|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
628-958 |
8.98e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 628 EVENQMFVEGSQISEATCE--KLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAK 705
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 706 MTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfedskvhaeqvLNDKESHIKTLTERL 785
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------------LTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 786 LKMKDWAAMLGEDITDDDNlELEMNSEsengayldnppkgalkkliHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELT 865
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEE-QIEELSE-------------------DIESLAAEIEELEELIEELESELEALLNERASLE 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 866 EHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL-------YQENEMKLHRKL-TVEENYRLEKEEklskVDEKISH 937
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrLEGLEVRIDNLQeRLSEEYSLTLEE----AEALENK 962
|
330 340
....*....|....*....|.
gi 2217297509 938 ATEELETYRKRAKDLEEELER 958
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
574-881 |
2.56e-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: 65.09 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 574 REKKLALMLSGLIEEKSKL------LEKFSLVQK---EYEGYEVESSLKDASFEKEATEAQSLEVENQMfvegsqiseat 644
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLrrerekAERYQALLKekrEYEGYELLKEKEALERQKEAIERQLASLEEEL----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 645 cEKLNRSNSELEDEIlclekelkeekskhSEQDELMADISKRIQSL-EDESKSLKSQVAEAKMTFKIFQMNEERLKIAIK 723
Cdd:TIGR02169 254 -EKLTEEISELEKRL--------------EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 724 DALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHI-------KTLTERLLKMKDWAAMLG 796
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 797 EDI----TDDDNLELEMNSESENGAYLDNPPKGA---LKKLIHAAK-LNASLKTLEGERNQIYIQLSEVDKTKEELTEHI 868
Cdd:TIGR02169 399 REInelkRELDRLQEELQRLSEELADLNAAIAGIeakINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330
....*....|...
gi 2217297509 869 KNLQTEQASLQSE 881
Cdd:TIGR02169 479 DRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
587-956 |
9.54e-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: 60.03 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 587 EEKSKLLEKFS--LVQKEYEGYEVESSLKDASFEKEATEAQSL-----EVENQMFVEGSQIS--EATCEKLNRSNSELED 657
Cdd:TIGR04523 270 SEKQKELEQNNkkIKELEKQLNQLKSEISDLNNQKEQDWNKELkselkNQEKKLEEIQNQISqnNKIISQLNEQISQLKK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 658 EILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQK 737
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 738 QLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENga 817
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 818 yLDNPPKgALKKLIhaAKLNASLKTLEGERNQIYIQLSEV---------DKTKEELTEHIKNLQTEQASLQSENTHFENE 888
Cdd:TIGR04523 508 -LEEKVK-DLTKKI--SSLKEKIEKLESEKKEKESKISDLedelnkddfELKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297509 889 NQKLQQKLKVMTElyqenemklhrkltveENYRLEKEekLSKVDEKISHATEELETYRKRAKDLEEEL 956
Cdd:TIGR04523 584 QEEKQELIDQKEK----------------EKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
687-1015 |
1.34e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 687 IQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTfedskvh 766
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 767 AEQVLNDKESHIKTLTERLLKMK-----DWAAMLGEDITDDDNLELEMNSE-SENGAYLDNppkgaLKKLIhaAKLNASL 840
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQ-----LNEQI--SQLKKEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 841 KTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLH 911
Cdd:TIGR04523 352 TNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 912 RKLTVEENYRL--------EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARN 983
Cdd:TIGR04523 432 KETIIKNNSEIkdltnqdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKE 507
|
330 340 350
....*....|....*....|....*....|..
gi 2217297509 984 AERNLNDLRKENAhnRQKLTETELKFELLEKD 1015
Cdd:TIGR04523 508 LEEKVKDLTKKIS--SLKEKIEKLESEKKEKE 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
590-960 |
8.66e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.95 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 590 SKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVENQMFVEG-----SQIS--EATCEKLNRSNSELEDEILCL 662
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINdlESKIQNQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 663 EKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKdalNENSQLQESQKQLLQ- 741
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSk 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 742 ---------EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKD---WAAMLGEDITDDDNLE-LE 808
Cdd:TIGR04523 495 ekelkklneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEeLK 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 809 MNSES-------------ENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQ 875
Cdd:TIGR04523 575 QTQKSlkkkqeekqelidQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 876 ASLQSENTHFENENQKLQQKLKVMTELYQ--ENEMKLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE 953
Cdd:TIGR04523 655 KEIRNKWPEIIKKIKESKTKIDDIIELMKdwLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENII 734
|
....*..
gi 2217297509 954 EELERTI 960
Cdd:TIGR04523 735 KNFNKKF 741
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
586-1018 |
8.68e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 586 IEEKSKLLEKFSLVQKEYEGYEVEssLKDASFEKEATEAQSLEVENQMfVEGSQISEATCEKLNR--SNSELEDEILcle 663
Cdd:pfam05483 211 LEMHFKLKEDHEKIQHLEEEYKKE--INDKEKQVSLLLIQITEKENKM-KDLTFLLEESRDKANQleEKTKLQDENL--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 664 keLKEEKSKHSEQDELmADISKRIQSLEDESKSLKSQVAEAKMTfkIFQMNEERlkiaikdalneNSQLQESQKQLLQEA 743
Cdd:pfam05483 285 --KELIEKKDHLTKEL-EDIKMSLQRSMSTQKALEEDLQIATKT--ICQLTEEK-----------EAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 744 EVwkeqVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMkdwAAMLGEDITDDDNLELEMNSE----SENGAYL 819
Cdd:pfam05483 349 FV----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELkkilAEDEKLL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 820 DNppKGALKKLIHAAK-----LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQ 894
Cdd:pfam05483 422 DE--KKQFEKIAEELKgkeqeLIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 895 KLKVMTElyQENEMKLHRKLTVEENYRLEKEE-----KLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIIS 969
Cdd:pfam05483 500 ENKELTQ--EASDMTLELKKHQEDIINCKKQEermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2217297509 970 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYA 1018
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1015 |
2.29e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 833 AAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENthfENENQKLQQKLKVMTELyQENEMKLHR 912
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV---EQLEERIAQLSKELTEL-EAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 913 KLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT---IHSYQGQIISHEKKAHDNWLAARNAERNLN 989
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180
....*....|....*....|....*.
gi 2217297509 990 DLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
561-958 |
3.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 561 RSFRSVRSRLYVGREKKLALMLSGLIEEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEAteaqsLEVENQMFVEGSQI 640
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD--ELSQELSDASRKIGE-----IEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 641 SEATCEKLNRSNSELEDEILclekelkeekskhsEQDELMADISKRIQSLEDESKSLKSQVAEakmtfkifqmneerlki 720
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIE--------------NVKSELKELEARIEELEEDLHKLEEALND----------------- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 721 aIKDALNEnSQLQESQKQLlqeaevwkeqvSELNKQKVTFEDSKVHAEQVLNDK-------ESHIKTLTERLLKMKDWAA 793
Cdd:TIGR02169 784 -LEARLSH-SRIPEIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 794 MLGEDItDDDNLEL-EMNSESENgayldnpPKGALKKLIhaaklnASLKTLEGERNQIYIQLSEVDKTKEELT------- 865
Cdd:TIGR02169 851 SIEKEI-ENLNGKKeELEEELEE-------LEAALRDLE------SRLGDLKKERDELEAQLRELERKIEELEaqiekkr 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 866 EHIKNLQTEQASLQSENTHFENENQKLQQklkvmtelYQENEMKLHrklTVEENyRLEKEEKLSKVDEKISHATEELETY 945
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEE--------IPEEELSLE---DVQAE-LQRVEEEIRALEPVNMLAIQEYEEV 984
|
410
....*....|...
gi 2217297509 946 RKRAKDLEEELER 958
Cdd:TIGR02169 985 LKRLDELKEKRAK 997
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
675-994 |
3.98e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 675 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 754
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 755 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKdwAAMLGEDITDDDNLELEMNSESEngayldnppkgALKKLIHAA 834
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE--AELAEAEEELEELAEELLEALRA-----------AAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 835 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRkl 914
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 915 tveenyRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 994
Cdd:COG1196 482 ------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
683-1019 |
4.54e-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: 54.68 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 683 ISKRIQSLEDESKS------LKSQVAEAKMTFKIFQMNEERLKI-AIKDALNENSQLQESQKQLLQEAEvwkEQVSELNK 755
Cdd:TIGR02168 198 LERQLKSLERQAEKaerykeLKAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELE---EKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 756 QKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDwaamlgeditdddNLELEMNSESENGAYLDNPPKGALKKLIHAAK 835
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRE-------------RLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 836 LNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVM-TELYQENEMKLHRKL 914
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 915 TVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIishekkahdnwlaaRNAERNLNDLRKE 994
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL----REEL--------------EEAEQALDAAERE 483
|
330 340
....*....|....*....|....*
gi 2217297509 995 NAHNRQKLTETELKFELLEKDPYAL 1019
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
716-960 |
1.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 716 ERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDW-AAM 794
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 795 LGEditdddnleLEMNSESENGAYLDNP--PKGALKKLIHAAKLNASLKTlegernqiyiQLSEVDKTKEELTEHIKNLQ 872
Cdd:COG4942 110 LRA---------LYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARRE----------QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 873 TEQASLQSENTHFENENQKLQQKLKvmtelyqenemklhrkltveenyrlEKEEKLSKVDEKISHATEELETYRKRAKDL 952
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA-------------------------ERQKLLARLEKELAELAAELAELQQEAEEL 225
|
....*...
gi 2217297509 953 EEELERTI 960
Cdd:COG4942 226 EALIARLE 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
675-957 |
1.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 675 EQDELMADISKRIQSLED------ESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDA-------LNENSQLQESQKQLLQ 741
Cdd:PRK03918 142 ESDESREKVVRQILGLDDyenaykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKekeleevLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 742 EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAY 818
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 819 LDNppkgALKKLihaAKLNASLKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQK 895
Cdd:PRK03918 302 YEE----YLDEL---REIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217297509 896 LKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEKIShateELETYRKRAKDLEEELE 957
Cdd:PRK03918 375 ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
574-1015 |
1.68e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 574 REKKLALMLSGLIEEKSKLLEKfSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVEnqmfvegsQISEATcEKLNRSNS 653
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEK-ELEEVLREINEISSELPELREELEKLEKEVKELE--------ELKEEI-EELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 654 ELEDEIlclekelkeekskhSEQDELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEE--RLKIAIKDALNENSQ 731
Cdd:PRK03918 249 SLEGSK--------------RKLEEKIRELEERIEELKKEIEELEEKVKELK---ELKEKAEEyiKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 732 LQESQKQLLQEAEVWKEQVSELNKqkvtfedskvhaeqvlndKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNS 811
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 812 ESENGAYLDNPPKGALKKLIHAA------------KLNASLKTLEGERNQIYIQLSEVDKTK-------EELTEH----- 867
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELekakeeieeeisKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrkel 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 868 IKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEMKLHRKLTVEENYRlEKEEKLSKVD-EKISHATEELETYR 946
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLK-ELEEKLKKYNlEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 947 KRA-------KDLEEELERtIHSYQGQIISHEKK-----------------------------------AHDNWLAARNA 984
Cdd:PRK03918 532 EKLiklkgeiKSLKKELEK-LEELKKKLAELEKKldeleeelaellkeleelgfesveeleerlkelepFYNEYLELKDA 610
|
490 500 510
....*....|....*....|....*....|.
gi 2217297509 985 ERNLNDLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
834-958 |
1.85e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.17 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 834 AKLNASLKTLEGERNQIYIQLSEVDKTKEEltEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqENEMKLHRK 913
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQVERLEAEVEELEAELEEKDERIERL-----ERELSEARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2217297509 914 ltvEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 958
Cdd:COG2433 456 ---EERREIRKDREISRLDREIERLERELEEERERIEELKRKLER 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
575-1014 |
2.34e-06 |
|
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: 52.10 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 575 EKKLALMLSGLI--EEKSKLLEKFSLVQkEYEGYEVESSLK-------DASFEKEATEAQSLEVENQMFVEGSQISEATC 645
Cdd:pfam01576 158 EERISEFTSNLAeeEEKAKSLSKLKNKH-EAMISDLEERLKkeekgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 646 EkLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDEskslKSQVAEAKMTFKIFQMNEERLKIAIKDA 725
Cdd:pfam01576 237 Q-LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESE----RAARNKAEKQRRDLGEELEALKTELEDT 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 726 LNENSQLQESQKQLLQEaevwkeqVSELnkQKVTFEDSKVHAEQVLNDKESH---IKTLTERLLKMKDWAAML--GEDIT 800
Cdd:pfam01576 312 LDTTAAQQELRSKREQE-------VTEL--KKALEEETRSHEAQLQEMRQKHtqaLEELTEQLEQAKRNKANLekAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 801 DDDNLELEMNSESENGAYLDNPPKGalkklihaaklnaslKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQS 880
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKR---------------KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 881 ENTHFENENQKLQQKLKVMtelyqenEMKLHrklTVEENYRLEKEEKLSkVDEKISHATEELETYRKRAKDLEE---ELE 957
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSL-------ESQLQ---DTQELLQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEakrNVE 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217297509 958 RTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1014
Cdd:pfam01576 517 RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
587-879 |
4.19e-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: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 587 EEKSKLLEKFSLVQKEYEgyEVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEilclekel 666
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIE--NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE-------- 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 667 keekskHSEQDELMADISKRIQS-------LEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQL 739
Cdd:TIGR02169 807 ------VSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 740 LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmkdwaAMLGEDITDDDNLELEMNSESENgayl 819
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEE---- 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 820 dNPPKGALKKLIHaaKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQ 879
Cdd:TIGR02169 950 -ELSLEDVQAELQ--RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
827-973 |
4.98e-06 |
|
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: 49.15 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 827 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL---- 902
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297509 903 -----YQ--ENEM-KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 973
Cdd:COG1579 86 rnnkeYEalQKEIeSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
607-973 |
6.35e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 607 EVESSLKDAsfeKEATEAQSLEVENQMFVEGSQISEATCEK--LNRSNSELEDEIlclekelkeekskhseqDELMADIS 684
Cdd:pfam15921 328 QLRSELREA---KRMYEDKIEELEKQLVLANSELTEARTERdqFSQESGNLDDQL-----------------QKLLADLH 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 685 KRIQ--SLEDE-SKSLKSQVAEAKMTFKIFQ-------MNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 754
Cdd:pfam15921 388 KREKelSLEKEqNKRLWDRDTGNSITIDHLRrelddrnMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 755 KQkvtFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDitdddnlELEMNSESENGAYLDNPPKGALKKLIHAA 834
Cdd:pfam15921 468 AQ---LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-------ERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 835 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNL--------------QTEQASLQSENTHFENENQKLQ------- 893
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilkdkkd 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 894 ---QKLKVMTELYQENEMKL----HRKLTVEENYRLEKEEKLSKVD---EKISHATEELETYRKRAKDLEEELERTIHSY 963
Cdd:pfam15921 618 akiRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
410
....*....|
gi 2217297509 964 QGQIISHEKK 973
Cdd:pfam15921 698 KMQLKSAQSE 707
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
722-907 |
6.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 722 IKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLlkmKDWAAMLGEDITD 801
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 802 DDNLELEMNSESeNGAYLDNppKGALKKLIHAAklNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSE 881
Cdd:COG3883 102 VSYLDVLLGSES-FSDFLDR--LSALSKIADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180
....*....|....*....|....*.
gi 2217297509 882 NTHFENENQKLQQKLKVMTELYQENE 907
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
600-896 |
7.52e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 600 QKEYEGYEVESSLK-----DASFEKEATEAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEIlclekelkeekskhS 674
Cdd:COG1196 219 KEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------E 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 675 EQDELMADISKRIQSLEDESKSLKSQVAEAkmtfkifQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELN 754
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 755 KQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMNSESEngayldnppkgalKKLIHAA 834
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------------RLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217297509 835 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL 896
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
586-929 |
1.36e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 586 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASF---EKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNS---ELEDEI 659
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELE-EKLEELRLevsELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 660 lclEKELKEEKSKHSEQDELMADI---SKRIQSLEDESKSLKSQVAEakmtfkifqmNEERLKIAIKDAlnenSQLQESQ 736
Cdd:TIGR02168 284 ---EELQKELYALANEISRLEQQKqilRERLANLERQLEELEAQLEE----------LESKLDELAEEL----AELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 737 KQLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITD-DDNLElemNSESEN 815
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRE---RLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 816 GAYLDNPPKGALKKLIHA-AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQ 894
Cdd:TIGR02168 424 EELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217297509 895 KLKVMTELYQENEMK------LHRKLTVEENYRLEKEEKLS 929
Cdd:TIGR02168 504 FSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAIEAALG 544
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
685-1015 |
2.44e-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: 48.81 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 685 KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENsQLQESQKQLLQEAEVWKEQV-SELNKQKVTFEDS 763
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL-QELKLKEQAKKALEYYQLKEkLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 764 KVHAEQVLNDKESHIKTLTERLLKMKdwaamlGEDITDDDNLELEMNSESENGAYLDNPPKGALKKLIHAAKLNASLKTL 843
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSK------QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 844 EGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRKLTV------- 916
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleser 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 917 -------EENYRLEKEEKLSKVDEKISHATEELETYRKRAKDL---EEELERTIHSYQGQIIshEKKAHDNWLAARNAER 986
Cdd:pfam02463 386 lssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleiLEEEEESIELKQGKLT--EEKEELEKQELKLLKD 463
|
330 340
....*....|....*....|....*....
gi 2217297509 987 NLNDLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
674-1036 |
3.36e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 674 SEQDELmADISKRIQSLEDESKSLKSQVAEAKMtfkifQMNEerLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 753
Cdd:TIGR02169 671 SEPAEL-QRLRERLEGLKRELSSLQSELRRIEN-----RLDE--LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 754 NKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAamlgEDITDDDNLELEMNSESEngayldnppkgalkklihA 833
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEARLSHSRIPEIQAE------------------L 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 834 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENEnqklqqklkvmtelyqenemklhrk 913
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------------------------- 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 914 ltvEENYRLEKEEKLskvdekishatEELETYRKRAKDLEEELErtihSYQGQIISHEKKahdnwlaARNAERNLNDLRK 993
Cdd:TIGR02169 856 ---IENLNGKKEELE-----------EELEELEAALRDLESRLG----DLKKERDELEAQ-------LRELERKIEELEA 910
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2217297509 994 ENAHNRQKLTETELKFELLEKDPYALDvPNTAFGREHSPYGPS 1036
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELS 952
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
840-1014 |
3.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 840 LKTLEGERNQIYIQLSEVdktkEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtELYQENEmKLHRKLTvEEN 919
Cdd:COG4717 73 LKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELE-ALEAELA-ELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 920 YRLE----KEEKLSKVDEKISHATEELETYRKrakDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKEN 995
Cdd:COG4717 146 ERLEeleeRLEELRELEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170
....*....|....*....
gi 2217297509 996 AHNRQKLTETELKFELLEK 1014
Cdd:COG4717 223 EELEEELEQLENELEAAAL 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
607-983 |
9.86e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 607 EVESSLKDASFEKEATEAQSLEVENQMFVEGSQISEATcEKLNRSNSELEDeilclekELKEEKSKHSEQDELMADI--- 683
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI-EKKDHLTKELED-------IKMSLQRSMSTQKALEEDLqia 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 684 SKRIQSLEDESKSLKSQVAEAKMTFKI----------------------FQMNEERLKIAIKDALNENSQLQESQKqLLQ 741
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFvvtefeattcsleellrteqqrLEKNEDQLKIITMELQKKSSELEEMTK-FKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 742 EAEVWKEQVSEL--NKQKVTFEDSKVH--AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMnseSENGA 817
Cdd:pfam05483 402 NKEVELEELKKIlaEDEKLLDEKKQFEkiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV---EDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 818 YLDNPPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSE-------VDKTKEELTEHIKNLQTEQASLQSENTHFENENQ 890
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqediinCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 891 KLQQKLKVMTELYQENEMKLHRKLTVEE-----------NYRLEKEEKLSKVDE----------KISHATEELETYRKRA 949
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSIEYEVLKKEkqmkilenkcnNLKKQIENKNKNIEElhqenkalkkKGSAENKQLNAYEIKV 638
|
410 420 430
....*....|....*....|....*....|....
gi 2217297509 950 KDLEEELERTIHSYQGQIISHEKKAHDNWLAARN 983
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-1014 |
1.20e-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: 46.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 685 KRIQSLEDESKSLKSQVAEAKMTF-----KIFQMNEERLKIAI-----KDALNEN-SQLQESQKQLLQ------------ 741
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLkknkdKINKLNSDLSKINSeikndKEQKNKLeVELNKLEKQKKEnkknidkfltei 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 742 -----EAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEMN-SESEN 815
Cdd:TIGR04523 148 kkkekELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeLKKQN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 816 gayldnppkgalkklihaAKLNASLKTLEGERNQIYIQLSEVDK----TKEELTEHIKNLQTEQASLQSENT---HFENE 888
Cdd:TIGR04523 228 ------------------NQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 889 NQKLQQKLKVMTELYQENEMK-LHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLE---EELERTIHSYQ 964
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQ 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217297509 965 GQIISHEKKAHDNWLAARNAERNLNDLR-------KENAHNRQKLTETELKFELLEK 1014
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQINDLEskiqnqeKLNQQKDEQIKKLQQEKELLEK 426
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
586-1005 |
1.63e-04 |
|
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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 586 IEEKSKLLEKFSLVQKEYEGYEVESSLKDASFEKEATEAQSLEVEnqmfvegSQISEATCEKLNRSNSELEDEilclEKE 665
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDIL----QRE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 666 LKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEV 745
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 746 WKEQVSELNKQKVT---FEDSKVHAEQVLNDKEShIKTLTERLLKMKDWAAMLGEDItddDNLELEMNSESENGAYLDNP 822
Cdd:TIGR00618 489 KAVVLARLLELQEEpcpLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSE---EDVYHQLTSERKQRASLKEQ 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 823 PKGALKKL-IHAAKLNASLKTLEGERN-----QIYIQ--LSEVDKTKEELTEHIKNLQtEQASLQSENTHFENENQKLQQ 894
Cdd:TIGR00618 565 MQEIQQSFsILTQCDNRSKEDIPNLQNitvrlQDLTEklSEAEDMLACEQHALLRKLQ-PEQDLQDVRLHLQQCSQELAL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 895 KL----KVMTELYQENE------MKLHRKLTVEENYRLEKE-----EKLSKVDEKISHATE---ELETYRKRAKDLEEEL 956
Cdd:TIGR00618 644 KLtalhALQLTLTQERVrehalsIRVLPKELLASRQLALQKmqsekEQLTYWKEMLAQCQTllrELETHIEEYDREFNEI 723
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2217297509 957 ERTIHSyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTET 1005
Cdd:TIGR00618 724 ENASSS-LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
747-958 |
1.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 747 KEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTL-------TERLLKMKDWAAMLGEDI------TDDDNLELEMNSES 813
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQrkkngenIARKQNKYDELVEEAKTIkaeieeLTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 814 engayldnpPKGALKKLIHA-AKLNASLKTLEGERN------------QiyiQLSEVDKTKEELTEHIKNLQTeqaSLQS 880
Cdd:PHA02562 253 ---------PSAALNKLNTAaAKIKSKIEQFQKVIKmyekggvcptctQ---QISEGPDRITKIKDKLKELQH---SLEK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297509 881 ENTHFENENQKLQQklkvmtelYQENEMKLHrkltveenyrlEKEEKLSKVDEKIShateeleTYRKRAKDLEEELER 958
Cdd:PHA02562 318 LDTAIDELEEIMDE--------FNEQSKKLL-----------ELKNKISTNKQSLI-------TLVDKAKKVKAAIEE 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-1022 |
2.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 826 ALKKLIhaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELY-- 903
Cdd:COG4942 31 QLQQEI--AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 904 -------------------QENEMKLHRKLTVEE---NYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIH 961
Cdd:COG4942 109 llralyrlgrqpplalllsPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217297509 962 SYQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKDPYALDVP 1022
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
834-959 |
2.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 834 AKLNASLKTLEGERNQI--YIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLH 911
Cdd:COG4717 105 EELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2217297509 912 RKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERT 959
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
826-1015 |
3.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 826 ALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQK---LQQKL-KVMTE 901
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeAQAEEyELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 902 LYQENEMKLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAKDLEEEL----------ERTIHSYQGQIIS 969
Cdd:COG1196 297 LARLEQDIARLEERRRELEerLEELEEELAELEEELEELEEELEELEEELEEAEEELeeaeaelaeaEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217297509 970 HEKKAHDNWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
675-907 |
4.89e-04 |
|
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: 44.83 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 675 EQDELMADISKRIQSLEDESKSLKSQVAEAKMTFK-IFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSEL 753
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 754 NKQKVTFEDSKVHAEQVLNDKESHIKT--------LTERLLKMKDWAAMLGEDITDD-DNLELEMNSESENGAYLDNPPK 824
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEqnnrdiagIKDKLAKIREARDRQLAVAEDDlQALESELREQLEAGKLEFNEEE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 825 GALKKLIHAAK--LNASLKTLEgERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTEL 902
Cdd:pfam12128 440 YRLKSRLGELKlrLNQATATPE-LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
....*
gi 2217297509 903 YQENE 907
Cdd:pfam12128 519 QSALD 523
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
680-905 |
5.19e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 680 MADISKRIQSLEDESKSLKSQVAEAkmtfkifqmnEERLKiAIKDAlNENSQLQESQKQLLQeaevwkeQVSELNKQKVT 759
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA----------EAALE-EFRQK-NGLVDLSEEAKLLLQ-------QLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 760 fedskvhAEQVLNDKESHIKTLTERLLKMKDWAAMLGED------ITDDDNLELEMNSESENgaYLDNPPKgalkklihA 833
Cdd:COG3206 231 -------ARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSAR--YTPNHPD--------V 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217297509 834 AKLNASLKTLEGERNQiyiqlsEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQE 905
Cdd:COG3206 294 IALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-782 |
5.43e-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: 44.66 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 561 RSFRSVRSRLY-----VGREKKLALMLSGLIEEKSKLLEKFSLVQKEYE--GYEVESSLKDASFEKEATEAQSLEVENQM 633
Cdd:TIGR02168 817 EEAANLRERLEslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEALALLRSEL 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 634 FVEGSQIseatcEKLNRSNSELEDEilclekelkeekskHSEQDELMADISKRIQSLEDESKSLKSQVAE-AKMTFKIFQ 712
Cdd:TIGR02168 897 EELSEEL-----RELESKRSELRRE--------------LEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAE 957
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297509 713 MNEERLKIAIKDALNENSQLQESQKQL-------LQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLN--DKESHIKTLT 782
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEeiDREARERFKD 1036
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
654-966 |
7.16e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 654 ELEDEILCLEKELKEEKSKHSEQDELMADIS------KRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALN 727
Cdd:PRK01156 153 KILDEILEINSLERNYDKLKDVIDMLRAEISnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 728 ENSQLQESQKQLLQEAEVWKEQVSELNKQkvtfeDSKVHAEQVLNDKeshIKTLTERLLKMKDWAAMLG-EDITDDDNLE 806
Cdd:PRK01156 233 DYNNLKSALNELSSLEDMKNRYESEIKTA-----ESDLSMELEKNNY---YKELEERHMKIINDPVYKNrNYINDYFKYK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 807 LEMNSESENGAYLDnppkGALKKLIHAAKlnaSLKTLEGERNQIYIQLSEVDKTKEELTEhiknLQTEQASLQSENTHFE 886
Cdd:PRK01156 305 NDIENKKQILSNID----AEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILE----LEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 887 NENQKLQQKLKVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEkISHATEELETYRKRAKDLEEELERTIHSYQGQ 966
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-ISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
677-789 |
9.43e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 677 DELMADISKRIQSLEDESKSLKSQVAEAKmtfKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQ 756
Cdd:smart00787 171 NSIKPKLRDRKDALEEELRQLKQLEDELE---DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNK 247
|
90 100 110
....*....|....*....|....*....|....*..
gi 2217297509 757 KVTFEDSKVHAEQVLND----KESHIKTLTERLLKMK 789
Cdd:smart00787 248 KSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQ 284
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
651-1000 |
9.45e-04 |
|
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: 43.67 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 651 SNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIF--QMNEERLKI------AI 722
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdEKQSEKDKKnkalaeRK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 723 KDALNENSQLQESQKQLLQEAEVWKEQVSElnkQKVTFEDSKVHAEQVL-NDKESHIKTLTERLLKMKDWAAMLGEDITD 801
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKE---QKREARTEKQAYWQVVeGALDAQLALLKAAIAARRSGAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 802 DDNLELE-MNSESENGAYLDNPPKGALKKLIHAAKLNASL--------KTLEGERNQIYIQLSEVDKTKEELTEhikNLQ 872
Cdd:pfam12128 755 WYKRDLAsLGVDPDVIAKLKREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQQ---QLA 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 873 TEQASLQSENTHFENENQKLQQKLKVMTElyqenemkLHRKLTVEENY--RLEKEEKLSKVDEKISHATEELETYRKRAK 950
Cdd:pfam12128 832 RLIADTKLRRAKLEMERKASEKQQVRLSE--------NLRGLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2217297509 951 DLEEELERTIHSYQGQIISHEKKAHD-NWLAARNAERNLNDLRKENAHNRQ 1000
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHSGSGLAeTWESLREEDHYQNDKGIRLLDYRK 954
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
840-964 |
1.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 840 LKTLEGERNQIYIQLSEVDKTK---EELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHR---K 913
Cdd:COG4913 663 VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2217297509 914 LTVEENYRLEK---EEKLSKVDEKISHA-TEELETYRKRAKDLEEELERTIHSYQ 964
Cdd:COG4913 743 ARLELRALLEErfaAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFN 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
576-1015 |
1.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 576 KKLALMLSGLIEEKSKLLEKFSLVQKEYEGYE-----VESSLKDA-SFEKEATEAQSLEVENQMFVEGSQISEATCEKLN 649
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeeingIEERIKELeEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 650 RSNSELEdeilclEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNEN 729
Cdd:PRK03918 369 AKKEELE------RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 730 SQL-QESQKQLLQEaevWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTlTERLLKMKDWAAMLgeditdddnLELE 808
Cdd:PRK03918 443 RELtEEHRKELLEE---YTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQL---------KELE 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 809 MNSESENGAYLDNPPKGALKKLIHAAKLNASLKTLEGERNQiyiqLSEVDKTKEELTEHIKNLQTEQASL--QSENTHFE 886
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELlkELEELGFE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 887 NEnQKLQQKLKVMTELYQE-NEMKLHRKltveenyRLE-KEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYq 964
Cdd:PRK03918 586 SV-EELEERLKELEPFYNEyLELKDAEK-------ELErEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY- 656
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2217297509 965 gqiiSHEKKahdnwlaaRNAERNLNDLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:PRK03918 657 ----SEEEY--------EELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
623-1004 |
1.31e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 623 EAQSLEVENQMFVEGSQISEATCEKLNRSNSELEDEILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQVA 702
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 703 EakmtfkifqmNEERlkiaikdalneNSQLQESQKQLLQEAEVWKEQVSELN--KQKVTFEdsKVHAEQVLNDKESHIKT 780
Cdd:pfam01576 86 E----------EEER-----------SQQLQNEKKKMQQHIQDLEEQLDEEEaaRQKLQLE--KVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 781 LTERLLKMKDWAAMLGEDITDDDNLELEMNSESENGAYLDNppkgalKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKT 860
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKN------KHEAMISDLEERLKKEEKGRQELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 861 KEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmTELYQENE-MKLHRKLtveENYRLEKEEKLSKvdEKISHAT 939
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKNNaLKKIREL---EAQISELQEDLES--ERAARNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 940 EEletyrKRAKDLEEELE----------------RTIHSYQGQIISHEKKAHDNwlAARNAERNLNDLRKENAHNRQKLT 1003
Cdd:pfam01576 290 AE-----KQRRDLGEELEalkteledtldttaaqQELRSKREQEVTELKKALEE--ETRSHEAQLQEMRQKHTQALEELT 362
|
.
gi 2217297509 1004 E 1004
Cdd:pfam01576 363 E 363
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
822-973 |
1.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 822 PPKGALKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFE--NENQKLQQKLKVM 899
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 900 TELYQENEMKLHRKLTVEENYR---------------------LEKEEKLSKVDEKISHATEELETYRKRAKDLEEELER 958
Cdd:COG4717 145 PERLEELEERLEELRELEEELEeleaelaelqeeleelleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*...
gi 2217297509 959 T---IHSYQGQIISHEKK 973
Cdd:COG4717 225 LeeeLEQLENELEAAALE 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
712-959 |
1.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 712 QMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSELNKQKvtfedsKVHAEQVLNDKEShIKTLTERLLKMKDW 791
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQV------KELREEAQELREK-RDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 792 AAMLGEDITDDDNlELEMNSESENGAYLDNPPKGALKKLIhaAKL-----NASLkTLEGERnQIYIQLSEVD------KT 860
Cdd:COG1340 80 RDELNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEI--ERLewrqqTEVL-SPEEEK-ELVEKIKELEkelekaKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 861 KEELTEHIKNLQTEQASLQSE-NTHFENEN---QKLQQKLKVMTELYQE-NEMK-----LHRKLtveenyrLEKEEKLSK 930
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEaEEIHKKIKelaEEAQELHEEMIELYKEaDELRkeadeLHKEI-------VEAQEKADE 227
|
250 260
....*....|....*....|....*....
gi 2217297509 931 VDEKISHATEELETYRKRAKDLEEELERT 959
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| YabA |
COG4467 |
Regulator of replication initiation timing YabA [Replication, recombination and repair]; |
846-913 |
2.12e-03 |
|
Regulator of replication initiation timing YabA [Replication, recombination and repair];
Pssm-ID: 443564 [Multi-domain] Cd Length: 107 Bit Score: 39.08 E-value: 2.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297509 846 ERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQENEMKLHRK 913
Cdd:COG4467 2 DKKELFDRLSELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKEKKAEKDIGE 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
680-958 |
2.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 680 MADISKRIQSLEDESKSLKSQVAEAKMTFKifqmNEERLkIAIKDALNENSQLQESQKQL--------LQEAEVWKEQVS 751
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLK----KESEL-IKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 752 ELNKQKVTFEDSKVHAEQVLNDK---ESHIKTLTERLLKMKDWAAMLGEDITDDDNLELEmNSESENGAYLDnpPKGALK 828
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLE--LKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 829 KLihaAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQT-----EQASLQSENTHFENENQKLQQKLKVMTELY 903
Cdd:PRK03918 613 EL---EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRR 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217297509 904 QENEMKLhRKLTVEENYRLEKEEKLskvdEKISHATEELETYRKRAKDLEEELER 958
Cdd:PRK03918 690 EEIKKTL-EKLKEELEEREKAKKEL----EKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
682-1013 |
2.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 682 DISKRIQSLEDESKSLKSQVAEAKMTFKIFQMNEERLKIAIKDALNENSQLQESQKQLLQEAEVWKEQVSElnkqkvtfe 761
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 762 dskvhAEQVLNDKESHIKTLTERLlkmkdwaamlgEDITDD-DNLELEMNSESENgayldnppKGALKKLIhaAKLNASL 840
Cdd:PRK02224 382 -----RREEIEELEEEIEELRERF-----------GDAPVDlGNAEDFLEELREE--------RDELRERE--AELEATL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 841 KTLEG--ERNQiyiQLSEVDKTKE-----ELTEHIKNL---QTEQASLQSENTHFENENQKLQQKLKVMTELyQENEMKL 910
Cdd:PRK02224 436 RTARErvEEAE---ALLEAGKCPEcgqpvEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 911 HRKLTVEENYRLEKEEKLSKVDEKishaTEELETYRKRAKDLEEELERTIHSYQgqiishekKAHDNWLAARNAERNLND 990
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEEKREAAA--------EAEEEAEEAREEVAELNS 579
|
330 340
....*....|....*....|...
gi 2217297509 991 LRKENAHNRQKLTETELKFELLE 1013
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
832-1015 |
2.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 832 HAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKL-KVMTELYQENE--M 908
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELeQARSELEQLEEelE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 909 KLHRKLTVEENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERtihsyqgqiISHEKKAHDNWLAARNAErnL 988
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ---------LEAQIAELQSEIAEREEE--L 152
|
170 180
....*....|....*....|....*..
gi 2217297509 989 NDLRKENAHNRQKLTETELKFELLEKD 1015
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEA 179
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
827-1013 |
2.36e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 827 LKKLIHAAKLNASLKTLEGERNQIYIQLSEVDKTKEELTE--HIKNLQTEQASL-----QSENTHFENENQ---KLQQKL 896
Cdd:pfam13868 11 LNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEeeRERALEEEEEKEeerkeERKRYRQELEEQieeREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 897 KVMTELYQENEMKLHRKLTVEENYRLEKEEKLSKVDEK---ISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKK 973
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLreeIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217297509 974 AHDNWLAARNA-ERNLNDLRKENAHNRQKLTE-TELKFELLE 1013
Cdd:pfam13868 171 REAEREEIEEEkEREIARLRAQQEKAQDEKAErDELRAKLYQ 212
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
673-1008 |
2.75e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 673 HSEQDELMADISKRIQSLEDESKSLKS-QVAEAKMTFKIFQMNEERLKIAIKdalnenSQLQESQKQLLQEAEVWKEQVS 751
Cdd:TIGR01612 488 NSKQDNTVKLILMRMKDFKDIIDFMELyKPDEVPSKNIIGFDIDQNIKAKLY------KEIEAGLKESYELAKNWKKLIH 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 752 ELNKQKVTFEDSKVHAeqvlndkESHIKTLTERLLKMKDwaamlgeDITDDDNLELEMNSESENGAYLDNPPKGA--LKK 829
Cdd:TIGR01612 562 EIKKELEEENEDSIHL-------EKEIKDLFDKYLEIDD-------EIIYINKLKLELKEKIKNISDKNEYIKKAidLKK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 830 LIhaaklnaslktlegERNQIYIqlSEVDKTKE-ELTEHIKNLQTEQASLQSENTH-FENENQKLQQKLkvmTELYQENE 907
Cdd:TIGR01612 628 II--------------ENNNAYI--DELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNEL---SSIVKENA 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 908 MKlhrklTVEENYRLEK-EEKLSKVDEKISHATEE--------LETYRKRAKDLEEELERTIHSYqgqiISHE--KKAHD 976
Cdd:TIGR01612 689 ID-----NTEDKAKLDDlKSKIDKEYDKIQNMETAtvelhlsnIENKKNELLDIIVEIKKHIHGE----INKDlnKILED 759
|
330 340 350
....*....|....*....|....*....|...
gi 2217297509 977 NWLAARNAERNLNDLRKENAH-NRQKLTETELK 1008
Cdd:TIGR01612 760 FKNKEKELSNKINDYAKEKDElNKYKSKISEIK 792
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
677-905 |
2.82e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 677 DELMADISKRiQSLEDESKSLKSQVAEAKMTFKIFQMNEERL-----KIAIKDALNEN--------SQLQESQKQLLQEA 743
Cdd:TIGR01612 1486 NELKEHIDKS-KGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALAIKNKFAKTkkdseiiiKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 744 EVWKEQVSELNKQKVTFEDSKVH---AEQVLNDKESHIKTLTERLLKMKDWAAMLGEDITDDDNLE-----LEMNSE--- 812
Cdd:TIGR01612 1565 EKSEQKIKEIKKEKFRIEDDAAKndkSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEkkissFSIDSQdte 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 813 -SENGAYLD----------NPPKGALKKLIHAAKLNASLKTLEGERNQ--------IYIQLSEVDKTKEELTEHIKNL-- 871
Cdd:TIGR01612 1645 lKENGDNLNslqefleslkDQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigIIEKIKEIAIANKEEIESIKELie 1724
|
250 260 270
....*....|....*....|....*....|....*..
gi 2217297509 872 QTEQASLQSENTH-FE--NENQKLQQKLKVMTELYQE 905
Cdd:TIGR01612 1725 PTIENLISSFNTNdLEgiDPNEKLEEYNTEIGDIYEE 1761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
923-1006 |
3.05e-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: 41.67 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 923 EKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNWLAARNAERNLNDLRKENAHNRQKL 1002
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
....
gi 2217297509 1003 TETE 1006
Cdd:COG4942 100 EAQK 103
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
675-1015 |
4.36e-03 |
|
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: 41.35 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 675 EQDELMADISKRIQSLEDESKSlkSQVAEAKMtfkifqmnEERL--KIAIKDALNEnsQLQESQKQLLQEAEVWKEQVSE 752
Cdd:pfam10174 412 DKDKQLAGLKERVKSLQTDSSN--TDTALTTL--------EEALseKERIIERLKE--QREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 753 LNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKmkdwaamlgediTDDDNLELEMNSEsengayldnppkgalKKLIH 832
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLK------------KDSKLKSLEIAVE---------------QKKEE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 833 AAKLNASLKTLEgernqiyiQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMtelyqenemklhr 912
Cdd:pfam10174 533 CSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV------------- 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 913 kltveENYRLEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTihsyQGQIISHEKKAHDNwLAARNAERNLNDLR 992
Cdd:pfam10174 592 -----ENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK----GAQLLEEARRREDN-LADNSQQLQLEELM 661
|
330 340
....*....|....*....|....*...
gi 2217297509 993 KENAHNRQKLTETELKFE-----LLEKD 1015
Cdd:pfam10174 662 GALEKTRQELDATKARLSstqqsLAEKD 689
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
834-1006 |
5.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 834 AKLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKVMTELYQ--------E 905
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQlrarieelR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 906 NEMKLHRKLTVEENYRLEKE------EKLSKVDEKISHATEEL-ETYRKRAKDLEeelERTIHSYQGQIISHEKKAHDNW 978
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELqSKMRSRAKLLM---KRAAHVKQQSSIEEQRRLLQTL 350
|
170 180
....*....|....*....|....*....
gi 2217297509 979 LAARNAERNLNDLRKE-NAHNRQKLTETE 1006
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSiREISCQQHTLTQ 379
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
685-895 |
6.06e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 685 KRIQSLEDESKSLKSQVaEAKMtfKIFQMNEERLKIaikdalnensQLQESQKQLLQEaevwKEQVSELNKQKVTFEDSK 764
Cdd:pfam15905 152 KKMSSLSMELMKLRNKL-EAKM--KEVMAKQEGMEG----------KLQVTQKNLEHS----KGKVAQLEEKLVSTEKEK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 765 V----HAEQVLNDKEsHIKTLTERLLKMKDWAAMLGEDI-TDDDNLELEMNSESENgayldnppKGALKKLIHaaKLNAS 839
Cdd:pfam15905 215 IeeksETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLkEKNDEIESLKQSLEEK--------EQELSKQIK--DLNEK 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217297509 840 LKTLEGERNQIyiqLSEvDKTKEEltehikNLQTEQASLQSENTHFENENQKLQQK 895
Cdd:pfam15905 284 CKLLESEKEEL---LRE-YEEKEQ------TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
582-1014 |
7.27e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 582 LSGLIEEKSKLLEK--FSLVQKEYEGYEVESSLKDA-SFEKEATEAqslEVENQMFVEGSQISEATCEKLNRSNSELE-D 657
Cdd:TIGR00606 438 LGRTIELKKEILEKkqEELKFVIKELQQLEGSSDRIlELDQELRKA---ERELSKAEKNSLTETLKKEVKSLQNEKADlD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 658 EILCLEKELKEEKSKHSEQDELMADISKRIQSLEDESKSLKSQvaeakmtfkifqmNEERLKIAIKDALNEnSQLQESQK 737
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSR-------------HSDELTSLLGYFPNK-KQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 738 QLLQEAEVWKEQVSELNKQKVTFEDSKVHAEQVLNDKESHIKTLTERLLKmkdwaAMLGEDITDD-DNLELEMNSESENG 816
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-----VCGSQDEESDlERLKEEIEKSSKQR 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 817 AYLDNppkgalkklihAAKLNASLKTLEGERNQIYIQLSEVD-KTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQK 895
Cdd:TIGR00606 656 AMLAG-----------ATAVYSQFITQLTDENQSCCPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 896 LKVMTELY--QENEMKLHRKLTVEENYRLEK-EEKLSKVDEKISHATEELETY---RKRAKDLEEELErTIHSYQGQIIS 969
Cdd:TIGR00606 725 RDEMLGLApgRQSIIDLKEKEIPELRNKLQKvNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVT-IMERFQMELKD 803
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2217297509 970 HEKKAHD--NWLAARNAERNLNDLRKENAHNRQKLTETELKFELLEK 1014
Cdd:TIGR00606 804 VERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
835-1020 |
7.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 835 KLNASLKTLEGERNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENENQKLQQKLKvmtELYQENEmklhrKL 914
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE---ELQKERQ-----DL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 915 TVEENyrlEKEEKLSKVDEKISHATEELETYRKRAKDLEEELERTIHSYQGQIISHEKKAHDNWLAARNAERNLNDLRKE 994
Cdd:COG4372 128 EQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180
....*....|....*....|....*.
gi 2217297509 995 NAHNRQKLTETELKFELLEKDPYALD 1020
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
829-1005 |
7.70e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 829 KLIHAAKLNASLKTLEGErNQIYIQLSEVDKTKEELTEHIKNLQTEQASLQSENTHFENenqklQQKLKVMTelYQENEM 908
Cdd:pfam09787 25 KLIASLKEGSGVEGLDSS-TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEA-----QQQEEAES--SREQLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297509 909 KLHRKLTVEENYRLEKEEKLSKVDEKISHateeletyrkrakdLEEELERTIHSYQGQIISHEKKAHDnwLAARNAERNL 988
Cdd:pfam09787 97 ELEEQLATERSARREAEAELERLQEELRY--------------LEEELRRSKATLQSRIKDREAEIEK--LRNQLTSKSQ 160
|
170
....*....|....*...
gi 2217297509 989 NDLRKENAHNRQK-LTET 1005
Cdd:pfam09787 161 SSSSQSELENRLHqLTET 178
|
|
| |
