|
Name |
Accession |
Description |
Interval |
E-value |
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-889 |
1.31e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 657 KKLKEINEKVSNSRDQLSTKVFELKlQLNRELETAET-LKNERKDSAKLRNEVNQLKDQLEREREIAYGLQEEASKLrvg 735
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELE-QLEEELEELNEqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 736 tgkDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEEGPSNHEDENGSYRKVLWK-- 813
Cdd:COG4372 128 ---EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELae 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510765 814 -HQKIKDLYRKGEQQREAEEMVNKLISLNQHPEVQHISFLELESFKKQISDYLHTVEKNIQKIKRNDDFTNLEPLPE 889
Cdd:COG4372 205 aEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
556-885 |
6.38e-05 |
|
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: 46.94 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 556 KEMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEakkklelkleeVETWKKQVSAL 635
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-----------ISDLNNQKEQD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 636 WNcksdhEALNTKLSKcveKGKKLKEINEKVSNSRDQLStkvfelklQLNRELETAE-TLKNERKDSAKLRNEVNQLKDQ 714
Cdd:TIGR04523 308 WN-----KELKSELKN---QEKKLEEIQNQISQNNKIIS--------QLNEQISQLKkELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 715 LEREREIAYGLQEEASKLRVGTgKDVKRQIL--ESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNH 792
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQI-NDLESKIQnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 793 TEEgpsNHEDENGSYRKVLwkHQKIKDL---YRKGEQ-----QREAEEMVNKLISLNQHPE---------VQHISFL--- 852
Cdd:TIGR04523 451 VKE---LIIKNLDNTRESL--ETQLKVLsrsINKIKQnleqkQKELKSKEKELKKLNEEKKeleekvkdlTKKISSLkek 525
|
330 340 350
....*....|....*....|....*....|....*
gi 1831510765 853 --ELESFKKQISDYLHTVEKNIQKIKRNDDFTNLE 885
Cdd:TIGR04523 526 ieKLESEKKEKESKISDLEDELNKDDFELKKENLE 560
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
558-847 |
7.11e-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: 46.64 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 558 MKTVQNVLKDVQTQLTTMKHKSEKFEKNMtgsversKKAEQRLQEEKLDHV-------KIQVEAKKKLELKLEEVETWKK 630
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEV-------EDLKTELEKEKLKNIeltahcdKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 631 QVSALWNCKSDHEALNTKLSKCVEKGKKLKEINEKVsnsRDQLSTKVFELKLQLNRELETAETLKNE----RKDSAKLRN 706
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV---REEFIQKGDEVKCKLDKSEENARSIEYEvlkkEKQMKILEN 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 707 EVNQLKDQLEREREIAYGLQEEASKL-RVGTGK-------DVKRQILESENAQLRQE------KQRREMEKSSLLETKMI 772
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALkKKGSAEnkqlnayEIKVNKLELELASAKQKfeeiidNYQKEIEDKKISEEKLL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 773 LSRQN-----EEQHKLiQSLMD---QNHTEEGPSNHEDENGSYRKVLWKHQKIKDLYRKGEQQR---------EAEEMVN 835
Cdd:pfam05483 675 EEVEKakaiaDEAVKL-QKEIDkrcQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQssakaaleiELSNIKA 753
|
330
....*....|..
gi 1831510765 836 KLISLNQHPEVQ 847
Cdd:pfam05483 754 ELLSLKKQLEIE 765
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
557-849 |
1.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 557 EMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEAKKKLELKLEEVETWKKQVSALW 636
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 637 NCKSDHEALNTKLSKCVEKGKKLKEINEKVSNSRDQLSTKVFELKlqlnrelETAETLKNERKDSAKLRNEVNQLKDQLE 716
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-------KKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 717 REREIAYGLQEEASKL-RVGTGKDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEE 795
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831510765 796 GPSNHEDEngsyRKVLWKHQKIKDLYRKGEQQREAEEMVNKLISLNQHPEVQHI 849
Cdd:PTZ00121 1783 EELDEEDE----KRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-889 |
1.31e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 657 KKLKEINEKVSNSRDQLSTKVFELKlQLNRELETAET-LKNERKDSAKLRNEVNQLKDQLEREREIAYGLQEEASKLrvg 735
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELE-QLEEELEELNEqLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 736 tgkDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEEGPSNHEDENGSYRKVLWK-- 813
Cdd:COG4372 128 ---EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELae 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510765 814 -HQKIKDLYRKGEQQREAEEMVNKLISLNQHPEVQHISFLELESFKKQISDYLHTVEKNIQKIKRNDDFTNLEPLPE 889
Cdd:COG4372 205 aEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
556-885 |
6.38e-05 |
|
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: 46.94 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 556 KEMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEakkklelkleeVETWKKQVSAL 635
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-----------ISDLNNQKEQD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 636 WNcksdhEALNTKLSKcveKGKKLKEINEKVSNSRDQLStkvfelklQLNRELETAE-TLKNERKDSAKLRNEVNQLKDQ 714
Cdd:TIGR04523 308 WN-----KELKSELKN---QEKKLEEIQNQISQNNKIIS--------QLNEQISQLKkELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 715 LEREREIAYGLQEEASKLRVGTgKDVKRQIL--ESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNH 792
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQI-NDLESKIQnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 793 TEEgpsNHEDENGSYRKVLwkHQKIKDL---YRKGEQ-----QREAEEMVNKLISLNQHPE---------VQHISFL--- 852
Cdd:TIGR04523 451 VKE---LIIKNLDNTRESL--ETQLKVLsrsINKIKQnleqkQKELKSKEKELKKLNEEKKeleekvkdlTKKISSLkek 525
|
330 340 350
....*....|....*....|....*....|....*
gi 1831510765 853 --ELESFKKQISDYLHTVEKNIQKIKRNDDFTNLE 885
Cdd:TIGR04523 526 ieKLESEKKEKESKISDLEDELNKDDFELKKENLE 560
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
558-847 |
7.11e-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: 46.64 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 558 MKTVQNVLKDVQTQLTTMKHKSEKFEKNMtgsversKKAEQRLQEEKLDHV-------KIQVEAKKKLELKLEEVETWKK 630
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEV-------EDLKTELEKEKLKNIeltahcdKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 631 QVSALWNCKSDHEALNTKLSKCVEKGKKLKEINEKVsnsRDQLSTKVFELKLQLNRELETAETLKNE----RKDSAKLRN 706
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV---REEFIQKGDEVKCKLDKSEENARSIEYEvlkkEKQMKILEN 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 707 EVNQLKDQLEREREIAYGLQEEASKL-RVGTGK-------DVKRQILESENAQLRQE------KQRREMEKSSLLETKMI 772
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALkKKGSAEnkqlnayEIKVNKLELELASAKQKfeeiidNYQKEIEDKKISEEKLL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 773 LSRQN-----EEQHKLiQSLMD---QNHTEEGPSNHEDENGSYRKVLWKHQKIKDLYRKGEQQR---------EAEEMVN 835
Cdd:pfam05483 675 EEVEKakaiaDEAVKL-QKEIDkrcQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQssakaaleiELSNIKA 753
|
330
....*....|..
gi 1831510765 836 KLISLNQHPEVQ 847
Cdd:pfam05483 754 ELLSLKKQLEIE 765
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-795 |
1.03e-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: 46.20 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 555 RKEMKTVQNVLKDVQTQL----TTMKHKSEKFEKNMTGSVERSKKAEQ-------------------RLQEEKLDHVKIQ 611
Cdd:TIGR02168 238 REELEELQEELKEAEEELeeltAELQELEEKLEELRLEVSELEEEIEElqkelyalaneisrleqqkQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 612 VEAKKKLELKLE--------EVETWKKQVSALwncKSDHEALNTKLSKCVEKGKKLKEINEKVSNSRDQLSTKVFELKLQ 683
Cdd:TIGR02168 318 LEELEAQLEELEskldelaeELAELEEKLEEL---KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 684 LNreletaetlknerkdsaKLRNEVNQLKDQLERereiaygLQEEasklrvgtgkdvkRQILESENAQLRQEKQRREMEk 763
Cdd:TIGR02168 395 IA-----------------SLNNEIERLEARLER-------LEDR-------------RERLQQEIEELLKKLEEAELK- 436
|
250 260 270
....*....|....*....|....*....|..
gi 1831510765 764 ssllETKMILSRQNEEQHKLIQSLMDQNHTEE 795
Cdd:TIGR02168 437 ----ELQAELEELEEELEELQEELERLEEALE 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
578-849 |
4.69e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 578 KSEKFEKNMTGSVERSKKAEQRL--QEEKLDHVKIQVEAKKKLelkleeVETWKKQVSALwncKSDHEALNTKLSKCVEK 655
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIeeLEEKIAELEKALAELRKE------LEELEEELEQL---RKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 656 GKKLKEINEKVSNSRDQLSTKVFELKLQ---LNRELETAETLKNERKD-SAKLRNEVNQLKDQLEREREIAYGLQEEASK 731
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAeIEELEAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 732 LRVG-TGKDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQ--------NEEQHKLIQSLMDQNHTEEGPSNHED 802
Cdd:TIGR02168 815 LNEEaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieeleeliEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1831510765 803 ENGSYRKVLWKH-QKIKDLYRKGEQQREA-EEMVNKLISLNQhpEVQHI 849
Cdd:TIGR02168 895 ELEELSEELRELeSKRSELRRELEELREKlAQLELRLEGLEV--RIDNL 941
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-795 |
1.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 592 RSKKAEQRLQEEKLDHVKIQVEAKKKLelkleeVETWKKQVSALwncKSDHEALNTKLSkcvEKGKKLKEINEKVSNSRD 671
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAE------LAELEAELEEL---RLELEELELELE---EAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 672 QLStkvfELKLQLNRELETAETLKNERkdsAKLRNEVNQLKDQLEREREIAYGLQEEASKLRvgtgkdVKRQILESENAQ 751
Cdd:COG1196 303 DIA----RLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAE------AELAEAEEALLE 369
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1831510765 752 LRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEE 795
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
557-849 |
1.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 557 EMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEAKKKLELKLEEVETWKKQVSALW 636
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 637 NCKSDHEALNTKLSKCVEKGKKLKEINEKVSNSRDQLSTKVFELKlqlnrelETAETLKNERKDSAKLRNEVNQLKDQLE 716
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-------KKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 717 REREIAYGLQEEASKL-RVGTGKDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEE 795
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1831510765 796 GPSNHEDEngsyRKVLWKHQKIKDLYRKGEQQREAEEMVNKLISLNQHPEVQHI 849
Cdd:PTZ00121 1783 EELDEEDE----KRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
597-788 |
1.63e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 597 EQRLQEEKLDHVKIQVEakkKLELKLEEVETWKKQVSALWNCKSDHEALNTKLSKCVEKGKKLKEINEKVSNSRDQLSTK 676
Cdd:COG4717 48 LERLEKEADELFKPQGR---KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 677 VF---------ELKLQLNRELETAETLKNERKDSAKLRNEVNQLKDQLEREREIAYGLQEEASKLRVGTGKDVKRQI--L 745
Cdd:COG4717 125 LQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeeL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1831510765 746 ESENAQLRQEKQRREMEKSSL------LETKMILSRQNEEQHKLIQSLM 788
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLLLL 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
625-878 |
2.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 625 VETWKKQvsalwncksdHEALNTKLSKCVEKGKKLKE----INEKVSNSRDQLStkvfELKLQLNRELETAETLKNERKD 700
Cdd:COG1340 38 LKELAEK----------RDELNAQVKELREEAQELREkrdeLNEKVKELKEERD----ELNEKLNELREELDELRKELAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 701 SAKLRNEVNQLKDQLEREReiayglqeeasklrvgtgkdvKRQilesENAQLRQEKQRREMEKSSLLETKMILSRQNEEQ 780
Cdd:COG1340 104 LNKAGGSIDKLRKEIERLE---------------------WRQ----QTEVLSPEEEKELVEKIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 781 HKLIQSLMDQNHT--EEGPSNHEDENGSYRKVLWKHQKIKDLYRKGEQQR-EAEEMVNKLISLNQHPEVQHISFLELESF 857
Cdd:COG1340 159 NEKLKELRAELKElrKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRkEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260
....*....|....*....|.
gi 1831510765 858 KKQISDYLHTVEKNIQKIKRN 878
Cdd:COG1340 239 LRELRKELKKLRKKQRALKRE 259
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
546-875 |
2.77e-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: 41.49 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 546 ANCTDCSGVRKEMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEakkklelkLEEV 625
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--------TVRL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 626 ETWKKQVSALwncksdhealntKLSKCVEKGKKLKEINEKVSNSRDQLSTKVF--ELKLQLNRELETAETLKNERKDSAK 703
Cdd:TIGR00618 597 QDLTEKLSEA------------EDMLACEQHALLRKLQPEQDLQDVRLHLQQCsqELALKLTALHALQLTLTQERVREHA 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 704 LRNEVNQLKDQLEREREiaygLQEEASKLRVGTGkdvKRQILESENAQLRQEKQ-----RREMEKSSLLETKMI--LSRQ 776
Cdd:TIGR00618 665 LSIRVLPKELLASRQLA----LQKMQSEKEQLTY---WKEMLAQCQTLLRELEThieeyDREFNEIENASSSLGsdLAAR 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 777 NEEQHKLIQSLMDQNHTEEGPSNHEDENGSYRKV--LWKHQKIKDLYRKGE-QQREAEEMVNKLISL----NQH-PEVQH 848
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTaaLQTGAELSHLAAEIQfFNRLREEDTHLLKTLeaeiGQEiPSDED 817
|
330 340
....*....|....*....|....*..
gi 1831510765 849 ISFLELESFKKQISDYLHTVEKNIQKI 875
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATL 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
554-790 |
3.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 554 VRKEMKTVQNVLKDVQTQLTTMKHKSEKFEK--NMTGSVERSKKAEQRLQEEKLDHVKiqvEAKKKLELKLEEVETWKKQ 631
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 632 VSALwncKSDHEALNTKLSKCVEKGKKLKEINEKVSNSRDQLSTKVFELKLQLNRELETAE-------TLKNERKDSAKL 704
Cdd:PRK03918 541 IKSL---KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylELKDAEKELERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 705 RNEVNQLKDQLEREREIAYGLQEEASKLRvGTGKDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLI 784
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELR-KELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
....*.
gi 1831510765 785 QSLMDQ 790
Cdd:PRK03918 697 EKLKEE 702
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
556-779 |
3.12e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 556 KEMKTVQNVLKDVQTQLTTMK----------HKSEKFEKNMTG----------SVERSKKAEQRLQEEKLDHVKIQVEAK 615
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARasrdeilaqsKESEKKLKNLEAellqlqedlaASERARRQAQQERDELADEIASGASGK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 616 KKLELKLEEVETWKKQVSA-LWNCKSDHEALNTKLSKCVEKGKKL-------KEINEKVSNSRDQLSTKVFELKLQLnRE 687
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEeLEEEQSNTELLNDRLRKSTLQVEQLttelaaeRSTSQKSESARQQLERQNKELKAKL-QE 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 688 LETaeTLKNERKDS-AKLRNEVNQLKDQLERE-REiayglQEEASKLRVGTGKDVKRQILESENAQLRQEKQRREMEKSS 765
Cdd:pfam01576 957 MEG--TVKSKFKSSiAALEAKIAQLEEQLEQEsRE-----RQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGN 1029
|
250
....*....|....
gi 1831510765 766 LLETKmiLSRQNEE 779
Cdd:pfam01576 1030 SRMKQ--LKRQLEE 1041
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
646-766 |
4.41e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.84 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 646 NTKLSKCVEKGKKLKEINEKVSNSRDQLSTKVFELKLQLNRELET----AETLKNERKDSAKLRNEVNQLKDQLER-ERE 720
Cdd:pfam11559 9 QTLLSRGFLRSGLLFDTAEGVEENIARIINVIYELLQQRDRDLEFreslNETIRTLEAEIERLQSKIERLKTQLEDlERE 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510765 721 IAYGLQEEAS---KLRVGTGK------DVKRQ--ILESENAQLRQEKQRREMEKSSL 766
Cdd:pfam11559 89 LALLQAKERQlekKLKTLEQKlknekeELQRLknALQQIKTQFAHEVKKRDREIEKL 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
555-796 |
8.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 555 RKEMKTVQNVLKDVQTQLTTMKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQveakkklelkleevetwkkqvsa 634
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE----------------------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 635 lwnckSDHEALNTKLSkcvEKGKKLKEINEKVSNSRDQLSTKVFELKLQLNRELETAETLKNERKDSAKLRNEVNQLKDQ 714
Cdd:COG1196 330 -----EELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 715 LEREREIAYGLQEEASKLRvgtgkDVKRQILESENAQLRQEKQRREMEKSSLLEtkmiLSRQNEEQHKLIQSLMDQNHTE 794
Cdd:COG1196 402 LEELEEAEEALLERLERLE-----EELEELEEALAELEEEEEEEEEALEEAAEE----EAELEEEEEALLELLAELLEEA 472
|
..
gi 1831510765 795 EG 796
Cdd:COG1196 473 AL 474
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
575-879 |
8.46e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 575 MKHKSEKFEKNMTGSVERSKKAEQRLQEEKLDHVKIQVEAKKKLELKLEEVETWKKQVSALWNCKSDHEAlntklskcve 654
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE---------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 655 kgKKLKEINEKVSNSRDQLSTKVFELKlqlnRELETAETLKNERKDSAKLRNEVNQLKDQLEREREIaygLQEEASKLRV 734
Cdd:pfam02463 237 --ERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE---LKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510765 735 GTGKDVKRQILESENAQLRQEKQRREMEKSSLLETKMILSRQNEEQHKLIQSLMDQNHTEEgpSNHEDENGSYRKVLWKH 814
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL--EQLEEELLAKKKLESER 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510765 815 QKiKDLYRKGEQQREAEEMVNKLISLNQHPEVQhisFLELESFKKQISDYLHTVEKNIQKIKRND 879
Cdd:pfam02463 386 LS-SAAKLKEEELELKSEEEKEAQLLLELARQL---EDLLKEEKKEELEILEEEEESIELKQGKL 446
|
|
| |
