|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
2637-2837 |
2.77e-105 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 335.11 E-value: 2.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2637 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2716
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2717 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2796
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779438 2797 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2837
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2635-2841 |
2.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2635 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2710
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2711 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2785
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779438 2786 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2841
Cdd:PRK03918 341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2641-2838 |
7.47e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADL 2720
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2721 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2800
Cdd:COG1196 326 AELEEELEEL---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039779438 2801 YQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2838
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2665-2840 |
1.46e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2665 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 2744
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2745 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 2824
Cdd:COG4717 145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170
....*....|....*.
gi 1039779438 2825 EIEELTKICDELIAKM 2840
Cdd:COG4717 221 ELEELEEELEQLENEL 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2641-2839 |
1.55e-06 |
|
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: 54.29 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2720
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2721 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2800
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779438 2801 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2839
Cdd:TIGR02168 844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2646-2829 |
6.59e-06 |
|
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: 51.98 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2646 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 2719
Cdd:TIGR02168 207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2720 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqa 2799
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------ 359
|
170 180 190
....*....|....*....|....*....|
gi 1039779438 2800 ayqasLRKEQLRVDALERTLEQKNKEIEEL 2829
Cdd:TIGR02168 360 -----LEELEAELEELESRLEELEEQLETL 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2641-2839 |
7.00e-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: 51.30 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD- 2719
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2720 ----------------LNSveKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRA 2783
Cdd:COG4942 110 lralyrlgrqpplallLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779438 2784 NAEIAQVRGKAQQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2839
Cdd:COG4942 187 RAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2642-2838 |
7.89e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2642 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIEDEQREKSISHQTVQ 2707
Cdd:PRK03918 471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2708 QLVLEKEQALAD--LNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK 2773
Cdd:PRK03918 551 LEELKKKLAELEkkLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779438 2774 ---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2838
Cdd:PRK03918 626 eelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2641-2839 |
1.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQALA 2718
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2719 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2798
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779438 2799 AAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2839
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2635-2837 |
1.16e-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: 51.22 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2635 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLE 2712
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2713 KEQALADLN--SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqv 2790
Cdd:TIGR02169 308 RSIAEKEREleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE---- 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779438 2791 rgkaqqeqaayqasLRKEQlrvDALERTLEQKNKEIEELTKICDELI 2837
Cdd:TIGR02169 383 --------------TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2646-2839 |
1.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2646 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMiEDEQreksishQTvQQLVLEKEQALadlnsVEK 2725
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2726 sLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaayqaSL 2805
Cdd:COG1340 142 -IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------EL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779438 2806 RKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2839
Cdd:COG1340 208 RKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2648-2838 |
1.32e-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: 51.22 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2648 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 2713
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2714 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 2792
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779438 2793 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2838
Cdd:TIGR02169 309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2631-2821 |
2.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2631 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaQMIEDEQREKSISHQTVQ 2707
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2708 -QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLKKCAQEYLSRVKKEEQRYQAL---KVHAEEKLDR 2782
Cdd:COG4717 144 lPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELqqrLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779438 2783 ANAEIAQVRGKAQQEqaayqaslrKEQLRVDALERTLEQ 2821
Cdd:COG4717 218 AQEELEELEEELEQL---------ENELEAAALEERLKE 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2655-2839 |
2.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2655 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 2732
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2733 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 2811
Cdd:PTZ00121 1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619
|
170 180
....*....|....*....|....*....
gi 1039779438 2812 VDALE-RTLEQKNKEIEELTKICDELIAK 2839
Cdd:PTZ00121 1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2638-2822 |
3.35e-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: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2638 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM--IEDEQREKSISHQT-VQQLVLEKE 2714
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesRLEELEEQLETLRSkVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2715 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgk 2793
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-- 474
|
170 180
....*....|....*....|....*....
gi 1039779438 2794 aqQEQAAYQASLRKEQLRVDALERTLEQK 2822
Cdd:TIGR02168 475 --QALDAAERELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2656-2831 |
3.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2656 KEREVSEwrdkYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FR 2732
Cdd:PRK03918 271 LKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2733 RYEKMKEVLEGFRKNEEVLKKCAQEY---------LSRVKKEEQRYQALKVHAE-EKLDRANAEIaqvrgkaqqeqaayQ 2802
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEKLEKElEELEKAKEEI--------------E 404
|
170 180
....*....|....*....|....*....
gi 1039779438 2803 ASLRKEQLRVDALERTLEQKNKEIEELTK 2831
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2643-2831 |
3.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2643 DSALQVARAEVI--AKEREVSEWRDKYEESRREVVE-MRKivAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQalad 2719
Cdd:PTZ00121 1575 DKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEeAKK--AEEAKIKAEELKKAEEEK----KKVEQLKKKEAE---- 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2720 lnsvEKSLADLFRRYEKMKEV-LEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVRgKAQQEQ 2798
Cdd:PTZ00121 1645 ----EKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELK-KKEAEE 1714
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779438 2799 AAYQASLRKEQ----LRVDALERTLEQKNKEIEELTK 2831
Cdd:PTZ00121 1715 KKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2650-2836 |
5.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2650 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 2723
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2724 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKE------------EQRYQALKVHAEEKLDRANAEiaqvr 2791
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDE-LEEELAELLKEleelgfesveelEERLKELEPFYNEYLELKDAE----- 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779438 2792 gkaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 2836
Cdd:PRK03918 612 ----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2636-2831 |
6.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2636 LFQQPDLDSALQVARAEviaKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQ 2715
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2716 A--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-- 2791
Cdd:PTZ00121 1677 AeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDee 1754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779438 2792 -----GKAQQEQAAYQASLRKEQLRV--DALERTLEQKNKEIEELTK 2831
Cdd:PTZ00121 1755 ekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2656-2836 |
9.55e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2656 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2735
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2736 KMKEVLEGFRKNEEVLKK-------CAQEY--------LSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2800
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKakgkcpvCGRELteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779438 2801 YQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 2836
Cdd:PRK03918 496 IKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2649-2831 |
9.60e-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: 48.13 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2649 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 2725
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2726 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 2802
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190
....*....|....*....|....*....|..
gi 1039779438 2803 ASLRK---EQLRVDALERTLEQKNKEIEELTK 2831
Cdd:TIGR02168 828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2668-2831 |
1.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2668 EESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2747
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2748 EEVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLrvDALERTLEQKNKEIE 2827
Cdd:COG4372 110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEEL--KELEEQLESLQEELA 167
|
....
gi 1039779438 2828 ELTK 2831
Cdd:COG4372 168 ALEQ 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2657-2842 |
1.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2657 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM-------------IEDEQRE----------KSIShQTVQQLVLEK 2713
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEHRKelleeytaelKRIE-KELKEIEEKE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2714 EQALADLNSVEKSLADLfRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEeqrYQALKvhaeEKLDRANAEIaqvrgk 2793
Cdd:PRK03918 476 RKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLK----EKLIKLKGEI------ 541
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779438 2794 aqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2842
Cdd:PRK03918 542 ---------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
2053-2164 |
2.55e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 45.89 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2053 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2125
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039779438 2126 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2164
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2646-2787 |
2.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2646 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI--VAEYEKtiaqmIEDEQREKSISHQTVQQlvlEKEQALADLNSV 2723
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779438 2724 EKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2787
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2650-2842 |
2.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2650 RAEVIAkerEVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE------DEQREKSISHQTVQQLVLEKEQALADLNSV 2723
Cdd:COG1340 31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2724 EKSLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE---------- 2777
Cdd:COG1340 108 GGSIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikela 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779438 2778 EKLDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2842
Cdd:COG1340 188 EEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1748-2120 |
3.08e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 1748 PPEPDESKDEKLHLVAPEELLSDRK-------SPGPGPATLPSVPEACVPKGFPAEARDLGGVESIPGTDDVIQPAAPVD 1820
Cdd:PHA03307 79 APANESRSTPTWSLSTLAPASPAREgsptppgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 1821 PGHPP--LADSSHHGDAVSSVSTHLTVQSASPSAARASPAPLAPEHTASAPSA-AGPGVEVTPTASPQHLAKNEPRSSDS 1897
Cdd:PHA03307 159 PAAVAsdAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpISASASSPAPAPGRSAADDAGASSSD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 1898 EEAFETPESTTPVKAPPAPPPpppevtpepevidPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDK 1977
Cdd:PHA03307 239 SSSSESSGCGWGPENECPLPR-------------PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 1978 PIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTESVPPSKStLSRSLSLQaSDFDGASCPGSPEAGTL 2057
Cdd:PHA03307 306 GPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAAVSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRP 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779438 2058 TTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQQEPGEESPVPSEEHLAP 2120
Cdd:PHA03307 372 SRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2645-2829 |
3.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2645 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI----------------VAEYEKTIAQmIEDEQREKSISHQTVQQ 2708
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2709 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2788
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779438 2789 QvrgkaqqeqaayqaSLRKeqlRVDALERTLEQKNKEIEEL 2829
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2641-2791 |
5.77e-04 |
|
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: 45.83 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQAL 2717
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLS 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779438 2718 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2791
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2636-2828 |
1.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2636 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM----------IEDEQREKSISHQT 2705
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAqaelaqaqeeLESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2706 VQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLkkcaQEYLSRVKKEEQRYqaLKVHAEEKLDRANA 2785
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL----QEELAALEQELQAL--SEAEAEQALDELLK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779438 2786 EIAqvRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 2828
Cdd:COG4372 191 EAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2647-2828 |
2.35e-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: 42.98 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2647 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQ---MIEDEQREKSISHQTVQQLVL----------- 2711
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdeka 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2712 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2783
Cdd:pfam13868 202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039779438 2784 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2828
Cdd:pfam13868 280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2628-2837 |
2.40e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2628 EVEKppgllfQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQR--EKSISHQT 2705
Cdd:PRK04778 307 YVEK------NSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2706 VQqlvlekeqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLS-------RVKKEE-----QRYQALK 2773
Cdd:PRK04778 381 LQ----------EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMF 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779438 2774 VHAEEKLDRANAEIAQVRgkaqqeqaayqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2837
Cdd:PRK04778 451 FEVSDEIEALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2659-2831 |
2.84e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2659 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMK 2738
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2739 EVLEG-FRKNEEV-------LKKCAQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA----------QVRGKAQQEQAA 2800
Cdd:TIGR04523 394 NDLESkIQNQEKLnqqkdeqIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKV 472
|
170 180 190
....*....|....*....|....*....|.
gi 1039779438 2801 YQASLRKEQLRVDALERTLEQKNKEIEELTK 2831
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2641-2839 |
3.00e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREV---------SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVL 2711
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKkkadeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2712 EKEQALAD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEI 2787
Cdd:PTZ00121 1362 AEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKA 1440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779438 2788 AQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2839
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
2680-2829 |
4.31e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2680 IVAEYEKTIAQMiedeqrEKSISHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKK 2753
Cdd:pfam13851 2 LMKNHEKAFNEI------KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2754 CAQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQ 2809
Cdd:pfam13851 76 QLENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNL 145
|
170 180
....*....|....*....|...
gi 1039779438 2810 L---RVDALERTLEQKNKEIEEL 2829
Cdd:pfam13851 146 LlekKLQALGETLEKKEAQLNEV 168
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2649-2789 |
4.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2649 ARAEVIAKEREVsEWRDKYEESR----REVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVE 2724
Cdd:PRK12704 49 KEAEAIKKEALL-EAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779438 2725 KSLADLFRRYEKMKEVLE---GFRKNE-------EVLKKCAQEYLSRVKKEEQRyqalkvhAEEKLDR-ANAEIAQ 2789
Cdd:PRK12704 128 KKEEELEELIEEQLQELErisGLTAEEakeilleKVEEEARHEAAVLIKEIEEE-------AKEEADKkAKEILAQ 196
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2661-2839 |
4.68e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2661 SEWRDKYEESRREVVEMRKIVAEyEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsVEKSLADLFRRYEKMKev 2740
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNKDD-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2741 legFRKNEEVLKKCAQEYLSRVKKEEQRYQALKV---HAEEKLDRANAEIAQVR------GKAQQEQAAYQASLRKEQLR 2811
Cdd:TIGR04523 552 ---FELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKENEK 628
|
170 180 190
....*....|....*....|....*....|..
gi 1039779438 2812 VDALERTLEQK----NKEIEELTKICDELIAK 2839
Cdd:TIGR04523 629 LSSIIKNIKSKknklKQEVKQIKETIKEIRNK 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2645-2836 |
5.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2645 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE-DEQREKSISHQTVQQLVLEKEQALADLNSV 2723
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2724 EKSlADLFRRYEKMKEVLEGFRKNEEVLKKCAQ----EYLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRGKAQQE 2797
Cdd:PTZ00121 1424 KKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEA 1502
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779438 2798 QAAYQASLRKEQLRvDALERTLEQKNKEIEELTKiCDEL 2836
Cdd:PTZ00121 1503 KKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK-ADEA 1539
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2641-2840 |
5.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2641 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektiaqmIEDEQREKSISHQTVQQLVLEKEQALA-- 2718
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2719 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkkcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2794
Cdd:COG1579 86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779438 2795 QQeqaayqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2840
Cdd:COG1579 134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2650-2835 |
5.91e-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: 42.27 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2650 RAEVIAKEREVsewrdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTV--QQLVLEKEQALADLNSVEKSL 2727
Cdd:pfam02463 185 LAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2728 ADLFRRYEKMKEVLEGFRKNEEVLK-----------KCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKA 2794
Cdd:pfam02463 258 QEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779438 2795 QQEQAAYQASLRKEQL----RVDALERTLEQKNKEIEELTKICDE 2835
Cdd:pfam02463 338 EELEKELKELEIKREAeeeeEEELEKLQEKLEQLEEELLAKKKLE 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2706-2830 |
6.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2706 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2778
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1039779438 2779 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2830
Cdd:COG4913 289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2650-2828 |
6.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2650 RAEVIAKER-EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLA 2728
Cdd:PRK01156 347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2729 DLFRRYEKMKEVLEGFRKNEEVLK---KC-------AQEYLSRVKKEeqrYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2798
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMEMLNgqsVCpvcgttlGEEKSNHIINH---YNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
170 180 190
....*....|....*....|....*....|
gi 1039779438 2799 AAYQASLRKEQLRVDALERTLEQKNKEIEE 2828
Cdd:PRK01156 504 KRKEYLESEEINKSINEYNKIESARADLED 533
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2700-2842 |
7.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2700 SISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEgfRKNEEVLKkcAQEYLSRVKKEEQRYQALKVHAEEK 2779
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--QARSELEQ--LEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779438 2780 LDRANAEIAQVRGKAQQEQAAYQA-SLRKEQL--RVDALERTLEQKNKEIEELTKICDELIAKMGK 2842
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDlEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2642-2836 |
7.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2642 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 2720
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2721 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2797
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779438 2798 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2836
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2735-2839 |
9.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779438 2735 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 2811
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1039779438 2812 VDALERTLEQKNKEIEELTKICDELIAK 2839
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
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