|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
2677-2877 |
1.25e-104 |
|
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: 333.57 E-value: 1.25e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2677 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2756
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2757 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2836
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907182994 2837 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2877
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2602-2878 |
3.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2602 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2681
Cdd:COG1196 212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2682 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADLN 2761
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2762 SVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAY 2841
Cdd:COG1196 327 ELEEELEEL---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907182994 2842 QASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2878
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2675-2881 |
4.27e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2675 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2750
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2751 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2825
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182994 2826 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2881
Cdd:PRK03918 341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2621-2871 |
1.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2621 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIgsTEVEKppglLFQQPDLDSALQVARAEviaKEREV 2700
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMK----LYEEEKKMKAEEAKKAE---EAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2701 SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMK 2778
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2779 EVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAYQASLRKEQLR 2851
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEA 1779
|
250 260
....*....|....*....|..
gi 1907182994 2852 V--DALERTLEQKNKEIEELTK 2871
Cdd:PTZ00121 1780 VieEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2681-2879 |
1.83e-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: 53.91 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2681 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2760
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2761 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2840
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907182994 2841 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2879
Cdd:TIGR02168 844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2705-2880 |
2.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2705 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 2784
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2785 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 2864
Cdd:COG4717 145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170
....*....|....*.
gi 1907182994 2865 EIEELTKICDELIAKM 2880
Cdd:COG4717 221 ELEELEEELEQLENEL 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2611-2868 |
4.06e-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: 52.76 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2611 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 2690
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2691 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLEKEQALADLN--SVEKS 2766
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLERSIAEKEREleDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2767 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEE---KLDRANAEIAQVRgKAQQEQAAYQA 2843
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYR-EKLEKLKREIN 402
|
250 260
....*....|....*....|....*
gi 1907182994 2844 SLRKEQLRVDALERTLEQKNKEIEE 2868
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNA 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2686-2869 |
8.46e-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: 51.60 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2686 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 2759
Cdd:TIGR02168 207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2760 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqa 2839
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------ 359
|
170 180 190
....*....|....*....|....*....|
gi 1907182994 2840 ayqasLRKEQLRVDALERTLEQKNKEIEEL 2869
Cdd:TIGR02168 360 -----LEELEAELEELESRLEELEEQLETL 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2681-2879 |
9.72e-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: 50.53 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2681 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADL 2760
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2761 NSV---------------EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANA 2825
Cdd:COG4942 110 LRAlyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907182994 2826 EIAQVRGKAQQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2879
Cdd:COG4942 189 ALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2682-2878 |
1.29e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2682 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIEDEQREKSISHQTVQ 2747
Cdd:PRK03918 471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2748 QLVLEKEQALAD--LNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK 2813
Cdd:PRK03918 551 LEELKKKLAELEkkLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907182994 2814 ---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2878
Cdd:PRK03918 626 eelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2681-2879 |
1.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2681 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQALA 2758
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2759 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2838
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907182994 2839 AAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2879
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2688-2878 |
1.66e-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: 50.84 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2688 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 2753
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2754 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 2832
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907182994 2833 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2878
Cdd:TIGR02169 309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2686-2879 |
2.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2686 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMiEDEQreksishQTvQQLVLEKEQALadlnsVEK 2765
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2766 sLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaayqaSL 2845
Cdd:COG1340 142 -IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------EL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907182994 2846 RKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2879
Cdd:COG1340 208 RKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2610-2862 |
2.78e-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: 50.06 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2610 AQKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisktalysrigSTEVEKppglLFQQPDLDS---AL 2686
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEEL-----------------EAQLEE----LESKLDELAeelAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2687 QVARAEVIAKEREvsEWRDKYEESRREVVEMRKIVAEYEKTIaqmieDEQREKsishqtVQQLVLEKEQALADLNSVEKS 2766
Cdd:TIGR02168 342 LEEKLEELKEELE--SLEAELEELEAELEELESRLEELEEQL-----ETLRSK------VAQLELQIASLNNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2767 LADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgkaqQEQAAYQASL 2845
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE----QALDAAEREL 484
|
250
....*....|....*..
gi 1907182994 2846 RKEQLRVDALERTLEQK 2862
Cdd:TIGR02168 485 AQLQARLDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2695-2879 |
3.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2695 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 2772
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2773 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 2851
Cdd:PTZ00121 1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619
|
170 180
....*....|....*....|....*....
gi 1907182994 2852 VDALE-RTLEQKNKEIEELTKICDELIAK 2879
Cdd:PTZ00121 1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2671-2851 |
4.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2671 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaQMIEDEQREKSISHQTVQ 2747
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2748 -QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLKKCAQEYLSRVKKEEQRYQAL---KVHAEEKLDR 2822
Cdd:COG4717 144 lPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELqqrLAELEEELEE 217
|
170 180
....*....|....*....|....*....
gi 1907182994 2823 ANAEIAQVRGKAQQEQAAYQASLRKEQLR 2851
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLK 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2696-2871 |
5.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2696 KEREVSEwrdkYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FR 2772
Cdd:PRK03918 271 LKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2773 RYEKMKEVLEGFRKNEEVLKKCAQEY---------LSRVKKEEQRYQALKVHAE-EKLDRANAEIaqvrgkaqqeqaayQ 2842
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEKLEKElEELEKAKEEI--------------E 404
|
170 180
....*....|....*....|....*....
gi 1907182994 2843 ASLRKEQLRVDALERTLEQKNKEIEELTK 2871
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2611-2879 |
5.64e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2611 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYSRigSTEVEkppgllfqqpDLDSALQVAR 2690
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELEEL--ELELE----------EAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2691 AEVIAKEREVSEWRdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShQTVQQLVLEKEQALADLNSVEKSLADL 2770
Cdd:COG1196 295 AELARLEQDIARLE---ERRRELEERLEELEEELAELEEELEELEEELEELE-EELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2771 FRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASLRKE 2848
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEAAEE 450
|
250 260 270
....*....|....*....|....*....|.
gi 1907182994 2849 QLRVDALERTLEQKNKEIEELTKICDELIAK 2879
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2690-2876 |
6.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2690 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 2763
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2764 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKE------------EQRYQALKVHAEEKLDRANAEiaqvr 2831
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDE-LEEELAELLKEleelgfesveelEERLKELEPFYNEYLELKDAE----- 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907182994 2832 gkaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 2876
Cdd:PRK03918 612 ----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2689-2871 |
1.23e-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: 47.74 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2689 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 2765
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2766 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 2842
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190
....*....|....*....|....*....|..
gi 1907182994 2843 ASLRK---EQLRVDALERTLEQKNKEIEELTK 2871
Cdd:TIGR02168 828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2696-2876 |
1.31e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2696 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2775
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2776 KMKEVLEGFRKNEEVLKK-------CAQEY--------LSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2840
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKakgkcpvCGRELteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907182994 2841 YQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 2876
Cdd:PRK03918 496 IKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2613-2831 |
2.01e-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: 47.37 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2613 LQEELEFAVMRIEALKlaRQIALASRSRQDTKREAAHppdvsisktaLYSRIGSTEVEKPpgllfqqpDLDSALQVARAE 2692
Cdd:TIGR02169 292 VKEKIGELEAEIASLE--RSIAEKERELEDAEERLAK----------LEAEIDKLLAEIE--------ELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2693 VIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLAD 2769
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907182994 2770 LFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2831
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
2011-2122 |
2.29e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 46.27 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2011 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2083
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907182994 2084 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2122
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2612-2882 |
2.74e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2612 KLQEELEFAVMRIE--ALKLARQIALASRSRQDTKREAAHPPDvsisktalysrigstEVEKppgllfqqpDLDSaLQVA 2689
Cdd:PRK03918 345 KKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPE---------------KLEK---------ELEE-LEKA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2690 RAEViakEREVSEWRDKYEESRREVVEMRKIVAEYEK------TIAQMIEDEQRE----------KSIShQTVQQLVLEK 2753
Cdd:PRK03918 400 KEEI---EEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKelleeytaelKRIE-KELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2754 EQALADLNSVEKSLADLfRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEeqrYQALKvhaeEKLDRANAEIaqvrgk 2833
Cdd:PRK03918 476 RKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLK----EKLIKLKGEI------ 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907182994 2834 aqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2882
Cdd:PRK03918 542 ---------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2708-2871 |
3.30e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2708 EESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2787
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2788 EEVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLrvDALERTLEQKNKEIE 2867
Cdd:COG4372 110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEEL--KELEEQLESLQEELA 167
|
....
gi 1907182994 2868 ELTK 2871
Cdd:COG4372 168 ALEQ 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2685-2869 |
4.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2685 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI----------------VAEYEKTIAQmIEDEQREKSISHQTVQQ 2748
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2749 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2828
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907182994 2829 QvrgkaqqeqaayqaSLRKeqlRVDALERTLEQKNKEIEEL 2869
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2686-2827 |
4.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2686 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI--VAEYEKtiaqmIEDEQREKSISHQTVQQlvlEKEQALADLNSV 2763
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182994 2764 EKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2827
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2690-2882 |
5.04e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2690 RAEVIAkerEVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE------DEQREKSISHQTVQQLVLEKEQALADLNSV 2763
Cdd:COG1340 31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2764 EKSLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE---------- 2817
Cdd:COG1340 108 GGSIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikela 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907182994 2818 EKLDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2882
Cdd:COG1340 188 EEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2676-2868 |
2.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2676 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektIAQMIEDEQREKSISHQTVQQLVLEKEQ 2755
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----LNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2756 ALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEIAQV---- 2830
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELlkea 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907182994 2831 -RGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 2868
Cdd:COG4372 193 nRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2595-2877 |
2.50e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2595 GYlepDLAEKNPPVFAQKLQEELEFAVMRIEALKLARqialASRSRQDTKREaahppdvsisKTALYSRIgSTEVEKPPG 2674
Cdd:PRK04778 246 GY---HLDHLDIEKEIQDLKEQIDENLALLEELDLDE----AEEKNEEIQER----------IDQLYDIL-EREVKARKY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2675 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQR--EKSISHQTVQqlvle 2752
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSELQ----- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2753 keqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLS-------RVKKEE-----QRYQALKVHAEEKL 2820
Cdd:PRK04778 383 -----EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMFFEVSDEI 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907182994 2821 DRANAEIAQVRgkaqqeqaayqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2877
Cdd:PRK04778 458 EALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2699-2871 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2699 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMK 2778
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2779 EVLEG-FRKNEEV-------LKKCAQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA----------QVRGKAQQEQAA 2840
Cdd:TIGR04523 394 NDLESkIQNQEKLnqqkdeqIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKV 472
|
170 180 190
....*....|....*....|....*....|.
gi 1907182994 2841 YQASLRKEQLRVDALERTLEQKNKEIEELTK 2871
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2681-2879 |
4.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2681 DLDSALQVARAEVIAKEREV---------SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVL 2751
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKkkadeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2752 EKEQALAD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEI 2827
Cdd:PTZ00121 1362 AEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKA 1440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907182994 2828 AQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2879
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2615-2868 |
4.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2615 EELEFAVMRIEALKLARQIalaSRSRQDTKREAAHPPDVSiSKTALYSRIGSTEVEKPPGL-LFQQPDLDSALQVARAEV 2693
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREV---ERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELeRIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2694 IAKEREVSEWRDKYEESRREVVEmrKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsvEKSLADLFRR 2773
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNE--RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ--------EEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2774 YEKMKEvLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKlDRANAEiAQVRGKAQQEQAAYQASLRKEQLRVD 2853
Cdd:pfam17380 440 LEEERA-REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR-DRKRAE-EQRRKILEKELEERKQAMIEEERKRK 516
|
250
....*....|....*
gi 1907182994 2854 ALERTLEQKNKEIEE 2868
Cdd:pfam17380 517 LLEKEMEERQKAIYE 531
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2689-2829 |
5.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2689 ARAEVIAKEREVsEWRDKYEESR----REVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVE 2764
Cdd:PRK12704 49 KEAEAIKKEALL-EAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907182994 2765 KSLADLFRRYEKMKEVLE---GFRKNE-------EVLKKCAQEYLSRVKKEEQRyqalkvhAEEKLDR-ANAEIAQ 2829
Cdd:PRK12704 128 KKEEELEELIEEQLQELErisGLTAEEakeilleKVEEEARHEAAVLIKEIEEE-------AKEEADKkAKEILAQ 196
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
2720-2869 |
5.31e-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: 40.66 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2720 IVAEYEKTIAQMiedeqrEKSISHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKK 2793
Cdd:pfam13851 2 LMKNHEKAFNEI------KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2794 CAQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQ 2849
Cdd:pfam13851 76 QLENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNL 145
|
170 180
....*....|....*....|...
gi 1907182994 2850 L---RVDALERTLEQKNKEIEEL 2869
Cdd:pfam13851 146 LlekKLQALGETLEKKEAQLNEV 168
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2687-2868 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2687 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQ---MIEDEQREKSISHQTVQQLVL----------- 2751
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdeka 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2752 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2823
Cdd:pfam13868 202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907182994 2824 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2868
Cdd:pfam13868 280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2701-2879 |
6.17e-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: 42.31 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2701 SEWRDKYEESRREVVEMRKIVAEyEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsVEKSLADLFRRYEKMKev 2780
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNKDD-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2781 legFRKNEEVLKKCAQEYLSRVKKEEQRYQALKV---HAEEKLDRANAEIAQVR------GKAQQEQAAYQASLRKEQLR 2851
Cdd:TIGR04523 552 ---FELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKENEK 628
|
170 180 190
....*....|....*....|....*....|..
gi 1907182994 2852 VDALERTLEQK----NKEIEELTKICDELIAK 2879
Cdd:TIGR04523 629 LSSIIKNIKSKknklKQEVKQIKETIKEIRNK 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2685-2876 |
6.93e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2685 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE-DEQREKSISHQTVQQLVLEKEQALADLNSV 2763
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2764 EKSlADLFRRYEKMKEVLEGFRKNEEVLKKCAQ----EYLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRGKAQQE 2837
Cdd:PTZ00121 1424 KKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEA 1502
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907182994 2838 QAAYQASLRKEQLRvDALERTLEQKNKEIEELTKiCDEL 2876
Cdd:PTZ00121 1503 KKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK-ADEA 1539
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2690-2868 |
6.98e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2690 RAEVIAKER-EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLA 2768
Cdd:PRK01156 347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2769 DLFRRYEKMKEVLEGFRKNEEVLK---KC-------AQEYLSRVKKEeqrYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2838
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMEMLNgqsVCpvcgttlGEEKSNHIINH---YNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
170 180 190
....*....|....*....|....*....|
gi 1907182994 2839 AAYQASLRKEQLRVDALERTLEQKNKEIEE 2868
Cdd:PRK01156 504 KRKEYLESEEINKSINEYNKIESARADLED 533
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2746-2870 |
7.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2746 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2818
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907182994 2819 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2870
Cdd:COG4913 289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2690-2875 |
8.40e-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: 41.88 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2690 RAEVIAKEREVsewrdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTV--QQLVLEKEQALADLNSVEKSL 2767
Cdd:pfam02463 185 LAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2768 ADLFRRYEKMKEVLEGFRKNEEVLK-----------KCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKA 2834
Cdd:pfam02463 258 QEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907182994 2835 QQEQAAYQASLRKEQL----RVDALERTLEQKNKEIEELTKICDE 2875
Cdd:pfam02463 338 EELEKELKELEIKREAeeeeEEELEKLQEKLEQLEEELLAKKKLE 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2681-2880 |
9.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2681 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektiaqmIEDEQREKSISHQTVQQLVLEKEQALA-- 2758
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2759 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkkcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2834
Cdd:COG1579 86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907182994 2835 QQeqaayqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2880
Cdd:COG1579 134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2682-2876 |
9.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2682 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 2760
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907182994 2761 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2837
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907182994 2838 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2876
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| |
