|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
2700-2903 |
3.87e-103 |
|
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: 329.33 E-value: 3.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2700 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 2779
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2780 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 2859
Cdd:pfam05010 78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779410 2860 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2903
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2625-2905 |
3.35e-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: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2625 AEKnppvfAQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpd 2704
Cdd:COG1196 212 AER-----YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE---------------------------------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2705 LDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALA 2784
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2785 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2864
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039779410 2865 AAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2905
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2698-2907 |
4.73e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2698 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 2774
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2775 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 2851
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779410 2852 --------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2907
Cdd:PRK03918 339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2644-2897 |
9.38e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2644 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIGSTEVEKPPGLLFQQPDLDSALQV-ARAEVIAKERE 2722
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2723 ----VSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFR 2798
Cdd:PTZ00121 1631 ekkkVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2799 RYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVrgKAQQEQAAYQASLRKEQLRV 2878
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHL--KKEEEKKAEEIRKEKEAVIE 1782
|
250
....*....|....*....
gi 1039779410 2879 DALERTLEQKNKEIEELTK 2897
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2708-2905 |
1.49e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2708 ALQVARAEVIAKErevSEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD-- 2785
Cdd:PTZ00121 1453 AEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADea 1527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2786 LNSVEKSLADLFRRYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQA 2865
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039779410 2866 AYQASLRK-EQLRVDALE-RTLEQKNKEIEELTKICDELIAK 2905
Cdd:PTZ00121 1607 MKAEEAKKaEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2759-2906 |
3.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2759 EDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADL---FRRYEKMKEVLEGFRKNEEvLKKCAQEYLSRVKKEEQRY 2835
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2836 QALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIA 2904
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
..
gi 1039779410 2905 KM 2906
Cdd:COG4717 235 EL 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2704-2905 |
8.40e-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: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2704 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 2783
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2784 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2863
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1039779410 2864 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2905
Cdd:TIGR02168 841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2711-2904 |
1.01e-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: 51.61 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2711 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIA---QMIGKPEDEqREKSISHQTVQQ---------LVLE 2778
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDekrQQLERLRRE-REKAERYQALLKekreyegyeLLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2779 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVR 2857
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLE 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2858 GKAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2904
Cdd:TIGR02169 308 RSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2705-2904 |
1.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2705 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIG-KPEDEQREKSISH 2769
Cdd:PRK03918 471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKlKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2770 qtVQQLVLEKEQALADLNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQA 2837
Cdd:PRK03918 551 --LEELKKKLAELEKKLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779410 2838 LK---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2904
Cdd:PRK03918 624 LEeelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2704-2905 |
1.75e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2704 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQR-EKSISH-----QTvQQLVL 2777
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlRKEIERlewrqQT-EVLSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2778 EKEQALadlnsVEKsLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVR 2857
Cdd:COG1340 133 EEEKEL-----VEK-IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELY 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779410 2858 GKAQqeqaayqaSLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2905
Cdd:COG1340 202 KEAD--------ELRKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2695-2897 |
2.49e-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: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2695 PPGLLFQQPDLDSALQVARAEVIAK-EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQ 2773
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2774 QLVLEKEQALADLNSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEI 2853
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779410 2854 AQVRGKAQQEQAAYQASLRK---EQLRVDALERTLEQKNKEIEELTK 2897
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2701-2905 |
2.91e-05 |
|
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: 48.99 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2701 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaqmigkpedEQREKSISHQTVQQLVLEKE 2780
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2781 QALADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKA 2860
Cdd:COG4942 120 PPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779410 2861 QQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2905
Cdd:COG4942 198 QKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2635-2908 |
3.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2635 KLQEELEFAVMRIE--ALKLARQIALASRSRQDTKREAAHPPDvsisktalysrigstEVEKppgllfqqpDLDSaLQVA 2712
Cdd:PRK03918 345 KKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPE---------------KLEK---------ELEE-LEKA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2713 RAEViakEREVSEWRDKYEESRREVVEMRKIVAEYE--KTIAQMIGKPEDEQREKSIshqtvqqlvleKEQALADLNSVE 2790
Cdd:PRK03918 400 KEEI---EEEISKITARIGELKKEIKELKKAIEELKkaKGKCPVCGRELTEEHRKEL-----------LEEYTAELKRIE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2791 KSLADLFRRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAY 2867
Cdd:PRK03918 466 KELKEIEEKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039779410 2868 QaSLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2908
Cdd:PRK03918 542 K-SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2694-2897 |
3.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2694 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmigkpedeqreksishq 2770
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2771 tVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 2850
Cdd:COG4717 127 -LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779410 2851 AEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 2897
Cdd:COG4717 199 EELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2701-2888 |
3.29e-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: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2701 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksisHQTVQQLVLEKE 2780
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2781 QALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQ 2855
Cdd:TIGR02168 393 LQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170 180 190
....*....|....*....|....*....|...
gi 1039779410 2856 VRgkaqQEQAAYQASLRKEQLRVDALERTLEQK 2888
Cdd:TIGR02168 473 AE----QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2736-2895 |
3.83e-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: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2736 EVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK 2812
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2813 NEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEI 2892
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQL 381
|
...
gi 1039779410 2893 EEL 2895
Cdd:TIGR02168 382 ETL 384
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2704-2905 |
7.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2704 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIgkpeDEQREKSISHQTVQQLVLEKEQ 2781
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2782 ALADlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQ 2861
Cdd:PTZ00121 1612 AKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAE 1678
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779410 2862 QEQAAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2905
Cdd:PTZ00121 1679 EAKKAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2634-2903 |
1.29e-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: 47.76 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2634 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 2713
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2714 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMigkPEDEQRE--KSISHQTVQQLVLEKEQALADLN--SV 2789
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRvkEKIGELEAEIASLERSIAEKEREleDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2790 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqa 2869
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE----------------- 382
|
250 260 270
....*....|....*....|....*....|....
gi 1039779410 2870 sLRKEQlrvDALERTLEQKNKEIEELTKICDELI 2903
Cdd:TIGR02169 383 -TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2634-2905 |
2.05e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2634 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYsrigstevekppgllfqqpDLDSALQVAR 2713
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELE-------------------ELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2714 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSL 2793
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2794 ADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASL 2871
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....
gi 1039779410 2872 RKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2905
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
2034-2145 |
2.19e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 46.27 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2034 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2106
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039779410 2107 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2145
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1729-2101 |
2.80e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 1729 PPEPDESKDEKLHLVAPEELLSDRK-------SPGPGPATLPSVPEACVPKGFPAEARDLGGVESIPGTDDVIQPAAPVD 1801
Cdd:PHA03307 79 APANESRSTPTWSLSTLAPASPAREgsptppgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 1802 PGHPP--LADSSHHGDAVSSVSTHLTVQSASPSAARASPAPLAPEHTASAPSA-AGPGVEVTPTASPQHLAKNEPRSSDS 1878
Cdd:PHA03307 159 PAAVAsdAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSpISASASSPAPAPGRSAADDAGASSSD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 1879 EEAFETPESTTPVKAPPAPPPpppevtpepevidPPAPEEPGCISEPPVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDK 1958
Cdd:PHA03307 239 SSSSESSGCGWGPENECPLPR-------------PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 1959 PIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTESVPPSKStLSRSLSLQaSDFDGASCPGSPEAGTL 2038
Cdd:PHA03307 306 GPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAAVSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRP 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779410 2039 TTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQQEPGEESPVPSEEHLAP 2101
Cdd:PHA03307 372 SRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLDAGAASGAFYARYPLLTP 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2708-2901 |
5.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2708 ALQVARAEVIAKEREV--SEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD 2785
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2786 L--NSVEKSLADLFRRYEKmkevlegfRKNEEVLKKCAQEylsrVKKEEQryqaLKVHAEEklDRANAEiaQVRGKAQQE 2863
Cdd:PTZ00121 1358 EaeAAEEKAEAAEKKKEEA--------KKKADAAKKKAEE----KKKADE----AKKKAEE--DKKKAD--ELKKAAAAK 1417
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779410 2864 QAAYQASLRKEQLR-VDALERTLEQKNKEiEELTKICDE 2901
Cdd:PTZ00121 1418 KKADEAKKKAEEKKkADEAKKKAEEAKKA-DEAKKKAEE 1455
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2704-2908 |
6.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2704 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 2783
Cdd:COG4372 63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2784 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2863
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779410 2864 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2908
Cdd:COG4372 221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2713-2908 |
7.11e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2713 RAEVIAKEREVSEWRDKYEESRREVVE-MRKIVAEYEKTIAQmIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEK 2791
Cdd:COG1340 31 RDELNEELKELAEKRDELNAQVKELREeAQELREKRDELNEK-VKELKEERDELNEKLNELREELDELRKELAELNKAGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2792 SLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE----------EK 2845
Cdd:COG1340 110 SIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikelaEE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779410 2846 LDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2908
Cdd:COG1340 190 AQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2720-2853 |
1.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2720 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSI-SHQTVQQLVLEKEQALADL-----------N 2787
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeEYEELREEYLELSRELAGLraeleelekrrE 690
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779410 2788 SVEKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2853
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2704-2905 |
1.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2704 DLDSALQVARAEVIAK---EREVSEWRDKYEESRReVVEMRKIVAEYEKTIAQMIGKPEDEQRE----KSISHQTVQQLV 2776
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKaeeKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAaeaaKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2777 LEKEQALAD--LNSVEKSLAD-LFRRYEKMKEVLEGFRKNEEVLKKCaqEYLSRVKKEEQRYQALKVHAEE--KLDRANA 2851
Cdd:PTZ00121 1361 AAEEKAEAAekKKEEAKKKADaAKKKAEEKKKADEAKKKAEEDKKKA--DELKKAAAAKKKADEAKKKAEEkkKADEAKK 1438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779410 2852 EIAQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2905
Cdd:PTZ00121 1439 KAEEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2713-2902 |
3.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2713 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmiGKPEDEQREKSISHQ--TVQQLVLEKEQALADLNSVE 2790
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEinGIEERIKELEEKEERLEELK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2791 KSLADLFRRYEKMKEVLEGFRKNEEVL-------KKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 2863
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKeelerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779410 2864 QAAYQAsLRK-------------EQLRVDALER-TLEQKN--KEIEELTKICDEL 2902
Cdd:PRK03918 425 KKAIEE-LKKakgkcpvcgreltEEHRKELLEEyTAELKRieKELKEIEEKERKL 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2751-2896 |
3.97e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2751 IAQMIGKPEDEQRE--KSIShqTVQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYL 2825
Cdd:TIGR02169 144 VTDFISMSPVERRKiiDEIA--GVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQ 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779410 2826 SRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 2896
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2710-2894 |
4.23e-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: 42.21 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2710 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL----------- 2777
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEREEEREAEREEIEEEKEREIARLRaqqekaqdeka 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2778 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2849
Cdd:pfam13868 202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039779410 2850 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2894
Cdd:pfam13868 280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2633-2891 |
4.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2633 AQKLQEELEfavmriealKLARQIALASRSRQDTKREAAhppdvsisktalysrigstevekppGLLFQQPDLDSALQVA 2712
Cdd:COG4942 22 AAEAEAELE---------QLQQEIAELEKELAALKKEEK-------------------------ALLKQLAALERRIAAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2713 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 2792
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2793 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgKAQQEQAAYQASLR 2872
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELE 226
|
250
....*....|....*....
gi 1039779410 2873 KEqlrVDALERTLEQKNKE 2891
Cdd:COG4942 227 AL---IARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2772-2896 |
7.05e-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: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2772 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2844
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1039779410 2845 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2896
Cdd:COG4913 289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2722-2848 |
9.88e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779410 2722 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKpEDEQREKSIS-HQTVQqlvlEKEQALADLNsveKSLADLFRRY 2800
Cdd:COG1340 168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADElHKEIV----EAQEKADELH---EEIIELQKEL 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039779410 2801 EKMKEVLEGFRKNEEVLKKcaqeylsrvKKEEQRYQALKVHAEEKLDR 2848
Cdd:COG1340 240 RELRKELKKLRKKQRALKR---------EKEKEELEEKAEEIFEKLKK 278
|
|
| |
