|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
242-595 |
1.40e-90 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 283.90 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 242 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 312
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 313 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 392
Cdd:pfam09738 93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 472
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 473 IILNSEIATNGEtsdTLNNVGYQGPTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 550
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622852868 551 DNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 595
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-645 |
1.31e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 264 ATLASLGGTSSRRGSGDTSISIDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 339
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 340 DNEktnfmyqVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIR--------- 410
Cdd:TIGR02168 711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeae 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 411 --QLQQKQASSIREISDLQETIewkDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDT 488
Cdd:TIGR02168 784 ieELEAQIEQLKEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATERRLED----LEEQIEELSEDIES 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 489 LNnvgyqgptkmtkAELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEddvlengtdmhv 568
Cdd:TIGR02168 857 LA------------AEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSE--ELRELESK------------ 909
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852868 569 mdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 645
Cdd:TIGR02168 910 ---RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
391-669 |
2.38e-10 |
|
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: 63.93 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 391 QFAEVKEALK-EREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLK 465
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 466 EELKKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKAELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ 545
Cdd:TIGR02169 758 SELKE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 546 KigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 625
Cdd:TIGR02169 819 Q--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622852868 626 AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 669
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-669 |
1.13e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 295 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEE 373
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 374 KNKEFErEKHAhsilqfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSE 453
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 454 RDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGPTKM--TKAELNALKSTGDgtldiRLKKLVDERECLL 531
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLE-----QKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 532 EQIKKLKGQLEERQK---------IGKLDNLRSEDDVLENGTDmhvmDLQRDANRQISDLKFKLAksEQEITALEQNVIR 602
Cdd:TIGR04523 499 KKLNEEKKELEEKVKdltkkisslKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKENL--EKEIDEKNKEIEE 572
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852868 603 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 669
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSI 632
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-669 |
1.37e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefFDSVRSERDDLREEVVMLKEELKKhg 472
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 473 iiLNSEIATNGETSDTLnnvgyQGPTKMTKAELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 546
Cdd:TIGR02168 773 --AEEELAEAEAEIEEL-----EAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 547 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 626
Cdd:TIGR02168 846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622852868 627 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 669
Cdd:TIGR02168 909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
316-646 |
3.06e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 316 KEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEV 395
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 396 KEALKEREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGI 473
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 474 ILNSEIATNGETSDTLNN-VGYQGPTKMTKAELNA---LKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigK 549
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA--Q 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 550 LDNLRSEDDVLENGTDmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE----- 621
Cdd:TIGR02169 898 LRELERKIEELEAQIE--------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeira 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622852868 622 -------------------DELKAEKRKLQRELRSALDKTEELE 646
Cdd:TIGR02169 970 lepvnmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-667 |
5.76e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALERQK----------------EFFDS 449
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealndlearlshSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 450 VRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNN-VGYQGPTKMTKAELNAlkstgdgtldiRLKKLVDERE 528
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEK-----------EIENLNGKKE 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 529 CLLEQIKKLkgQLEERQKIGKLDNLRSEDDVLENgtDMHVM-DLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 607
Cdd:TIGR02169 865 ELEEELEEL--EAALRDLESRLGDLKKERDELEA--QLRELeRKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852868 608 SRYKSAAENAEKIEDeLKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 667
Cdd:TIGR02169 941 GEDEEIPEEELSLED-VQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-663 |
8.79e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 291 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTNFM-YQVDTLKDMLLELEEQLAE 366
Cdd:PRK03918 327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 367 SRRQYEE--------KNKEFEREK----------------------HAHSILQFQFAEVKEALKEREEMLEEIRQL---- 412
Cdd:PRK03918 403 IEEEISKitarigelKKEIKELKKaieelkkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLrkel 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 413 --------QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKEELKKhGIILNSEIATN 482
Cdd:PRK03918 483 relekvlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 483 GETSDTLnnvgyqgptKMTKAELNA-LKSTGDGTLD----------------IRLKKLVDERECLLEQIKKLKGQLEErq 545
Cdd:PRK03918 562 EKKLDEL---------EEELAELLKeLEELGFESVEeleerlkelepfyneyLELKDAEKELEREEKELKKLEEELDK-- 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 546 kigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 625
Cdd:PRK03918 631 ---AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622852868 626 AEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 663
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
286-670 |
1.43e-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: 58.11 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 286 DTEASIREIK-ELNELKDQIQDVEG--------------------KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKT 344
Cdd:TIGR04523 163 DLKKQKEELEnELNLLEKEKLNIQKnidkiknkllklelllsnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 345 NFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEAL------KEREEMLEEIRQLQQKQas 418
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnqKEQDWNKELKSELKNQE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 419 siREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyqgpt 498
Cdd:TIGR04523 321 --KKLEEIQNQISQNNKIISQLNEQIS---QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 499 kmtKAELNALKSTGDGT------LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMH----- 567
Cdd:TIGR04523 390 ---ESQINDLESKIQNQeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNS--EIKDLTNQDSVKELIIKNLdntre 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 568 -----VMDLQRDANRQISDLKFK---LAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSAL 639
Cdd:TIGR04523 465 sletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622852868 640 D---------KTEELEVSNGHLVKRLEKMKANRSALLSQQ 670
Cdd:TIGR04523 545 DelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
393-646 |
1.73e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 472
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 473 IILNS---EIATNGETSDTLNNVGyqGPTKMTKAELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI-- 547
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAG--GSIDKLRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAle 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 548 --GKLDNLRSEDDVLengtdmhvMDLQRDANRQISDL-------KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 618
Cdd:COG1340 158 knEKLKELRAELKEL--------RKEAEEIHKKIKELaeeaqelHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260
....*....|....*....|....*...
gi 1622852868 619 KIEDELKAEKRKLQRELRSALDKTEELE 646
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
368-645 |
3.41e-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: 56.99 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 443
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 444 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgptkmTKAELNALKSTGDgTLDIR 519
Cdd:TIGR02168 318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----------------LEAELEELESRLE-ELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 520 LKKLVDERECLLEQIKKLKGQLEE-RQKI----GKLDNLRSEddVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEIT 594
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERlEARLerleDRRERLQQE--IEELLKKLEEAELK-ELQAELEELEEELEELQEELE 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622852868 595 ALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 645
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-626 |
3.71e-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: 57.00 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 286 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 364
Cdd:TIGR02169 234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 365 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 444
Cdd:TIGR02169 304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 445 efFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQgptkmTKAELNALKStgdgtldiRLKKLV 524
Cdd:TIGR02169 380 --FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELAD-----LNAAIAGIEA--------KINELE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 525 DERECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLE 604
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340
....*....|....*....|..
gi 1622852868 605 SQVSRYKSAAENAEKIEDELKA 626
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
393-619 |
3.33e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 472
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 473 IILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 550
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852868 551 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 619
Cdd:COG4942 191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-661 |
5.19e-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: 53.14 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 370 QYEEKNKEFEREKHAHSILQFQFAEvkealKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 444
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 445 EFFdSVRSERDDLREEVVMLKEELKKhgiiLNSEIatngetsdtlnnvgyqgptKMTKAELNALKSTGDgtldiRLKKLV 524
Cdd:TIGR02168 289 ELY-ALANEISRLEQQKQILRERLAN----LERQL-------------------EELEAQLEELESKLD-----ELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 525 DERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 604
Cdd:TIGR02168 340 AELEEKLEELKEELESLEA-----ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852868 605 SQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 661
Cdd:TIGR02168 407 ARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
391-670 |
1.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 391 QFAEVKEALKERE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 464
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 465 KEELKKHGIILNSEIATNGETSDTLNNvgyqgptkmTKAELNALKSTGDG------TLDIRLKKLVDERECLLEQIKKLK 538
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEE---------LEEELAELEEELEEleeeleELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 539 GQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 618
Cdd:COG1196 365 EALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622852868 619 KIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 670
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-633 |
1.20e-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: 51.99 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 397 EALKEREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 469
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 470 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKAELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 549
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 550 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 629
Cdd:TIGR02169 440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490
|
....
gi 1622852868 630 KLQR 633
Cdd:TIGR02169 491 ELAE 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-666 |
1.44e-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: 51.61 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 377 EFEREKHAhsiLQFQFAEVKEALKEREEMLEEIRQLQQK------QASSIREISDLQETIEWKD--KKIGALERQKEffd 448
Cdd:TIGR02169 167 EFDRKKEK---ALEELEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEGYEllKEKEALERQKE--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 449 SVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLN------NVGYQGPTKMTKAELNALKSTGDGT------- 515
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISE----LEKRLEEIEQLLEELNkkikdlGEEEQLRVKEKIGELEAEIASLERSiaekere 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 516 ---LDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISD 581
Cdd:TIGR02169 317 ledAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAeleevdKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 582 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 661
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
....*
gi 1622852868 662 NRSAL 666
Cdd:TIGR02169 477 EYDRV 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
383-638 |
2.07e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 383 HAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 462
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 463 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkaeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 540
Cdd:COG3883 83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 541 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 620
Cdd:COG3883 145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250
....*....|....*...
gi 1622852868 621 EDELKAEKRKLQRELRSA 638
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
293-666 |
2.84e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 293 EIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFmyqVDTLKDMLLELEEQLAESRRQYE 372
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL---KELEKRLEELEERHELYEEAKAK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 373 EKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEW----------------KDKK 436
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 437 IGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILN--SEIATNGETSDTLNNV-----GYQGPT--------KMT 501
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELeeklkKYNLEElekkaeeyEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 502 KAELNALKSTGDGTLD--IRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVlengtDMHVMDLQ------- 572
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL-----EERLKELEpfyneyl 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 573 --RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEEL 645
Cdd:PRK03918 606 elKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEEL 685
|
410 420
....*....|....*....|.
gi 1622852868 646 EVSNGHLVKRLEKMKANRSAL 666
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEER 706
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
413-666 |
3.44e-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: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 413 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 492
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 493 gyqgptkmTKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 568
Cdd:COG4942 74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 569 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 648
Cdd:COG4942 132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
250
....*....|....*...
gi 1622852868 649 NGHLVKRLEKMKANRSAL 666
Cdd:COG4942 208 LAELAAELAELQQEAEEL 225
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
372-562 |
3.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 451
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 452 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKAELNALKSTGDGTLDIRLKKLVDERECLL 531
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1622852868 532 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 562
Cdd:COG4717 206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-636 |
1.17e-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: 48.63 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 290 SIREIKELNELKDQIQDVEgkymqglkemkdSLAEVEEKYKKAMVSNA-QLDNEKTNFMYQVDtlkdmlleleeqlaesr 368
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQ------------ELLQEETRQKLNLSTRLrQLEDERNSLQEQLE----------------- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 369 rQYEEKNKEFEREKhahSILQFQFAEVKealKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQK---- 444
Cdd:pfam01576 507 -EEEEAKRNVERQL---STLQAQLSDMK---KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKnrlq 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 445 EFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMTKAElnalkstgdgTLDIRLKKLV 524
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL----------SLARALEEAL 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 525 DERECLLEQIKKLKGQLEerqkigklDNLRSEDDVlenGTDMHVMD-LQRDANRQISDLKFKLAKSEQEITALEQNVIRL 603
Cdd:pfam01576 650 EAKEELERTNKQLRAEME--------DLVSSKDDV---GKNVHELErSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
330 340 350
....*....|....*....|....*....|....
gi 1622852868 604 ESQVSRYKSAAENAEKIEDELKAEKRK-LQRELR 636
Cdd:pfam01576 719 EVNMQALKAQFERDLQARDEQGEEKRRqLVKQVR 752
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
289-669 |
1.19e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 289 ASIREIKELneLKDQIQDVEGKYM---QGLKEMKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TN 345
Cdd:pfam15921 468 AQLESTKEM--LRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 346 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISD 425
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 426 LQETIEWKDKKI--GALERQKEFFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKA 503
Cdd:pfam15921 626 RVSDLELEKVKLvnAGSERLRAVKD-IKQERDQLLNEV-------------------------------------KTSRN 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 504 ELNALKSTgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlk 583
Cdd:pfam15921 668 ELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI---- 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 584 fklakseqeiTALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKM 659
Cdd:pfam15921 737 ----------TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEK 805
|
410
....*....|
gi 1622852868 660 KANRSALLSQ 669
Cdd:pfam15921 806 VANMEVALDK 815
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
372-489 |
1.61e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 451
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622852868 452 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 489
Cdd:COG2433 458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
391-661 |
1.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 391 QFAEVKEA------LKEREEMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVML 464
Cdd:COG4913 233 HFDDLERAhealedAREQIELLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 465 KEELKKHgiilnseiatngetsdtlnnvgyqgptkmtKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEER 544
Cdd:COG4913 308 EAELERL------------------------------EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 545 QKigKLDNLrseddvlengtdmhvmdlqrdaNRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDEL 624
Cdd:COG4913 358 ER--RRARL----------------------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622852868 625 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 661
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
368-646 |
1.70e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 368 RRQYEEKNKEFER-------EKHAHSILQFQ---FAEVKEALKEREEMLEEIRQLQQKqassiREISDL-QETIEWKDKK 436
Cdd:pfam17380 302 RQEKEEKAREVERrrkleeaEKARQAEMDRQaaiYAEQERMAMERERELERIRQEERK-----RELERIrQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 437 IGALERqkeffdsVRSERDDLREEVVMLKEELKKHGIILNSEiatngetsdtlnnvgyQGPTKMTKAELNALKSTGDGTL 516
Cdd:pfam17380 377 MRELER-------LQMERQQKNERVRQELEAARKVKILEEER----------------QRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 517 DIRLKKLVDERECLLE-----------QIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQI---SDL 582
Cdd:pfam17380 434 QREVRRLEEERAREMErvrleeqerqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieEER 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852868 583 KFKLAKSEQEitaLEQNVIRLESQvsRYKSAAENAEKIEDElkaEKRKLQRELRSALDKTEELE 646
Cdd:pfam17380 514 KRKLLEKEME---ERQKAIYEEER--RREAEEERRKQQEME---ERRRIQEQMRKATEERSRLE 569
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
297-660 |
2.16e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 297 LNELKDQIQDVEGKY---MQGLKEMKDSLAEVEEKYKKAM-VSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYE 372
Cdd:pfam15921 262 LQQHQDRIEQLISEHeveITGLTEKASSARSQANSIQSQLeIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 373 EKNKEFEREkhahsiLQFQFAEVKEALKEREEMLEEIRQLQQKQAssiREISDLQetiewKDKKIGALERQKE------- 445
Cdd:pfam15921 342 DKIEELEKQ------LVLANSELTEARTERDQFSQESGNLDDQLQ---KLLADLH-----KREKELSLEKEQNkrlwdrd 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 446 -----FFDSVRSERDDLREEVVMLKEELKKhgiiLNSEiaTNGETSDTLNNVGYQGPTKMTKAELNA-LKSTGDgtldiR 519
Cdd:pfam15921 408 tgnsiTIDHLRRELDDRNMEVQRLEALLKA----MKSE--CQGQMERQMAAIQGKNESLEKVSSLTAqLESTKE-----M 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 520 LKKLVDE---RECLLEQ----IKKLKGQLEERQKIGKLDNlrSEDDVLENGTDMHVMDLQ---------RDANRQISDLK 583
Cdd:pfam15921 477 LRKVVEEltaKKMTLESsertVSDLTASLQEKERAIEATN--AEITKLRSRVDLKLQELQhlknegdhlRNVQTECEALK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 584 FKLAKSEQEITALEQ---NVIRLESQVSRyKSAAENAEKIEDELKAEKRKLQ-RELRSALDKTE----ELEVSNGHLvkR 655
Cdd:pfam15921 555 LQMAEKDKVIEILRQqieNMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQEFKILKDKKDakirELEARVSDL--E 631
|
....*
gi 1622852868 656 LEKMK 660
Cdd:pfam15921 632 LEKVK 636
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
515-644 |
3.88e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 515 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 581
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622852868 582 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 644
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
368-664 |
3.89e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 368 RRQYEEKNKEFEREKHAHSilQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 447
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQ--ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 448 DSVRSERDDLREEVVMLKEELKKHGIILNSEIatngETSDTLNNVgyqgptkmtKAELNALKSTGDGTLDIRLKKLVDER 527
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEK----EEIEELEKE---------LKELEIKREAEEEEEEELEKLQEKLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 528 ECLLEQIKKLKGQLEERQKIGKLDNlrseddvlENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 607
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKE--------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852868 608 SRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 664
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
288-661 |
4.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 288 EASIREIKELN-ELKDQIQDVEG--KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleeQL 364
Cdd:PRK03918 203 EEVLREINEISsELPELREELEKleKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK--------KE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 365 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQK 444
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 445 EFFDsvrsERDDLREEVVMLKEELKKhgiiLNSEIAtnGETSDTLnnvgyqgptkmtKAELNALKStgdgtldiRLKKLV 524
Cdd:PRK03918 355 EELE----ERHELYEEAKAKKEELER----LKKRLT--GLTPEKL------------EKELEELEK--------AKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 525 DERECLLEQIKKLKGQLEERQK-IGKLDNLRSEDDVLENG-TDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIR 602
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKaIEELKKAKGKCPVCGRElTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852868 603 LE------SQVSRYKSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 661
Cdd:PRK03918 485 LEkvlkkeSELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
292-644 |
5.11e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 292 REIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--RR 369
Cdd:PRK03918 228 KEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSefYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 370 QYEEKNKEFEREKhahSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEW---------------KD 434
Cdd:PRK03918 304 EYLDELREIEKRL---SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 435 KKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGP------TKMTKAELNAL 508
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 509 KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 588
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852868 589 SEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 644
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
376-660 |
5.24e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 376 KEFEREKHAHSILQFQFAEVKEALKEREEMLEEIrqlqqkqassIREISDLQETIEWKDKKIGALERQKEFFDSVRSERD 455
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEV----------LREINEISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 456 DLREEVVMLKEELKKHGIILnseiatnGETSDTLNNVgyqgptkmtKAELNALKST--------GDGTLDIRLKKLVDER 527
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKI-------RELEERIEEL---------KKEIEELEEKvkelkelkEKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 528 ECLLEQIKKLKGQLEER-----QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKLAKSEQEITALEQNVIR 602
Cdd:PRK03918 306 LDELREIEKRLSRLEEEingieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852868 603 LESqvsryKSAAENAEKIEDELK-AEKRK--LQRELRSALDKTEELEVSNGHLVKRLEKMK 660
Cdd:PRK03918 377 LKK-----RLTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
293-627 |
7.62e-05 |
|
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: 46.12 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 293 EIKELNELKD------QIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMvsnAQLDNEKTNFMYQVDTLKDMLLELEEQLAE 366
Cdd:TIGR00618 599 LTEKLSEAEDmlaceqHALLRKLQPEQDLQDVRLHLQQCSQELALKL---TALHALQLTLTQERVREHALSIRVLPKELL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 367 SRRQYEEKnkEFEREKHAHSILQFQFAEVKEALKEREEMLEEI-RQLQQKQASSIREISDLQETIEWKDKKIGALERQ-- 443
Cdd:TIGR00618 676 ASRQLALQ--KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASSSLGSDLAAREDALNQSLKELMHQar 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 444 -----KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNgetsdtlnnvgyQGPTKMTKAELNALKSTGDGTLDI 518
Cdd:TIGR00618 754 tvlkaRTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREED------------THLLKTLEAEIGQEIPSDEDILNL 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 519 RLKKLVDERECLLEQIKKL-KGQLEERQKIGKL-DNLRSEDDVLENGTDMHVMDLQRDANRQISDLK--FKLAKSEQEIT 594
Cdd:TIGR00618 822 QCETLVQEEEQFLSRLEEKsATLGEITHQLLKYeECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFdgDALIKFLHEIT 901
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622852868 595 AleQNVIRLESQ-----VSRY--KSAAENAEKIEDELKAE 627
Cdd:TIGR00618 902 L--YANVRLANQsegrfHGRYadSHVNARKYQGLALLVAD 939
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
368-667 |
8.91e-05 |
|
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: 45.81 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 447
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 448 DSVRSERDDLREEVVMLKEELKKhgiilnseiATNGETSDTLNNvgyQGPTKMTKAELNALKSTGDGTLDIRLKKLVDER 527
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVFQ---------GTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 528 ECLLEQIKKLKGQLEERQ-KIGKLDNLRseddvLENGTDMHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRL 603
Cdd:TIGR00606 343 TELLVEQGRLQLQADRHQeHIRARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852868 604 ESQVsryKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 667
Cdd:TIGR00606 418 QSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-666 |
1.06e-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: 45.82 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 501 TKAELNALKSTgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQIS 580
Cdd:TIGR02168 696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 581 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 660
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
....*.
gi 1622852868 661 ANRSAL 666
Cdd:TIGR02168 852 EDIESL 857
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-670 |
1.56e-04 |
|
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: 45.01 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 283 ISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKamvsNAQLDNEKTNFMYQVDTLKDmllelee 362
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK----YNDLKKQKEELENELNLLEK------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 363 qlaesrrQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQassireiSDLQETIEWKDKKIGALER 442
Cdd:TIGR04523 181 -------EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-------NQLKDNIEKKQQEINEKTT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 443 QkefFDSVRSERDDLREEVVMLKEELKKHgiilNSEIATNGETSDTLNNvgyqgptkmtkaELNALKStgdgtldiRLKK 522
Cdd:TIGR04523 247 E---ISNTQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEK------------QLNQLKS--------EISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 523 LVDEREclLEQIKKLKGQLEERQKigKLDNLRSEDDvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIR 602
Cdd:TIGR04523 300 LNNQKE--QDWNKELKSELKNQEK--KLEEIQNQIS---------------QNNKIISQLNEQISQLKKELTNSESENSE 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852868 603 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 670
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
266-459 |
1.70e-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: 45.05 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 266 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 345
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 346 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 424
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622852868 425 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 459
Cdd:TIGR02168 972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-670 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 519 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 587
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 588 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 667
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 1622852868 668 SQQ 670
Cdd:TIGR02168 393 LQI 395
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-470 |
3.41e-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: 43.89 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 288 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 367
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 447
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190
....*....|....*....|....*....|..
gi 1622852868 448 DS---------VRSERDDLREEVVMLKEELKK 470
Cdd:TIGR02168 420 QQeieellkklEEAELKELQAELEELEEELEE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
519-670 |
3.82e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 519 RLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKFKLAKSEQEITALEQ 598
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEE--ELEQARSELEQLEE--------ELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852868 599 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 670
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
370-661 |
4.08e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 370 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefFDS 449
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ---LTA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 450 VRSERDDLREEVVMLKEELKKHGIiLNSEIATNGETSDTLNNVGYQGPTKMTkAELNALKStgdgtlDIRLKKLVDER-- 527
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKL-KNIELTAHCDKLLLENKELTQEASDMT-LELKKHQE------DIINCKKQEERml 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 528 ---ECLLEQIKKLKGQLEERQK--IGKLDNLRSE-DDVLENGTDMHVMDLQRDANRQI-----SDLKFKLAKSEQEITAL 596
Cdd:pfam05483 534 kqiENLEEKEMNLRDELESVREefIQKGDEVKCKlDKSEENARSIEYEVLKKEKQMKIlenkcNNLKKQIENKNKNIEEL 613
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852868 597 EQnvirlESQVSRYKSAAENAE---------KIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 661
Cdd:pfam05483 614 HQ-----ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-550 |
4.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 295 KELNELKDQIQDVEgKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQvdtlkdmlleleeqlaesrrQYEEK 374
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE--------------------SVEEL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 375 NKEFEREKHAHSilqfQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ--KEFFDSVRS 452
Cdd:PRK03918 591 EERLKELEPFYN----EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELRE 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 453 ERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLnnvgyqgptkmtKAELNALKSTGDGTLDirLKKLVDERECLLE 532
Cdd:PRK03918 667 EYLELSRELAGLRAELEE----LEKRREEIKKTLEKL------------KEELEEREKAKKELEK--LEKALERVEELRE 728
|
250 260
....*....|....*....|
gi 1622852868 533 QIKKLKGQLEER--QKIGKL 550
Cdd:PRK03918 729 KVKKYKALLKERalSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-640 |
4.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 286 DTEASIRE-IKELNELKDQIQDvegkymqgLKEMKDSLAEVEEkykkAMVSNAQLDN-EKTNFMYQVDTLKDMLLELEEQ 363
Cdd:PRK02224 262 DLRETIAEtEREREELAEEVRD--------LRERLEELEEERD----DLLAEAGLDDaDAEAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 364 LAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIG----A 439
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGdapvD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 440 LERQKEFFDSVRSERDDLREEVVMLKEELKkhgiilnsEIATNGETSDTLNNVG--------------------YQGPTK 499
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLR--------TARERVEEAEALLEAGkcpecgqpvegsphvetieeDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 500 MTKAELNALKSTGDgTLDIR------LKKLVDERECLLEQIKKLKGQLEER-----QKIGKLDNLRSEDDVLENGTDMH- 567
Cdd:PRK02224 479 ELEAELEDLEEEVE-EVEERleraedLVEAEDRIERLEERREDLEELIAERretieEKRERAEELRERAAELEAEAEEKr 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 568 -----VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRL------ESQVSRYKSAAENAEKIEDELK---AEKRKLQR 633
Cdd:PRK02224 558 eaaaeAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRerlAEKRERKR 637
|
....*..
gi 1622852868 634 ELRSALD 640
Cdd:PRK02224 638 ELEAEFD 644
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
398-665 |
5.06e-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: 42.83 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 398 ALKEREEMLEEIRQLQQKQASSIREISDLQETIEwkdkkigalerqkeffdSVRSERDDLREEVVMLKEELKKhgiilns 477
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEK-----------------ALLKQLAALERRIAALARRIRA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 478 eiatngetsdtlnnvgyqgptkmTKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNL 553
Cdd:COG4942 74 -----------------------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 554 R---SEDDVLENGTDMHVMD-LQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKR 629
Cdd:COG4942 123 AlllSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622852868 630 KLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSA 665
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
386-646 |
5.37e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 386 SILQFQFAEVKEALKEREEMLEE----IRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEv 461
Cdd:pfam10174 341 AILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAG- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 462 vmLKEELKkhgiilnsEIATNGETSDTlnnvgyqgptkmtkaelnALKStgdgtldirLKKLVDERECLLEQIKKLKgQL 541
Cdd:pfam10174 420 --LKERVK--------SLQTDSSNTDT------------------ALTT---------LEEALSEKERIIERLKEQR-ER 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 542 EERQKIGKLDNLRSEDDVLENGTDM----------HVMDLQRDANRQISDLKFKLAKSEQEITALEQNV---IRLESQVS 608
Cdd:pfam10174 462 EDRERLEELESLKKENKDLKEKVSAlqpeltekesSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecSKLENQLK 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622852868 609 RYKSAAENA---EKIEDEL----------KAEKRKLQRELRSALDKTEELE 646
Cdd:pfam10174 542 KAHNAEEAVrtnPEINDRIrlleqevaryKEESGKAQAEVERLLGILREVE 592
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
315-658 |
6.25e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 315 LKEMKDSLAEVEEKYK-----------KAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKH 383
Cdd:pfam05483 263 LEESRDKANQLEEKTKlqdenlkelieKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 384 AHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREI--------SDLQETIEWKDKKIGALERQKEFFDSVRSERD 455
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIItmelqkksSELEEMTKFKNNKEVELEELKKILAEDEKLLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 456 DlREEVVMLKEELKKhgiilnseiatngetsdtlnnvgyqgptkmTKAELNALKSTGDGT---LDIRLKKLVDERECLLE 532
Cdd:pfam05483 423 E-KKQFEKIAEELKG------------------------------KEQELIFLLQAREKEihdLEIQLTAIKTSEEHYLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 533 QIKKLKGQLEERqkigKLDNLRseddvLENGTDMHVMDlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVsryKS 612
Cdd:pfam05483 472 EVEDLKTELEKE----KLKNIE-----LTAHCDKLLLE-NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI---EN 538
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622852868 613 AAENAEKIEDELKAEKRKLQR---ELRSALDKTEELEVSNGHLVKRLEK 658
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
292-664 |
8.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 292 REIKELNELKDQIQDVEGKYMQgLKEMKDSLaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQlaesRRQY 371
Cdd:COG4717 92 ELQEELEELEEELEELEAELEE-LREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHAHSILQFQFAEVKEalKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKeffdsvr 451
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 452 sERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQ---------GPTKMTKAELNALKSTGDGTLDIRLKK 522
Cdd:COG4717 237 -EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllalLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 523 LVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDM-HVMDLQRDANRQISDLKFKLAKSE----------Q 591
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeEELQLEELEQEIAALLAEAGVEDEeelraaleqaE 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622852868 592 EITALEQNVIRLESQVSRYKSAAENAEKI--EDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 664
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-490 |
1.46e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 291 IREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRR 369
Cdd:TIGR02169 793 IPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 370 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIRE----ISDLQETIEWKDKKIGALERQKE 445
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKG 941
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622852868 446 FFDSVRSER---DDLREEVVMLKEELKKHGIILNSEIATNGETSDTLN 490
Cdd:TIGR02169 942 EDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
401-658 |
1.68e-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: 41.54 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 401 EREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ-KEFFDSVRSERDDLREEVVMLkEELKKHGIILNSEI 479
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKiKILEQQIKDLNDKLKKNKDKI-NKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 480 ATNGETSDTLnnvgyqgptkmtKAELNALKstgdgtldiRLKKLVDERECL-LEQIKKLKGQLEERQKigKLDNLRSEDD 558
Cdd:TIGR04523 113 KNDKEQKNKL------------EVELNKLE---------KQKKENKKNIDKfLTEIKKKEKELEKLNN--KYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 559 VLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITALE---QNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQREL 635
Cdd:TIGR04523 170 ELENELNLLEKEKL-NIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260
....*....|....*....|...
gi 1622852868 636 RSALDKTEELEVSNGHLVKRLEK 658
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSE 271
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
293-660 |
1.72e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 293 EIKELNELKDQIQDVEGKyMQGLKEMKDSLAEVEEKYKKAM-VSNAQLDNEKTNFMYQVDTLKDmLLELEEQLAESRRQY 371
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEeKKKADEAKKKAEEAKKADEAKK-KAEEAKKAEEAKKKA 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHAHSILQFQfaEVKEALKEREEMLEEIRQLQQ--KQASSIREISDLQETIEWKDkkigALERQKEffDS 449
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKK----AEEAKKA--DE 1538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 450 VRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLnnvgyqgptKMTKAELnaLKSTGDGTLDIRLKKLVDEREC 529
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM---------ALRKAEE--AKKAEEARIEEVMKLYEEEKKM 1607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 530 LLEQIKKlkgqlEERQKIgKLDNLRSEDDVlengtdmhvmdlqrdaNRQISDLKFKLA----KSEQEITALEQNVIRLES 605
Cdd:PTZ00121 1608 KAEEAKK-----AEEAKI-KAEELKKAEEE----------------KKKVEQLKKKEAeekkKAEELKKAEEENKIKAAE 1665
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852868 606 QVSRY---KSAAENAEKIEDELKAEKRKLQRELRSAlDKTEELEVSNGHLVKRLEKMK 660
Cdd:PTZ00121 1666 EAKKAeedKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELK 1722
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
611-670 |
1.82e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 611 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 670
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
288-467 |
2.12e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 288 EASIREIKE-LNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleEQLAE 366
Cdd:TIGR02169 832 EKEIQELQEqRIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 367 SRRQYEEKNKEFEREKHAHSILQfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALE----R 442
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmL 976
|
170 180
....*....|....*....|....*
gi 1622852868 443 QKEFFDSVRSERDDLREEVVMLKEE 467
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
292-636 |
2.77e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 292 REIKELNELKDQIQDVEGKYMQGLKEMKDSlAEVEEKYKKAMVSNAQLDNEKTNfmyQVDTLKDMLLELEEQLAESRRQY 371
Cdd:pfam05557 45 RESDRNQELQKRIRLLEKREAEAEEALREQ-AELNRLKKKYLEALNKKLNEKES---QLADAREVISCLKNELSELRRQI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHahsilqfQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 451
Cdd:pfam05557 121 QRAELELQSTNS-------ELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 452 SERD---DLREEVVMLKEELKKhgiiLNSEIATNGetsdtlnnvgyqgptkMTKAELNALKSTGDgtldiRLKKLVDERE 528
Cdd:pfam05557 194 SELAripELEKELERLREHNKH----LNENIENKL----------------LLKEEVEDLKRKLE-----REEKYREEAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 529 CLLEQIKKLKGQLEERQKIGKLD--NLRSEDDVLENgtdmHVMDLQRDANrqisdLKFKLAKSEQEITALEQNVIRLESQ 606
Cdd:pfam05557 249 TLELEKEKLEQELQSWVKLAQDTglNLRSPEDLSRR----IEQLQQREIV-----LKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350
....*....|....*....|....*....|
gi 1622852868 607 VSRYKSAAENAEKIEDELKAEKRKLQRELR 636
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVL 349
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
391-470 |
2.80e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.44 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 391 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 468
Cdd:PRK05431 10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89
|
..
gi 1622852868 469 KK 470
Cdd:PRK05431 90 DE 91
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
335-669 |
2.90e-03 |
|
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: 40.98 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 335 SNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHS---ILQFQFAEVKEALKEREEmleeiRQ 411
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKnarLDLRRLFDEKQSEKDKKN-----KA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 412 LQQKQASSIREISDLQETIEWKDKKIGA-LERQKEFFDSVRSERDDLREEVVmlkEELKKHGIILNSEIATNGETSdtln 490
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVE---GALDAQLALLKAAIAARRSGA---- 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 491 nvgyqgptkmtKAELNALKSTGDGTLDirlKKLVDErecllEQIKKLKGQLEE-RQKIGKLDNLRSEddVLENGTDMHVM 569
Cdd:pfam12128 746 -----------KAELKALETWYKRDLA---SLGVDP-----DVIAKLKREIRTlERKIERIAVRRQE--VLRYFDWYQET 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 570 DLQRDANRQIsdlkfKLAKSEQEITALEQNVIRLESQVSRYKSAAEN----AEKIEDELKAEKRKLQRELRS----ALDK 641
Cdd:pfam12128 805 WLQRRPRLAT-----QLSNIERAISELQQQLARLIADTKLRRAKLEMerkaSEKQQVRLSENLRGLRCEMSKlatlKEDA 879
|
330 340
....*....|....*....|....*....
gi 1622852868 642 T-EELEVSNGHLVKRLEKMKANRSALLSQ 669
Cdd:pfam12128 880 NsEQAQGSIGERLAQLEDLKLKRDYLSES 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
387-596 |
3.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 387 ILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQEtiewkdKKIGALERQKEFF------DSVRSERDDLREE 460
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ------ERREALQRLAEYSwdeidvASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 461 VVMLKEElkkhgiilNSEIATNGETSDTLnnvgyqgptkmtKAELNALKSTGDGtLDIRLKKLVDERECLLEQIKKLKGQ 540
Cdd:COG4913 677 LERLDAS--------SDDLAALEEQLEEL------------EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDR 735
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852868 541 LEERQKIGKL-DNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITAL 596
Cdd:COG4913 736 LEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-480 |
3.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 291 IREIKEL-----NELKDQIQDVEGKYMQGLkEMKDSLAEVEEKYKKamvsnaqLDNEKTnfmyQVDTLKDMLLELEEQLA 365
Cdd:PRK03918 576 LKELEELgfesvEELEERLKELEPFYNEYL-ELKDAEKELEREEKE-------LKKLEE----ELDKAFEELAETEKRLE 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 366 ESRRQYEEKNKEFEREKHAHsiLQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKE 445
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
170 180 190
....*....|....*....|....*....|....*
gi 1622852868 446 FFDsvrserdDLREEVVMLKEELKKHGIILNSEIA 480
Cdd:PRK03918 722 RVE-------ELREKVKKYKALLKERALSKVGEIA 749
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
284-468 |
3.64e-03 |
|
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: 40.33 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 284 SIDTEASIREIKEL---NELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMvsnAQLDNEKTNFM--YQVDTLKDMLL 358
Cdd:COG5185 304 SIDIKKATESLEEQlaaAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL---EAIKEEIENIVgeVELSKSSEELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 359 ELEEQLAESRRQYEEKNKEfeREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIG 438
Cdd:COG5185 381 SFKDTIESTKESLDEIPQN--QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622852868 439 AL------ERQKEFFDSVRSERDDLREEVVMLKEEL 468
Cdd:COG5185 459 EEsqsrleEAYDEINRSVRSKKEDLNEELTQIESRV 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
293-491 |
3.76e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 293 EIKELNELKDQIQDVEGKYMQGLK--EMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQ 370
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 371 YEEKNK----EFEREKHAHSILQFQFAEVKEALKEREEmleEIRQLQQKQASSIReiSDLQETIEWKDKKIGALERQKEF 446
Cdd:PTZ00121 1753 EEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDE---KRRMEVDKKIKDIF--DNFANIIEGGKEGNLVINDSKEM 1827
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622852868 447 FDSVRSERDDLREEVVMLKEELKKHGIILNSEiatNGETSDTLNN 491
Cdd:PTZ00121 1828 EDSAIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEAD 1869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
575-667 |
4.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 575 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 654
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|...
gi 1622852868 655 RLEKMKANRSALL 667
Cdd:COG4942 98 ELEAQKEELAELL 110
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
535-664 |
4.46e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 39.62 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 535 KKLKGQLEERQKI-GKLDNLRSEDDVLENGTDMHVMDLQ---RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-- 608
Cdd:pfam04849 171 EKLRGLEEENLKLrSEASHLKTETDTYEEKEQQLMSDCVeqlSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVdl 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852868 609 --RYKSAAENAEKIEDELKAEK---RKLQRELRSALDKTEELEvsnGHLVKRLEKMKANRS 664
Cdd:pfam04849 251 qhKCKELGIENEELQQHLQASKeaqRQLTSELQELQDRYAECL---GMLHEAQEELKELRK 308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-471 |
5.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 291 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLEleeqlaesRRQ 370
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE-------LEKLEKLLQL--------LPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 371 YEEKNKeferekhahsiLQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIE-----WKDKKIGALERQKE 445
Cdd:COG4717 131 YQELEA-----------LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEelleqLSLATEEELQDLAE 199
|
170 180
....*....|....*....|....*.
gi 1622852868 446 FFDSVRSERDDLREEVVMLKEELKKH 471
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEEL 225
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
373-644 |
5.79e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 373 EKNKEFEREK--HAHSILqfqfAEVKEALKEREEMLEEIRQLQQKQASSIRE-------ISDLQETIE------------ 431
Cdd:PRK02224 226 EEQREQARETrdEADEVL----EEHEERREELETLEAEIEDLRETIAETEREreelaeeVRDLRERLEeleeerddllae 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 432 --WKDKKIGALERQKEFFDSVRSE-RDDLREEVVMLK--------------------EELKKHGIILNSEIATNGETSDT 488
Cdd:PRK02224 302 agLDDADAEAVEARREELEDRDEElRDRLEECRVAAQahneeaeslredaddleeraEELREEAAELESELEEAREAVED 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 489 lnnvgYQGPTKMTKAELNALKSTGDGT------LDIRLKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLE 561
Cdd:PRK02224 382 -----RREEIEELEEEIEELRERFGDApvdlgnAEDFLEELREERDELREREAELEATLRTaRERVEEAEALLEAGKCPE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 562 NGTDM----HVMDLQrDANRQISDLKFKLAKSEQEITALEQNVIRL------ESQVSRYKSAAENAEKI---------ED 622
Cdd:PRK02224 457 CGQPVegspHVETIE-EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELiaerretieEK 535
|
330 340
....*....|....*....|...
gi 1622852868 623 ELKAE-KRKLQRELRSALDKTEE 644
Cdd:PRK02224 536 RERAEeLRERAAELEAEAEEKRE 558
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
530-666 |
6.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 530 LLEQIKKLKG---QLEE-RQKIGKLDNLRseddvlENGTDMHVMDLQRDANRQIsDLKFKLAKSEQEITALEQNVIRLES 605
Cdd:COG4913 230 LVEHFDDLERaheALEDaREQIELLEPIR------ELAERYAAARERLAELEYL-RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852868 606 QVSRYKSAAENAEKIEDELKAEKRKLQRELRSA-LDKTEELEVSNGHLVKRLEKMKANRSAL 666
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARL 364
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
292-645 |
6.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 292 REIKELNELKDQIQDVEGKYMQGLKEMKdslaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQY 371
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIE----RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 372 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIewkdKKIGALERQKEFFDSVR 451
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAII----KKLSVLQKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 452 SERDDLREEVVMLKEELKKHGIILNSEIATNGETSDtlnnvgYQGPTKMTKAELNALKSTGDGTLDIrLKKLVDERECLL 531
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE------YSKNIERMSAFISEILKIQEIDPDA-IKKELNEINVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 532 EQIKKLKGQLEERQK--IGKLDNLRSEDDVLEN-------GTDM---HVMDLQRDANRQISDLKFKLAKSEQEITALEQN 599
Cdd:PRK01156 419 QDISSKVSSLNQRIRalRENLDELSRNMEMLNGqsvcpvcGTTLgeeKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1622852868 600 VIRLES--------QVSRYKSAAENAEKIEDELKAEKRKLQReLRSALDKTEEL 645
Cdd:PRK01156 499 IVDLKKrkeyleseEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEI 551
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
392-469 |
6.78e-03 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 36.80 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 392 FAEVKEALKER---EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdsvrsERDDLREEVVMLKEEL 468
Cdd:pfam02403 11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83
|
.
gi 1622852868 469 K 469
Cdd:pfam02403 84 K 84
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
525-666 |
6.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 525 DERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENgtdmHVMDLQRDANR-----QISDLKFKLAKSEQEITALEQ 598
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyAELQEELEELEEELEELEA----ELEELREELEKlekllQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852868 599 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSnghLVKRLEKMKANRSAL 666
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAEL 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
393-664 |
7.52e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 393 AEVKEALKEREEmleeirQLQQKQASSIREISDLQETIewkdkkigaLERQKEffdsVRSERDDLREEVVMLKEELKKHG 472
Cdd:pfam02463 165 SRLKRKKKEALK------KLIEETENLAELIIDLEELK---------LQELKL----KEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 473 IILNSEIATNGETSDTLNNVGyqgptkMTKAELNALKStgdGTLDIRLKKLVDERECLLEQIKKLKGQLEER-QKIGKLD 551
Cdd:pfam02463 226 LLYLDYLKLNEERIDLLQELL------RDEQEEIESSK---QEIEKEEEKLAQVLKENKEEEKEKKLQEEELkLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 552 NLRSEDDVLENgtdmhvmdLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKL 631
Cdd:pfam02463 297 ELKSELLKLER--------RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
250 260 270
....*....|....*....|....*....|...
gi 1622852868 632 QRELRSALDKTEELEVSNGHLVKRLEKMKANRS 664
Cdd:pfam02463 369 EQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
394-629 |
9.11e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 394 EVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREE---VVMLKEELKK 470
Cdd:COG1340 58 EAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqtEVLSPEEEKE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 471 hgIILN-SEIATNGETSDTLNNVgyQGPTKMTKAELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigK 549
Cdd:COG1340 138 --LVEKiKELEKELEKAKKALEK--NEKLKELRAELKELRKEAE-EIHKKIKELAEEAQELHEEMIELYKEADELRK--E 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852868 550 LDNLRSEDDVLENGTDMHvmdlqrdaNRQISDLKFKLAKSEQEITALEQNVIRLESQVSRyKSAAENAEKIEDELKAEKR 629
Cdd:COG1340 211 ADELHKEIVEAQEKADEL--------HEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKKGEK 281
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