNFH 88
Cdd:cd17007 112 LAFH 115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
396-591 |
2.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 396 EQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQ-- 473
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 474 ---KEIQELDIISTSENL-----RLNCLKV-----EELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQ 540
Cdd:COG3883 97 rsgGSVSYLDVLLGSESFsdfldRLSALSKiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24663450 541 IEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKA 591
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
275-744 |
2.60e-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: 51.66 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 275 QQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQ--------QSYRHDVQELQQNNTVLSNDLVLAREMCATFRMQND 346
Cdd:pfam15921 263 QQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQsqleiiqeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 347 DLEmQLNQNPILLQKAMEE--EEKHKLSSEKFNklktlytkIRDEHIQLLREQSDCNKSLNKEKQVNSQLLleTKELTNE 424
Cdd:pfam15921 343 KIE-ELEKQLVLANSELTEarTERDQFSQESGN--------LDDQLQKLLADLHKREKELSLEKEQNKRLW--DRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 425 IskikvnveekekTNLILQKQIEEHKEKIAHLEAVKNEMKEkfdDVVKQKEIQELDIISTSENLRlnclKVEELNGNLND 504
Cdd:pfam15921 412 I------------TIDHLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLE----KVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 505 TLEKLSNAESQINAKTEDIEKMLKAF--------EAEKALLLTQIEQQSVESKSHSEAQNAQ-LQEIMDNLEQKDKEFNE 575
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVsdltaslqEKERAIEATNAEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 576 VKLQLSSAESQISLKALEIQNnlkafeaeksvlltkIEQLGIEHKNNSEA---QNAQLQLTLNN--LEQNESALqqtqei 650
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIEN---------------MTQLVGQHGRTAGAmqvEKAQLEKEINDrrLELQEFKI------ 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 651 vnqLRQENASAGQRNEDLQSKLSLTEVKLTQA-TQQIDAVtssyqicsTDLSELRKLVIKTVKEICNSKLSGSEQQPL-- 727
Cdd:pfam15921 612 ---LKDKKDAKIRELEARVSDLELEKVKLVNAgSERLRAV--------KDIKQERDQLLNEVKTSRNELNSLSEDYEVlk 680
|
490
....*....|....*..
gi 24663450 728 DAVPNIIREMETILNKF 744
Cdd:pfam15921 681 RNFRNKSEEMETTTNKL 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-591 |
6.98e-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: 49.76 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 392 QLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVV 471
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 472 ----KQKEIQELDIISTSENL-----RLNCLK-----VEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALL 537
Cdd:COG4942 111 ralyRLGRQPPLALLLSPEDFldavrRLQYLKylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24663450 538 LTQIEQQSVESKSHSEAQNAQLQEimdnLEQKDKEFNEVKLQLSSAESQISLKA 591
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-586 |
8.44e-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: 50.07 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 268 LEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKnFDALQQsyrhDVQELQQnnTVLSNDLVLAREMCATFRMQNDD 347
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLK----EKREYEG--YELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 348 LEMQLNQNPILLQkameeeEKHKLSSEKFNKLKTLYTKIRDehiqllreqsdcnKSLNKEKQVNSQLLletkELTNEISK 427
Cdd:TIGR02169 249 LEEELEKLTEEIS------ELEKRLEEIEQLLEELNKKIKD-------------LGEEEQLRVKEKIG----ELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 428 IKVNVEEK-------EKTNLILQKQIEEHKEKIAHLE-----------AVKNEMKEKFDDV-VKQKEIQELDIIS----- 483
Cdd:TIGR02169 306 LERSIAEKereledaEERLAKLEAEIDKLLAEIEELEreieeerkrrdKLTEEYAELKEELeDLRAELEEVDKEFaetrd 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 484 --TSENLRLNCLK--VEELNGN---LNDTLEKLSNAESQINAKTEDIEKMLKAFEAE---KALLLTQIEQQSVESKSHSE 553
Cdd:TIGR02169 386 elKDYREKLEKLKreINELKREldrLQEELQRLSEELADLNAAIAGIEAKINELEEEkedKALEIKKQEWKLEQLAADLS 465
|
330 340 350
....*....|....*....|....*....|...
gi 24663450 554 AQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQ 586
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
417-688 |
8.66e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 417 ETKELTNEISK------IKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKekfddvvkqkeiQELDIISTSENLRL 490
Cdd:COG3206 149 LAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 491 NCLKVEELNGNLNDTLEKLSNAESQINAktedIEKMLKAFEAEKALLLTQIEQQSVESKshSEAQNAQLQEIMDNLEQKD 570
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 571 KEFNEVKLQLSSAESQIslkALEIQNNLKAFEAEKSVLltkieqlgiehknnsEAQNAQLQLTLNNLEQNESALQQTQEI 650
Cdd:COG3206 291 PDVIALRAQIAALRAQL---QQEAQRILASLEAELEAL---------------QAREASLQAQLAQLEARLAELPELEAE 352
|
250 260 270
....*....|....*....|....*....|....*...
gi 24663450 651 VNQLRQENASAGQRNEDLQSKlsLTEVKLTQATQQIDA 688
Cdd:COG3206 353 LRRLEREVEVARELYESLLQR--LEEARLAEALTVGNV 388
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
452-693 |
1.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 452 KIAHLEAVKNEMKEKFDDVvkQKEIQELDiistsenlrlncLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFE 531
Cdd:COG3883 17 QIQAKQKELSELQAELEAA--QAELDALQ------------AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 532 AEKALLLTQIEQQSVESKSHS------EAQNAQ--------LQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQNN 597
Cdd:COG3883 83 ERREELGERARALYRSGGSVSyldvllGSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 598 LKAFEAEKSVLLTKIEQLgiehKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEV 677
Cdd:COG3883 163 KAELEAAKAELEAQQAEQ----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|....*.
gi 24663450 678 KLTQATQQIDAVTSSY 693
Cdd:COG3883 239 AAAAAASAAGAGAAGA 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
501-694 |
1.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 501 NLNDTLEKLSNAESQINAKTEDIEKMLKafEAEKALLLTQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQL 580
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELE--EAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 581 SSAESQISLKALEIQNNLKAfeAEKSVLLTKIEQLGIEHKNNSE---AQNAQLQLTLNNLEQNESALQQ-TQEIVNQLRQ 656
Cdd:COG3206 243 AALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytPNHPDVIALRAQIAALRAQLQQeAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24663450 657 ENASAGQRNEDLQ----------SKLSLTEVKLTQATQQIDAVTSSYQ 694
Cdd:COG3206 321 ELEALQAREASLQaqlaqlearlAELPELEAELRRLEREVEVARELYE 368
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
257-620 |
3.39e-05 |
|
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: 48.18 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 257 VEDLVDTNNHELEafsQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTV--LSNDLVlA 334
Cdd:pfam05483 361 LEELLRTEQQRLE---KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFekIAEELK-G 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 335 REMCATFRMQN-----DDLEMQLNqnpillqkAMEEEEKHKLssekfNKLKTLYTKIRDEHIQLLREQSDCNKslnkekq 409
Cdd:pfam05483 437 KEQELIFLLQArekeiHDLEIQLT--------AIKTSEEHYL-----KEVEDLKTELEKEKLKNIELTAHCDK------- 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 410 vnsqLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEA----VKNEMKEKFDDVVKQKEIQELDIISTS 485
Cdd:pfam05483 497 ----LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDKSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 486 ENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMlkafeaekallltQIEQQSVESKSHSEAQNAQLQEIMDN 565
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL-------------HQENKALKKKGSAENKQLNAYEIKVN 639
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24663450 566 -----LEQKDKEFNEVklqLSSAESQISLKALEIQNNLKAFE-----AEKSVLLTKIEQLGIEHK 620
Cdd:pfam05483 640 kleleLASAKQKFEEI---IDNYQKEIEDKKISEEKLLEEVEkakaiADEAVKLQKEIDKRCQHK 701
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
408-734 |
4.01e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 408 KQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIeehKEKIAHLEAVKNEMKEKFDDVVKQKEIQEL-----DII 482
Cdd:COG5185 183 GLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTL---LEKAKEIINIEEALKGFQDPESELEDLAQTsdkleKLV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 483 STSENLRLNCL-----KVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNA 557
Cdd:COG5185 260 EQNTDLRLEKLgenaeSSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 558 QLQEIMD------------------------NLEQKDKEFNEVKLQLSSAESQISLKALEI----QNNLKAFEAEKSVLL 609
Cdd:COG5185 340 NLTAEIEqgqesltenleaikeeienivgevELSKSSEELDSFKDTIESTKESLDEIPQNQrgyaQEILATLEDTLKAAD 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 610 TKIEQLG--IEHKNNSEAQNAQLQLTL----------NNLEQNESALQQTQEIVNQLRQENASAGQRNEDLQSKLS---- 673
Cdd:COG5185 420 RQIEELQrqIEQATSSNEEVSKLLNELiselnkvmreADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVStlka 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24663450 674 ---LTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVIKTVKEICNSKLSGSEQQPLDAVPNII 734
Cdd:COG5185 500 tleKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAA 563
|
|
| ANTH_N_Sla2p_HIP1_like |
cd16986 |
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ... |
3-88 |
4.58e-05 |
|
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.
Pssm-ID: 340783 Cd Length: 117 Bit Score: 43.91 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 3 HKAKEAKTFWMIISRqPLMQSRFTAWKFSHLLHKVLREGHE--SAIRHSQSHKKMILE-VGKMWGLLQDDIGCCIQAYSK 79
Cdd:cd16986 30 THQKGPQFYEELSKR-LLLNNPVVQFKALVTLHKVLRDGPPelSLLGGYLDAWLPELVrVKNTQQSLSEFYSQLIKKYVR 108
|
....*....
gi 24663450 80 LLATKLNFH 88
Cdd:cd16986 109 YLELKVVFH 117
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-568 |
4.64e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 269 EAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLsndlvlaremcatfrmqnDDL 348
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL------------------DEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 349 EMQLNQNPILLQKAMEEEEKHKLSSEkfnKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKI 428
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIA---ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 429 KVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIistsENLRlnclkvEELNGNLNDTLEK 508
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI----DNLQ------ERLSEEYSLTLEE 955
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24663450 509 LSNAESQINAKTEDIEKMLKAFEAEKALL----LTQIE--QQSVESKSHSEAQNAQLQEIMDNLEQ 568
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEeyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
267-714 |
8.07e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 267 ELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNntvlsndlvLAREMCATFRMQND 346
Cdd:pfam01576 27 ELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR---------LEEEEERSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 347 DLEMQlnQNPILLQKAMEEEE--KHKLSSEKFnklkTLYTKIR--DEHIQLLREQsdcnkslnkekqvNSQLLLETKELT 422
Cdd:pfam01576 98 KKKMQ--QHIQDLEEQLDEEEaaRQKLQLEKV----TTEAKIKklEEDILLLEDQ-------------NSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 423 NEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEA-VKNEMKEKfDDVVKQKEIQELDIISTSENLRLNCLKVEELNGN 501
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErLKKEEKGR-QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 502 LNDTLEKLSNAESQINAKTED---IEKMLKAFEAEKALLLTQIEQQSVeSKSHSEAQNAQLQEIMDNLEqkdkefNEVKL 578
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERA-ARNKAEKQRRDLGEELEALK------TELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 579 QLSSAESQISLKA---LEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNN----------LEQNESALQ 645
Cdd:pfam01576 311 TLDTTAAQQELRSkreQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNkanlekakqaLESENAELQ 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24663450 646 QTQEIVNQLRQENASAGQRNE----DLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVIKTVKEI 714
Cdd:pfam01576 391 AELRTLQQAKQDSEHKRKKLEgqlqELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
495-691 |
8.10e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 495 VEELNGNLNDTLE-KLSNAESQINAKT-EDIEKMLKAFEAEKA------------LLLTQIEQQSVESKSHSEAQNAQLQ 560
Cdd:PRK10929 47 VEALQSALNWLEErKGSLERAKQYQQViDNFPKLSAELRQQLNnerdeprsvppnMSTDALEQEILQVSSQLLEKSRQAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 561 -------EIMDNLEQKDKEFNEVKLQLSSAESQISLK-----ALEiQNNLKAFEAEKSVLLTKIEQLGIE---------- 618
Cdd:PRK10929 127 qeqdrarEISDSLSQLPQQQTEARRQLNEIERRLQTLgtpntPLA-QAQLTALQAESAALKALVDELELAqlsannrqel 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 619 -------HKNNSEAQNAQLQL---TLNNLEQN--ESALQQTQEIVNQ---LRQENASAGQRNEDLQSKLSltevkltQAT 683
Cdd:PRK10929 206 arlrselAKKRSQQLDAYLQAlrnQLNSQRQReaERALESTELLAEQsgdLPKSIVAQFKINRELSQALN-------QQA 278
|
....*...
gi 24663450 684 QQIDAVTS 691
Cdd:PRK10929 279 QRMDLIAS 286
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
494-705 |
8.96e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 494 KVEELNGNLNDTLEKLSNAESQINAKTEDIEkmlkafEAEKALLLTQIEQQSVESKShsEAQNAQLQEIMDNLEQKDKEF 573
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELS------DASRKIGEIEKEIEQLEQEE--EKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 574 NEVKLQLSSAESQISLKALEIQNNLKAFEA-EKSVLLTKIEQLGiEHKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVN 652
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQ-AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24663450 653 QLRQE-----------NASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRK 705
Cdd:TIGR02169 833 KEIQElqeqridlkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
269-583 |
9.25e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 269 EAFSQ---AQQQLSMLEGIISEKEASIEELSFKLDAMQKnfdALQQSYRHDVQELQQNNTVLSNDLVLAREMCATFRMQN 345
Cdd:pfam12128 248 QEFNTlesAELRLSHLHFGYKSDETLIASRQEERQETSA---ELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 346 DDLEMQLnqnpilLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQllletkELTNEI 425
Cdd:pfam12128 325 EALEDQH------GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 426 SKIKvnveekEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENL--RLNCLKVEElngnln 503
Cdd:pfam12128 393 AGIK------DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklRLNQATATP------ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 504 DTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLtqieqqsvESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSA 583
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELR--------QARKRRDQASEALRQASRRLEERQSALDELELQLFPQ 532
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-657 |
1.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 408 KQVNS------QLLLETKELTNEISKIKVNVEEKEKTnlilQKQIEEHKEKIAHLEAVKnEMKEKFDDVVKQKEIQELDI 481
Cdd:COG4913 204 KPIGDlddfvrEYMLEEPDTFEAADALVEHFDDLERA----HEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 482 istsenLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNAQLQE 561
Cdd:COG4913 279 ------AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 562 IMDNLEQKDKEFNEV--KLQLSSAESQISLKAL--EIQNNLKAFEAEKSVLLTKIEQLGIEHKnNSEAQNAQLQLTLNNL 637
Cdd:COG4913 353 ELEERERRRARLEALlaALGLPLPASAEEFAALraEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIASL 431
|
250 260
....*....|....*....|.
gi 24663450 638 EQNESAL-QQTQEIVNQLRQE 657
Cdd:COG4913 432 ERRKSNIpARLLALRDALAEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
413-615 |
1.68e-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: 44.53 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 413 QLLLETKELTNEISKIKVNVEEkektnliLQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIistsenlrlnc 492
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 493 lkvEELNGNLNDTLEKLSNAESQinaktedieKMLKAFEAEKALLLTQIEQQsveskshseaqNAQLQEIMDNLEQKDKE 572
Cdd:COG1579 69 ---EEVEARIKKYEEQLGNVRNN---------KEYEALQKEIESLKRRISDL-----------EDEILELMERIEELEEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24663450 573 FNEVKLQLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQL 615
Cdd:COG1579 126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
504-688 |
1.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 504 DTLEKLSNAE---SQINAKTEDIEKMLKAFE--AEKAL----LLTQIEQQSVESKSHS-EAQNAQLQEIMDNLEQKDKEF 573
Cdd:COG1196 176 EAERKLEATEenlERLEDILGELERQLEPLErqAEKAEryreLKEELKELEAELLLLKlRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 574 NEVKLQLSSAESQIS---LKALEIQNNLKAFEAEKSVLLTKIEQL--GIEHKN--NSEAQNAQLQLTLNNLEQNESALQQ 646
Cdd:COG1196 256 EELEAELAELEAELEelrLELEELELELEEAQAEEYELLAELARLeqDIARLEerRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24663450 647 TQEIVnQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDA 688
Cdd:COG1196 336 EEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
426-625 |
2.03e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 426 SKIKVNVEE-KEKTNLI--LQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNL 502
Cdd:PHA02562 174 DKIRELNQQiQTLDMKIdhIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 503 NDTLEKLSNAESQINAKTEDIEKMLKAFE------------AEKALLLTQIEQQSVE-SKSHSEAQNA--QLQEIMDNLE 567
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqqiSEGPDRITKIKDKLKElQHSLEKLDTAidELEEIMDEFN 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24663450 568 QKDKEFNEVKLQLSSAESQISLkaleIQNNLKAFEAEksvlltkIEQLGIEHKNNSEA 625
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLIT----LVDKAKKVKAA-------IEELQAEFVDNAEE 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-671 |
2.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 359 LQKAMEEEEKH---KLSSEKFNKLKTLYTKIRDehiqllREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEK 435
Cdd:PTZ00121 1436 AKKKAEEAKKAdeaKKKAEEAKKAEEAKKKAEE------AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 436 EKTNlilqkQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRL--NCLKVEELNGNLNDTLEKLSNAE 513
Cdd:PTZ00121 1510 KKAD-----EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAE 1584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 514 SQINAKTEDIEKMLKAFEAEKALLLTQIEQQSvESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKL--QLSSAESQISLKA 591
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKA 1663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 592 LEIQNnlKAFEAEKSVLLTKIEQlgiEHKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLRQENASAGQRNEDLQSK 671
Cdd:PTZ00121 1664 AEEAK--KAEEDKKKAEEAKKAE---EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
357-726 |
3.40e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 357 ILLQKAMEEEEKHK-LSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISkikvnveek 435
Cdd:COG5022 846 VLIQKFGRSLKAKKrFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLS--------- 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 436 ekTNLILQKQIEEhkEKIAHLEAVKNEMkekfdDVVKQKEIQEldiistsenlrlnclkveelngNLNDTLEKLSNAESQ 515
Cdd:COG5022 917 --SDLIENLEFKT--ELIARLKKLLNNI-----DLEEGPSIEY----------------------VKLPELNKLHEVESK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 516 INAKTEDIEKMLKAFEAEKALLLTQIEqqsvESKSHSEAQNAQLQEIMDnLEQKDKEFNEVKLQLSSAESQIslkaleiq 595
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREGNKANS----ELKNFKKELAELSKQYGA-LQESTKQLKELPVEVAELQSAS-------- 1032
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 596 nNLKAFEAEKSVLLTKIEQLgiehKNNSEAQNAQLQLTLNNLE-QNESALQQTQEIVNQLRQENASAGQRNEDLQSKlSL 674
Cdd:COG5022 1033 -KIISSESTELSILKPLQKL----KGLLLLENNQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKDLEVT-NR 1106
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24663450 675 TEVKLTQATQQIDAVTSSYQICsTDLSELRKLVIKTVKEIcNSKLSGSEQQP 726
Cdd:COG5022 1107 NLVKPANVLQFIVAQMIKLNLL-QEISKFLSQLVNTLEPV-FQKLSVLQLEL 1156
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
263-695 |
3.52e-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: 44.73 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 263 TNNHELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNdlvlaremcatFR 342
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE-----------LQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 343 MQNDDLEMQLNQnpiLLQKAMEEEEKHKLSSEKFNKLKTLytkirDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELT 422
Cdd:pfam05557 139 ERLDLLKAKASE---AEQLRQNLEKQQSSLAEAEQRIKEL-----EFEIQSQEQDSEIVKNSKSELARIPELEKELERLR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 423 NEISKIKVNVEekekTNLILQKQIEEHKEKIAHLEAVKNEM------KEKFddvvkQKEIQELDIISTSENLRLNC---- 492
Cdd:pfam05557 211 EHNKHLNENIE----NKLLLKEEVEDLKRKLEREEKYREEAatleleKEKL-----EQELQSWVKLAQDTGLNLRSpedl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 493 -LKVEEL-NGNLNdtlekLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHsEAQNAQLQE--------- 561
Cdd:pfam05557 282 sRRIEQLqQREIV-----LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH-KALVRRLQRrvllltker 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 562 --IMDNLEQKDKEFNEVKlqLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNLEQ 639
Cdd:pfam05557 356 dgYRAILESYDKELTMSN--YSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24663450 640 NESAlqQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQI 695
Cdd:pfam05557 434 ADPS--YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKV 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-538 |
3.53e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 257 VEDLVDTNNHELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQnntvLSNDLVLARE 336
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 337 MCATFRMQNDDLEMQLNQnpiLLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLL 416
Cdd:COG1196 324 ELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 417 ETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDvvKQKEIQELDIISTSENLRLnclkvE 496
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE--LEEEEEALLELLAELLEEA-----A 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 24663450 497 ELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLL 538
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
285-705 |
3.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 285 ISEKEASIEELSFKLDAMQKNFDALQQSYR--HDVQELQQNNTVLSNDLVlaremcatfrmqnddlemqlNQNPILLQKA 362
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLT--------------------GLTPEKLEKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 363 MEEEEKHKLSSEKfnKLKTLYTKIRdehiQLLREQSDCNKSLNKEKQVNSQLLLETKELTNE-----ISKIKVNVEEKEK 437
Cdd:PRK03918 393 LEELEKAKEEIEE--EISKITARIG----ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEK 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 438 TNLILQKQIEEHKEKIAHLEAVKNEMKEkfddVVKQKEIQELdIISTSENLR-LNCLKVEELNGNLNDTLEKLSNAESQI 516
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 517 NAKTEDIEKmLKAFEAEKALLLTQIeqQSVESKshseaqnaqLQEIMDNLEQKD-KEFNEVKLQLSSAEsqislKALEIQ 595
Cdd:PRK03918 542 KSLKKELEK-LEELKKKLAELEKKL--DELEEE---------LAELLKELEELGfESVEELEERLKELE-----PFYNEY 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 596 NNLKAFEAEKSVLLTKIEQLgiehKNNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLRQENASagQRNEDLQSKLSLT 675
Cdd:PRK03918 605 LELKDAEKELEREEKELKKL----EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGL 678
|
410 420 430
....*....|....*....|....*....|
gi 24663450 676 EVKLTQATQQIDAVTSSYQICSTDLSELRK 705
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
425-714 |
3.96e-04 |
|
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: 44.65 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 425 ISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLE---AVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNgn 501
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRdqiTSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLD-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 502 lnDTLEKLSNAESQI-NAKTEDIEKMLKAFEAEKALL--LTQIEQQSVESKshsEAQNAQLQEIMDNLEQKDKEFNEVKL 578
Cdd:TIGR00606 269 --NEIKALKSRKKQMeKDNSELELKMEKVFQGTDEQLndLYHNHQRTVREK---ERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 579 QLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLGIEHKNNSE------------AQNAQLQLTLNNLEQNESALQQ 646
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSErqiknfhtlvieRQEDEAKTAAQLCADLQSKERL 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24663450 647 TQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSyqicSTDLSELRKLVIKTVKEI 714
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS----SDRILELDQELRKAEREL 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
287-707 |
3.97e-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: 44.78 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 287 EKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNDLVLAREMCATFRMQNDDLEMQLNQNPILLQKAMEEE 366
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 367 EKHklSSEKFNKLKtlytKIRDEHIQLLREQSDcnksLNKEKQVNSQLLLETKELTNEISKIKVNVE------------- 433
Cdd:pfam01576 253 EEE--TAQKNNALK----KIRELEAQISELQED----LESERAARNKAEKQRRDLGEELEALKTELEdtldttaaqqelr 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 434 ---EKEKTNLilQKQIEEhkEKIAHlEAVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLS 510
Cdd:pfam01576 323 skrEQEVTEL--KKALEE--ETRSH-EAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 511 NAESQINAKTEDIEKMLKAFEAEkallLTQIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQI--- 587
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQAR----LSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqdt 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 588 -------SLKALEIQNNLKAFEAEKSVLLTKIEQlGIEHKNNSEAQ----NAQLQLTLNNLEQNESALQQTQEIVNQLRQ 656
Cdd:pfam01576 474 qellqeeTRQKLNLSTRLRQLEDERNSLQEQLEE-EEEAKRNVERQlstlQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 24663450 657 ENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTssyqicsTDLSELRKLV 707
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLV 596
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
269-705 |
4.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 269 EAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQ----------QSYRHDVQELQQNNTVLSNDLVLAREMC 338
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEaqleelesklDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 339 ATFRMQNDDLEMQLNQnpilLQKAMEEEekhklsSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLET 418
Cdd:TIGR02168 361 EELEAELEELESRLEE----LEEQLETL------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 419 KEltNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEI--QELDIIST--------SENL 488
Cdd:TIGR02168 431 EE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqARLDSLERlqenlegfSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 489 RLNCLKVEELNGNLNDTLEKLSNAESQINAK------------TEDIEKMLKAFEAEKA--------LLLTQIEQQSVES 548
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISVDEGYEAAIeaalggrlqavvVENLNAAKKAIAFLKQnelgrvtfLPLDSIKGTEIQG 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 549 KSHSEAQNAQ-LQEIMDNLEQKDKEF--------------------NEVKLQLSSAESQISL------------------ 589
Cdd:TIGR02168 589 NDREILKNIEgFLGVAKDLVKFDPKLrkalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdlvrpggvitggsakt 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 590 -----------------------KALEIQNNLKAFEAEKSVLLTKIEQL---GIEHKNNSEAQNAQLQLTLNNLEQNESA 643
Cdd:TIGR02168 669 nssilerrreieeleekieeleeKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQLEER 748
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24663450 644 LQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRK 705
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-466 |
6.16e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 272 SQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLSNDLVLAREmcatfrmQNDDLEMQ 351
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE-------DFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 352 LNQNPILLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLletkeltneiSKIKVN 431
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL----------ARLEKE 207
|
170 180 190
....*....|....*....|....*....|....*
gi 24663450 432 VEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEK 466
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
269-478 |
6.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 269 EAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSyrhdVQELQQNNTVLSNDLVLAREMCATFRMQNDDL 348
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 349 EMQLNQNPILLQKAM--------EEEEKHKLSSEKFNKLKTL------YTKIRDEHIQLLREQSDCNKSLNKEKQVNSQL 414
Cdd:COG4942 96 RAELEAQKEELAELLralyrlgrQPPLALLLSPEDFLDAVRRlqylkyLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24663450 415 LLETK-ELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQKEIQE 478
Cdd:COG4942 176 LEALLaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
625-872 |
7.27e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 625 AQNAQLQLTLNNLEQNESALQQTQEIVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTssyqicsTDLSELR 704
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 705 KLVIKTvkeicnsklsgseQQPLDAVPNIIREMETILNKFNNASAINYVASTEGLQ----NVMYLGYVFIKLYDQCDVIY 780
Cdd:COG4942 90 KEIAEL-------------RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavrRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 781 KTTTAIETgqeifsKTNLLCTDICQLFQYLLNNETKEPERQKTITDIQTKLRDIEKLIEKIKASFEQKIDLDKLLEIELR 860
Cdd:COG4942 157 ADLAELAA------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|..
gi 24663450 861 EMDAAIDDAASK 872
Cdd:COG4942 231 RLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
503-722 |
7.59e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 503 NDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKshseAQNAQLQEIMDNLEQKDKEFNEVKLQLSS 582
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 583 AESQISLKALEIQNNLKA-------------FEAEKSVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNLEQNESALQQTQE 649
Cdd:COG4942 95 LRAELEAQKEELAELLRAlyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24663450 650 IVNQLRQENASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVIKTVKEICNSKLSGS 722
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
264-656 |
8.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 264 NNHELEAFSQAQQQLSMLEGIISEKEASIEELSFKLDAMQKNFDALQQSYRHDVQELQQNNTVLsndlvlaremcatfrm 343
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ---------------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 344 QNDDLEMQLNQNPILLQKAMEEEEKHKlssEKFNKLKTLYTKIRDEHIQLLREQSDCnkSLNKEKQVNS------QLLLE 417
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELR---ELEEELEELEAELAELQEELEELLEQL--SLATEEELQDlaeeleELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 418 TKELTNEISKIKVNVE--EKEKTNLILQKQIEEHKEKIAHLE-------------------------------------- 457
Cdd:COG4717 208 LAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 458 ----------AVKNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEkmL 527
Cdd:COG4717 288 llflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--L 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 528 KAFEAEKALLLTQIeqqsvesKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESqiSLKALEIQNNLKAFEAEKSV 607
Cdd:COG4717 366 EELEQEIAALLAEA-------GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEE 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24663450 608 LLTKIEQLGIEHKNNSEAQnAQLQLTLNNLEQNES---ALQQTQEIVNQLRQ 656
Cdd:COG4717 437 LEEELEELEEELEELREEL-AELEAELEQLEEDGElaeLLQELEELKAELRE 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
258-637 |
1.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 258 EDLVDTNNHELEAFSQAQQQLSMLEGIISEK----EASIEELSFK-LDAMQKNFDALQQSYRHDV------QELQQNNTV 326
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKhTQALEELTEQLEQAKRNKAnlekakQALESENAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 327 LSNDLVLAREMCATFRMQNDDLEMQLNQnpilLQKAMEEEEKHKlsSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNK 406
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQE----LQARLSESERQR--AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 407 EKQVNSQlLLETKELTNEiskikvnvEEKEKTNLilqkqieehKEKIAHLEAVKNEMKEKFDDVVKQKEIQELDIISTSE 486
Cdd:pfam01576 463 VSSLESQ-LQDTQELLQE--------ETRQKLNL---------STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 487 NLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKmlKAFEAEKALLLTQIEQQSVESKSHSEAQNAQLqeiMDNL 566
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE--KAAAYDKLEKTKNRLQQELDDLLVDLDHQRQL---VSNL 599
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24663450 567 EQKDKEFNevklQLSSAESQISLKALEIQNNLKAFEAEK---SVLLTKIEQLGIEHKNNSEAQNAQLQLTLNNL 637
Cdd:pfam01576 600 EKKQKKFD----QMLAEEKAISARYAEERDRAEAEAREKetrALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
302-665 |
1.25e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 302 MQKNFDALQQSYRHdVQELQQNNTVLSNDLV--LAREMCATFRMQNDDLEMQLNQNPILLQKAMEEEEK--HKL---SSE 374
Cdd:TIGR01612 2271 LHKSIESIKKLYKK-INAFKLLNISHINEKYfdISKEFDNIIQLQKHKLTENLNDLKEIDQYISDKKNIflHALnenTNF 2349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 375 KFNKLKTLYTKIrdehIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKia 454
Cdd:TIGR01612 2350 NFNALKEIYDDI----INRENKADEIENINNKENENIMQYIDTITKLTEKIQDILIFVTTYENDNNIIKQHIQDNDEN-- 2423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 455 HLEAVKNEMK---EKFDDVvkQKEIQELDIISTSENLRLNCLKVeeLNGNLNDTLEKLS------NAESQINAKTEDIEK 525
Cdd:TIGR01612 2424 DVSKIKDNLKktiQSFQEI--LNKIDEIKAQFYGGNNINNIIIT--ISQNANDVKNHFSkdltieNELIQIQKRLEDIKN 2499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 526 MLKAFEAEKALLLTQ-----IEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFN---EVKLQ-LSSAESQISLKALEIQN 596
Cdd:TIGR01612 2500 AAHEIRSEQITKYTNaihnhIEEQFKKIENNSNKDEVYKINEIDNIIEKIINYNkepEVKLHaIIDNKNEFASIIPDIKN 2579
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24663450 597 NLKAFEAEKSVLLTKIEQLGIEHKNNseAQNAQLQLtlnNLEQN--ESALQQTQEIVNQLRQENASAGQRN 665
Cdd:TIGR01612 2580 LIALIESEYGNNNNISYKVAIKHEED--ANNIILDL---NKSQNilNHLIHKNKKIIEDLGNIKHGIHNNN 2645
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-615 |
1.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 358 LLQKAMEEEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEIskikvnvEEKEK 437
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI-------EELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 438 TNLILQKQIEEHKEKIAHLEAVKNEMKEKFDDVVKQ-KEIQELDIISTsENLRLNCLKVEELNG--NLNDTLEKLSNAES 514
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvKELKELKEKAE-EYIKLSEFYEEYLDElrEIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 515 QINAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNA-QLQEIMDNLEQKDKEFN--EVKLQLSSAESqislKA 591
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkAKKEELERLKKRLTGLTpeKLEKELEELEK----AK 400
|
250 260
....*....|....*....|....
gi 24663450 592 LEIQNNLKAFEAEKSVLLTKIEQL 615
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKEL 424
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
365-618 |
1.43e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 365 EEEKHKLSSEKFNKLKTLYTKIRDEHIQLLREQSDCNKSLNKEKQVNSQLlletKELTNEISKIKvnvEEKEKTNLILQ- 443
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL----AELEKKLDELE---EELAELLKELEe 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 444 ---KQIEEHKEKIAHLEAVKNEMKEkFDDVVKQKEIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAESQINAKT 520
Cdd:PRK03918 582 lgfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 521 -EDIEKMLKAFEAEKALLLTQIEQqsveskshSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISlKALEIQNNLK 599
Cdd:PRK03918 661 yEELREEYLELSRELAGLRAELEE--------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVK 731
|
250 260
....*....|....*....|
gi 24663450 600 AFEAE-KSVLLTKIEQLGIE 618
Cdd:PRK03918 732 KYKALlKERALSKVGEIASE 751
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
501-689 |
1.46e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 501 NLNDTLEKLSNAESQiNAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHSEAQNAQL--QEIMDNLEQKDKEFNEVKL 578
Cdd:pfam12795 21 DLQQALSLLDKIDAS-KQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLslEELEQRLLQTSAQLQELQN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 579 QLSSAESQIslkaLEIQNNLKAFEAEKSVLLTKIEQLGiEHKNNSEAQNAQLQLTLNNLEQNESALQQTQeiVNQLRQEN 658
Cdd:pfam12795 100 QLAQLNSQL----IELQTRPERAQQQLSEARQRLQQIR-NRLNGPAPPGEPLSEAQRWALQAELAALKAQ--IDMLEQEL 172
|
170 180 190
....*....|....*....|....*....|.
gi 24663450 659 ASAGQRNEDLQSKLSLTEVKLTQATQQIDAV 689
Cdd:pfam12795 173 LSNNNRQDLLKARRDLLTLRIQRLEQQLQAL 203
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
258-614 |
2.26e-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: 42.34 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 258 EDLVDTNNHELEAFSQAQQQLSMLEGI---ISEKEASIEELSFKLDAMqkNFDALQQSYRHDVQELQQNNTVLSNDLVLA 334
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFqmeLKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 335 REMCATFRMQNDDLEMQLN-------QNPILLQKAMEEEEKhklSSEKFNKLKTLYTKIRDEhiqllREQSDCNKSLNKE 407
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNelkseklQIGTNLQRRQQFEEQ---LVELSTEVQSLIREIKDA-----KEQDSPLETFLEK 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 408 KQVNSQLLLETKELTNEISKIKVNVEEKEKtnlilqkqieehKEKIAHLEAVKNEMKEKFDDVVKQKEiqeldiistsen 487
Cdd:TIGR00606 921 DQQEKEELISSKETSNKKAQDKVNDIKEKV------------KNIHGYMKDIENKIQDGKDDYLKQKE------------ 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 488 lrlnclkvEELNGnLNDTLEKLSNAESQINaktEDIEKMLKAFEAEKallltqIEQQSVESKSHSEAQNAQLQEIMDNLE 567
Cdd:TIGR00606 977 --------TELNT-VNAQLEECEKHQEKIN---EDMRLMRQDIDTQK------IQERWLQDNLTLRKRENELKEVEEELK 1038
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24663450 568 QKDKEFNEVKLQLSSAESQislkalEIQNNLKAFEAEKSVLLTKIEQ 614
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQ------KLEENIDLIKRNHVLALGRQKG 1079
|
|
| seadorna_VP4 |
TIGR04235 |
seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with ... |
824-1073 |
2.31e-03 |
|
seadornavirus VP4 protein; This protein family occurs in the seadornavirus virus group, with designation VP4 in Banna virus, Kadipiro virus, and Liao ning virus. Although this family has been suggested to resemble methyltransferases, members show apparent N-terminal sequence similarity to the outer capsid protein VP5 of the orbivirus group, such as bluetongue virus, which also belong to the Reoviridae.
Pssm-ID: 211958 Cd Length: 618 Bit Score: 41.81 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 824 ITDIQTKLRDIEKLIEKIKA---SFEQKIDLDKLLEIELREMDAAIDDAASK----ITDLLAKAREKdnqtnlevngkiV 896
Cdd:TIGR04235 50 IKSTKQEMMDRQVLKEDYKAlalAVGQEIKFDNATQHQLNRLGSAIYKADHErekeLTDLLNAINEN------------E 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 897 DACTTLMECVKAL--IQKSRLLQhEIVasqkgnasanefyrrnsqwsdglISASKSVAKAANylVEAANKAIESESGKNf 974
Cdd:TIGR04235 118 IAVNDIIENQKAItaAEKADLIL-EIV-----------------------ISTARAVAATGR--AAADGVGVVPVFGPS- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 975 elIVAAQEIAACTTQMV--IASKVKAERNSQKLTDLTKASRSV-------------TQATGT-LVATVKDCNSQLEQQSE 1038
Cdd:TIGR04235 171 --VANGAKVGIDTAESVaeTAIAVKASGIITQLNDVFHAFQSVhvapndvikpavvVAGTSTdLIGKLKAIYDRLRRHND 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 24663450 1039 IELSKLT-PSQIKTMEMEiHVKVLEIEQALQMQRLK 1073
Cdd:TIGR04235 249 IGFSKATvPDTIPNSYMV-KPVVSDEYDSWQLYVIH 283
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
402-715 |
3.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 402 KSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFDdvvkqkEIQELDi 481
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE------EIEELE- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 482 istsenlrlncLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMlkafeAEKALLLTQIEQQSVESKshseaqnaQLQE 561
Cdd:PRK03918 245 -----------KELESLEGSKRKLEEKIRELEERIEELKKEIEEL-----EEKVKELKELKEKAEEYI--------KLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 562 IMDNLEqkdKEFNEVKLQLSSAESQISlkalEIQNNLKAFEAEKSvlltKIEQLGIEHKnnseaqnaQLQLTLNNLEQNE 641
Cdd:PRK03918 301 FYEEYL---DELREIEKRLSRLEEEIN----GIEERIKELEEKEE----RLEELKKKLK--------ELEKRLEELEERH 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24663450 642 SALQQTQEIVNQLRQENASAGQRN-EDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELRKLVI--KTVKEIC 715
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelKKAKGKC 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-593 |
3.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 381 TLYTKIRDEHIQLLREQSDcnkSLNKEKQVNSQLLLET-KELTNEISKIKVNVEEKEKtnliLQKQIEEHKEKIAHLEAV 459
Cdd:COG4717 38 TLLAFIRAMLLERLEKEAD---ELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 460 KNEMKEKFDDVVKQKEIQELDIISTSENLRLNCLKvEELNgNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLT 539
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24663450 540 QIEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALE 593
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
420-652 |
3.53e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 420 ELTNEISKIKVNVEEKEKTnlilqkqieehkekiahlEAVKNEMKEKFDDVVKQKEIQEldiistsenlrlnclKVEELN 499
Cdd:PLN03229 538 DMLNEFSRAKALSEKKSKA------------------EKLKAEINKKFKEVMDRPEIKE---------------KMEALK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 500 GNLndTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQ--IEQQSVESKSHSEAQNAQLQEIMDNLEQKDKEFN--- 574
Cdd:PLN03229 585 AEV--ASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSmgLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINkki 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 575 EVKLQLSSAESQISLKALEIQnnlKAFEAEKSVLLTKIEQLGIEHKNN-SEAQNA-QLQLTLNNLEQNESALQQTQEIVN 652
Cdd:PLN03229 663 ERVIRSSDLKSKIELLKLEVA---KASKTPDVTEKEKIEALEQQIKQKiAEALNSsELKEKFEELEAELAAARETAAESN 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
395-658 |
3.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 395 REQSDCNKSLNKEKQvnsqlllETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEavknEMKEKFDDVVKQK 474
Cdd:PRK02224 199 KEEKDLHERLNGLES-------ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 475 EIQELDIISTSENLRLNCLKVEELNGNLNDTLEKLSNAEsqinAKTEDIEKMLKAFEAEKALLLTQIEQQSVESKSHS-- 552
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDD----ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNee 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 553 -----------EAQNAQLQEIMDNLEqkdKEFNEVKLQLSSAESQISLKALEIQNNLKAFE-AEksvlltkiEQLGiehk 620
Cdd:PRK02224 344 aeslredaddlEERAEELREEAAELE---SELEEAREAVEDRREEIEELEEEIEELRERFGdAP--------VDLG---- 408
|
250 260 270
....*....|....*....|....*....|....*...
gi 24663450 621 nNSEAQNAQLQLTLNNLEQNESALQQTQEIVNQLRQEN 658
Cdd:PRK02224 409 -NAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
389-568 |
3.94e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 389 EHIQLLREQSDCNKSLNKEKQVNSQLLLETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEAVKNEMKEKFD 468
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 469 DVVKQKEIQ----ELDIIStsenlrlncLKVEELNGNLNDTLEKLSNAESQInaktEDIEKMLKAFEAEKALLLTQIEQQ 544
Cdd:COG1579 84 NVRNNKEYEalqkEIESLK---------RRISDLEDEILELMERIEELEEEL----AELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|....
gi 24663450 545 SVESKSHSEAQNAQLQEIMDNLEQ 568
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
417-746 |
4.02e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 417 ETKELTNEISKIKVNVEEKEKTNLILQK-------QIEEHKEKIAHLEAVKNEMKEKfdDVVKQKEIQELD--------- 480
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnkdeeKINNSNNKIKILEQQIKDLNDK--LKKNKDKINKLNsdlskinse 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 481 ------IISTSE----NLRLNCLKVEELNGNLNDTLEKLSNAESQINAKTEDIEKMLKAFEAEKALLLTQIEQ-QSVESK 549
Cdd:TIGR04523 112 ikndkeQKNKLEvelnKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 550 SHSeaQNAQLQEIMDNLEQKDKEFNEVKLQLSSAESQISLKALEIQNNLKAFEAEKSVLLTKIEQLgIEHKNNSEAQNAQ 629
Cdd:TIGR04523 192 IKN--KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL-NQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 630 LQLTLNNLEQNESALQQTQEIVNQLRQE-----NASAGQRNEDLQSKLSLTEVKLTQATQQIDAVTSSYQICSTDLSELR 704
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24663450 705 KlvIKTVKEICNSKLSGSEQQPLDAVPNIIREMETILNKFNN 746
Cdd:TIGR04523 349 K--ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
417-509 |
7.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24663450 417 ETKELTNEISKIKVNVEEKEKTNLILQKQIEEHKEKIAHLEA-VKNEMKEKFDDVVKQKEIQELDiistSENLRLNcLKV 495
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEReLSEARSEERREIRKDREISRLD----REIERLE-REL 481
|
90
....*....|....
gi 24663450 496 EELNGNLNDTLEKL 509
Cdd:COG2433 482 EEERERIEELKRKL 495
|
|
| |
