|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
2565-2765 |
4.29e-105 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 334.72 E-value: 4.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2565 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQA 2644
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2645 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 2724
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779444 2725 EQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 2765
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2563-2769 |
3.23e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2563 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQM-IEDEQREKSIshQTVQQLV 2638
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELeKELESLEGSK--RKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2639 LEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA----- 2713
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerl 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779444 2714 ------------EIAQVRGKAQQEQAAYQASLRKEQLR-------VDALERTLEQKNKEIEELTKICDELIAKMG 2769
Cdd:PRK03918 341 eelkkklkelekRLEELEERHELYEEAKAKKEELERLKkrltgltPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2569-2766 |
7.58e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQALADL 2648
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2649 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2728
Cdd:COG1196 326 AELEEELEEL---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190
....*....|....*....|....*....|....*...
gi 1039779444 2729 YQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2766
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2593-2768 |
1.41e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2593 DKYEESRREVVEMRKIVAEYEKtiaqmIEDEQREKSISHQTVQQLVLEKEQALADLnSVEKSLADLFRRYEKMKEVLEGF 2672
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2673 RKNEEVLKKCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNK 2752
Cdd:COG4717 145 PERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170
....*....|....*.
gi 1039779444 2753 EIEELTKICDELIAKM 2768
Cdd:COG4717 221 ELEELEEELEQLENEL 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2569-2767 |
1.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREksisHQTVQQLVLEKEQALADL 2648
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----SKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2649 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2728
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779444 2729 YQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 2767
Cdd:TIGR02168 844 EE---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2574-2757 |
6.63e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2574 LQVARAE-VIAKEREVSEWR-----DKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD 2647
Cdd:TIGR02168 207 RQAEKAErYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEE-LTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2648 LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqa 2727
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------ 359
|
170 180 190
....*....|....*....|....*....|
gi 1039779444 2728 ayqasLRKEQLRVDALERTLEQKNKEIEEL 2757
Cdd:TIGR02168 360 -----LEELEAELEELESRLEELEEQLETL 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2569-2767 |
6.64e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALAD- 2647
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAEl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2648 ----------------LNSveKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRA 2711
Cdd:COG4942 110 lralyrlgrqpplallLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779444 2712 NAEIAQVRGKAQQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 2767
Cdd:COG4942 187 RAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2570-2766 |
9.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2570 LDSALQVARAE------VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIEDEQREKSISHQTVQ 2635
Cdd:PRK03918 471 IEEKERKLRKElrelekVLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEK 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2636 QLVLEKEQALAD--LNSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK 2701
Cdd:PRK03918 551 LEELKKKLAELEkkLDELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779444 2702 ---VHAEEKLDRANAEIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 2766
Cdd:PRK03918 626 eelDKAFEELAETEKRLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2569-2767 |
1.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIEdEQREKSISHQTVQQLVLEKEQALA 2646
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2647 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 2726
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779444 2727 AAYQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 2767
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2563-2765 |
1.21e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2563 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQRE--KSISHQTVQQLVLE 2640
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2641 KEQALADLN--SVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqv 2718
Cdd:TIGR02169 308 RSIAEKEREleDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE---- 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779444 2719 rgkaqqeqaayqasLRKEQlrvDALERTLEQKNKEIEELTKICDELI 2765
Cdd:TIGR02169 383 --------------TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2576-2766 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2576 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIED-----EQREKSISHQTVQQ---------LVLEK 2641
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2642 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRG 2720
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLER 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779444 2721 KAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 2766
Cdd:TIGR02169 309 SIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2574-2767 |
1.52e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2574 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMiEDEQreksishQTvQQLVLEKEQALadlnsVEK 2653
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2654 sLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEylsRVKKEEQRyQALKVHAEEkLDRANAEIAQVRGKAQqeqaayqaSL 2733
Cdd:COG1340 142 -IKELEKELEKAKKALEKNEKLKELRAELKEL---RKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAD--------EL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779444 2734 RKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 2767
Cdd:COG1340 208 RKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2559-2749 |
2.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2559 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaQMIEDEQREKSISHQTVQ 2635
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2636 -QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLKKCAQEYLSRVKKEEQRYQAL---KVHAEEKLDR 2710
Cdd:COG4717 144 lPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELqqrLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779444 2711 ANAEIAQVRGKAQQEqaayqaslrKEQLRVDALERTLEQ 2749
Cdd:COG4717 218 AQEELEELEEELEQL---------ENELEAAALEERLKE 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2583-2767 |
2.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2583 AKEREVSEWRDKYEESRREVVEMRKIVAEYEKTiaqmiEDEQREKSISHQTVQQLVLEKEQALAD--LNSVEKSLADLFR 2660
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2661 RYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRK-EQLR 2739
Cdd:PTZ00121 1541 KAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAK 1619
|
170 180
....*....|....*....|....*....
gi 1039779444 2740 VDALE-RTLEQKNKEIEELTKICDELIAK 2767
Cdd:PTZ00121 1620 IKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2566-2750 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2566 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM--IEDEQREKSISHQT-VQQLVLEKE 2642
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesRLEELEEQLETLRSkVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2643 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgk 2721
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-- 474
|
170 180
....*....|....*....|....*....
gi 1039779444 2722 aqQEQAAYQASLRKEQLRVDALERTLEQK 2750
Cdd:TIGR02168 475 --QALDAAERELAQLQARLDSLERLQENL 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2584-2759 |
3.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2584 KEREVSEwrdkYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSIShqtvqqlvLEKEQALADLNSVEKSLADL---FR 2660
Cdd:PRK03918 271 LKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE--------KRLSRLEEEINGIEERIKELeekEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2661 RYEKMKEVLEGFRKNEEVLKKCAQEY---------LSRVKKEEQRYQALKVHAE-EKLDRANAEIaqvrgkaqqeqaayQ 2730
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEKLEKElEELEKAKEEI--------------E 404
|
170 180
....*....|....*....|....*....
gi 1039779444 2731 ASLRKEQLRVDALERTLEQKNKEIEELTK 2759
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2571-2759 |
3.80e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2571 DSALQVARAEVI--AKEREVSEWRDKYEESRREVVE-MRKivAEYEKTIAQMIEDEQREKsishQTVQQLVLEKEQalad 2647
Cdd:PTZ00121 1575 DKNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEeAKK--AEEAKIKAEELKKAEEEK----KKVEQLKKKEAE---- 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2648 lnsvEKSLADLFRRYEKMKEV-LEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVRgKAQQEQ 2726
Cdd:PTZ00121 1645 ----EKKKAEELKKAEEENKIkAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELK-KKEAEE 1714
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779444 2727 AAYQASLRKEQ----LRVDALERTLEQKNKEIEELTK 2759
Cdd:PTZ00121 1715 KKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2578-2764 |
5.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2578 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAE------YEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSV 2651
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2652 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKE------------EQRYQALKVHAEEKLDRANAEiaqvr 2719
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDE-LEEELAELLKEleelgfesveelEERLKELEPFYNEYLELKDAE----- 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779444 2720 gkaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 2764
Cdd:PRK03918 612 ----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2564-2759 |
6.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2564 LFQQPDLDSALQVARAEviaKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQ 2643
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2644 A--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-- 2719
Cdd:PTZ00121 1677 AeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDee 1754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1039779444 2720 -----GKAQQEQAAYQASLRKEQLRV--DALERTLEQKNKEIEELTK 2759
Cdd:PTZ00121 1755 ekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2577-2759 |
9.91e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2577 ARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEK--- 2653
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2654 SLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHA---EEKLDRANAEIAQVRGKAQQEQAAYQ 2730
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190
....*....|....*....|....*....|..
gi 1039779444 2731 ASLRK---EQLRVDALERTLEQKNKEIEELTK 2759
Cdd:TIGR02168 828 SLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2584-2764 |
1.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2584 KEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYE 2663
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2664 KMKEVLEGFRKNEEVLKK-------CAQEY--------LSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 2728
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKakgkcpvCGRELteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1039779444 2729 YQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 2764
Cdd:PRK03918 496 IKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2596-2759 |
1.74e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2596 EESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 2675
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2676 EEVLkkcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaayqaslRKEQLrvDALERTLEQKNKEIE 2755
Cdd:COG4372 110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEEL--KELEEQLESLQEELA 167
|
....
gi 1039779444 2756 ELTK 2759
Cdd:COG4372 168 ALEQ 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2585-2770 |
2.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2585 EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM-------------IEDEQRE----------KSIShQTVQQLVLEK 2641
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreLTEEHRKelleeytaelKRIE-KELKEIEEKE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2642 EQALADLNSVEKSLADLfRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEeqrYQALKvhaeEKLDRANAEIaqvrgk 2721
Cdd:PRK03918 476 RKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEE---YEKLK----EKLIKLKGEI------ 541
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779444 2722 aqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 2770
Cdd:PRK03918 542 ---------KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
2007-2118 |
2.46e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 46.27 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2007 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 2079
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039779444 2080 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 2118
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2574-2715 |
3.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2574 LQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI--VAEYEKtiaqmIEDEQREKSISHQTVQQlvlEKEQALADLNSV 2651
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779444 2652 EKSLADLFRRYEKMKEVlegfRKNEEVLKKcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 2715
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2573-2757 |
3.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2573 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKI----------------VAEYEKTIAQmIEDEQREKSISHQTVQQ 2636
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2637 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 2716
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039779444 2717 QvrgkaqqeqaayqaSLRKeqlRVDALERTLEQKNKEIEEL 2757
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2578-2770 |
3.39e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2578 RAEVIAkerEVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE------DEQREKSISHQTVQQLVLEKEQALADLNSV 2651
Cdd:COG1340 31 RDELNE---ELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2652 EKSLADLFRRYEKM--------------KEVLEGFRKNEEVLK--KCAQEYLSRVKKEEQRYQALKVHAE---------- 2705
Cdd:COG1340 108 GGSIDKLRKEIERLewrqqtevlspeeeKELVEKIKELEKELEkaKKALEKNEKLKELRAELKELRKEAEeihkkikela 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779444 2706 EKLDRANAEIAQVRGKaqqeqaayQASLRKEqlrVDALERTLEQKNKEIEELTKICDELIAKMGK 2770
Cdd:COG1340 188 EEAQELHEEMIELYKE--------ADELRKE---ADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1741-2074 |
4.72e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.93 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 1741 GKPSISSPPEPDESKDEKLHLVAPEELLSDRKSPGPGPAtlPSVPEACVPKGfPAEARDLGGVESIPG-TDDVIQPAAPV 1819
Cdd:PHA03307 116 PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPA--AGASPAAVASD-AASSRQAALPLSSPEeTARAPSSPPAE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 1820 DPGHPPLADSSHHGDAVSSVSTHLTVQRSSDSEEAFETPESTTPVKAPPAPPPPPPEVTPEPEVIDPPAP-EEPGCISEP 1898
Cdd:PHA03307 193 PPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPiTLPTRIWEA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 1899 PVVVPDGPRSSESVEGSPFRPSHSSSAVFDEDKPIASSGTYNLDfdsielvdnFQSLEPCSADSKGQECKVSTRrksTES 1978
Cdd:PHA03307 273 SGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS---------SSSSSRESSSSSTSSSSESSR---GAA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 1979 VPPSKStLSRSLSLQaSDFDGASCPGSPEAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKKKQAT-KKPTETPPVKETQ 2057
Cdd:PHA03307 341 VSPGPS-PSRSPSPS-RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATgRFPAGRPRPSPLD 418
|
330
....*....|....*..
gi 1039779444 2058 QEPGEESPVPSEEHLAP 2074
Cdd:PHA03307 419 AGAASGAFYARYPLLTP 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2569-2719 |
5.85e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM---IEDEQREKSISHQTVQQLVLEKEQAL 2645
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLS 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779444 2646 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 2719
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2564-2756 |
2.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2564 LFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQM----------IEDEQREKSISHQT 2633
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAqaelaqaqeeLESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2634 VQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLkkcaQEYLSRVKKEEQRYqaLKVHAEEKLDRANA 2713
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL----QEELAALEQELQAL--SEAEAEQALDELLK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779444 2714 EIAqvRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEE 2756
Cdd:COG4372 191 EAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2556-2765 |
2.33e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2556 EVEKppgllfQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQR--EKSISHQT 2633
Cdd:PRK04778 307 YVEK------NSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERiaEQEIAYSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2634 VQqlvlekeqalADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLS-------RVKKEE-----QRYQALK 2701
Cdd:PRK04778 381 LQ----------EELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklheikrYLEKSNlpglpEDYLEMF 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779444 2702 VHAEEKLDRANAEIAQVRgkaqqeqaayqaslrkeqLRVDALERTLEQKNKEIEELTKICDELI 2765
Cdd:PRK04778 451 FEVSDEIEALAEELEEKP------------------INMEAVNRLLEEATEDVETLEEETEELV 496
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2575-2756 |
2.49e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2575 QVARAEVIAKEREVSEWRDK-YEESRREvvEMRkiVAEYEKTIAQ---MIEDEQREKSISHQTVQQLVL----------- 2639
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELeKEEEREE--DER--ILEYLKEKAEreeEREAEREEIEEEKEREIARLRaqqekaqdeka 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2640 EKEQALADLNSVE-------KSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYlsRVKKEEQRYQALKVHAE-EKLDRA 2711
Cdd:pfam13868 202 ERDELRAKLYQEEqerkerqKEREEAEKKARQRQELQQAREEQIELKERRLAEE--AEREEEEFERMLRKQAEdEEIEQE 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039779444 2712 NAEiaQVRGKAQQEQAAYQASLR-KEQLRVDALERTLEQKNKEIEE 2756
Cdd:pfam13868 280 EAE--KRRMKRLEHRRELEKQIEeREEQRAAEREEELEEGERLREE 323
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2569-2767 |
3.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREV---------SEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVL 2639
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKkkadeakkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2640 EKEQALAD--LNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEI 2715
Cdd:PTZ00121 1362 AEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKA 1440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039779444 2716 AQVRgKAQQEQAAYQASLRKEQLRVDALE-RTLEQKNKEIEELTKiCDELIAK 2767
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKK-ADEAKKK 1491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2587-2759 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2587 EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQmIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMK 2666
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ-LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2667 EVLEG-FRKNEEV-------LKKCAQEYLSrVKKEEQRYQALKVHAEEKLDRANAEIA----------QVRGKAQQEQAA 2728
Cdd:TIGR04523 394 NDLESkIQNQEKLnqqkdeqIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKV 472
|
170 180 190
....*....|....*....|....*....|.
gi 1039779444 2729 YQASLRKEQLRVDALERTLEQKNKEIEELTK 2759
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
2608-2757 |
4.20e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2608 IVAEYEKTIAQMiedeqrEKSISHQTVQQLVL------EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKK 2681
Cdd:pfam13851 2 LMKNHEKAFNEI------KNYYNDITRNNLELikslkeEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2682 CAQEYL----------SRVKKEEQRYQALKVHAEEKL--------------DRANAEIAQVRGKaqqeqaayqaSLRKEQ 2737
Cdd:pfam13851 76 QLENYEkdkqslknlkARLKVLEKELKDLKWEHEVLEqrfekvererdelyDKFEAAIQDVQQK----------TGLKNL 145
|
170 180
....*....|....*....|...
gi 1039779444 2738 L---RVDALERTLEQKNKEIEEL 2757
Cdd:pfam13851 146 LlekKLQALGETLEKKEAQLNEV 168
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2577-2717 |
4.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2577 ARAEVIAKEREVsEWRDKYEESR----REVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVE 2652
Cdd:PRK12704 49 KEAEAIKKEALL-EAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779444 2653 KSLADLFRRYEKMKEVLE---GFRKNE-------EVLKKCAQEYLSRVKKEEQRyqalkvhAEEKLDR-ANAEIAQ 2717
Cdd:PRK12704 128 KKEEELEELIEEQLQELErisGLTAEEakeilleKVEEEARHEAAVLIKEIEEE-------AKEEADKkAKEILAQ 196
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2573-2764 |
4.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2573 ALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIE-DEQREKSISHQTVQQLVLEKEQALADLNSV 2651
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2652 EKSlADLFRRYEKMKEVLEGFRKNEEVLKKCAQ----EYLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRGKAQQE 2725
Cdd:PTZ00121 1424 KKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEA 1502
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039779444 2726 QAAYQASLRKEQLRvDALERTLEQKNKEIEELTKiCDEL 2764
Cdd:PTZ00121 1503 KKAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK-ADEA 1539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2589-2767 |
5.68e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2589 SEWRDKYEESRREVVEMRKIVAEyEKTIAQMIEDEQREKSISHQTVQQLVLEKEQaladlnsVEKSLADLFRRYEKMKev 2668
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKEKIEKLESEKKE-------KESKISDLEDELNKDD-- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2669 legFRKNEEVLKKCAQEYLSRVKKEEQRYQALKV---HAEEKLDRANAEIAQVR------GKAQQEQAAYQASLRKEQLR 2739
Cdd:TIGR04523 552 ---FELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIkeieekEKKISSLEKELEKAKKENEK 628
|
170 180 190
....*....|....*....|....*....|..
gi 1039779444 2740 VDALERTLEQK----NKEIEELTKICDELIAK 2767
Cdd:TIGR04523 629 LSSIIKNIKSKknklKQEVKQIKETIKEIRNK 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2634-2758 |
5.95e-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: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2634 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 2706
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1039779444 2707 KLDRANAEIAQVRgkaqqeqaayqASLRKEQLRVDALERTLEQKNKEIEELT 2758
Cdd:COG4913 289 RLELLEAELEELR-----------AELARLEAELERLEARLDALREELDELE 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2569-2768 |
6.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2569 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEyektiaqmIEDEQREKSISHQTVQQLVLEKEQALA-- 2646
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------LEKEIKRLELEIEEVEARIKKYEEQLGnv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2647 ----DLNSVEKSLADLfrryEKMKEVLEgfrknEEVLkkcaqeylsrvkkeeqryqalkvHAEEKLDRANAEIAQVRGKA 2722
Cdd:COG1579 86 rnnkEYEALQKEIESL----KRRISDLE-----DEIL-----------------------ELMERIEELEEELAELEAEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039779444 2723 QQeqaayqaslRKEQLR--VDALERTLEQKNKEIEELTKICDELIAKM 2768
Cdd:COG1579 134 AE---------LEAELEekKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2578-2763 |
6.31e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2578 RAEVIAKEREVsewrdkyEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTV--QQLVLEKEQALADLNSVEKSL 2655
Cdd:pfam02463 185 LAELIIDLEEL-------KLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2656 ADLFRRYEKMKEVLEGFRKNEEVLK-----------KCAQEYLSRVKKEEQRYQALK--VHAEEKLDRANAEIAQVRGKA 2722
Cdd:pfam02463 258 QEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllakEEEELKSELLKLERRKVDDEEklKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1039779444 2723 QQEQAAYQASLRKEQL----RVDALERTLEQKNKEIEELTKICDE 2763
Cdd:pfam02463 338 EELEKELKELEIKREAeeeeEEELEKLQEKLEQLEEELLAKKKLE 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2570-2764 |
7.08e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2570 LDSALQVARAEViakeREVSEW-RDKYEESRREVVEMRKIVAEYEKtiAQMIEDEQREKSISHQTVQQLVLEKEQALADL 2648
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2649 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkkcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 2725
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1039779444 2726 QAAYQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 2764
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2628-2770 |
7.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2628 SISHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEgfRKNEEVLKkcAQEYLSRVKKEEQRYQALKVHAEEK 2707
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE--QARSELEQ--LEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779444 2708 LDRANAEIAQVRGKAQQEQAAYQA-SLRKEQL--RVDALERTLEQKNKEIEELTKICDELIAKMGK 2770
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDlEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2578-2756 |
7.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2578 RAEVIAKER-EVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLA 2656
Cdd:PRK01156 347 RYDDLNNQIlELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2657 DLFRRYEKMKEVLEGFRKNEEVLK---KC-------AQEYLSRVKKEeqrYQALKVHAEEKLDRANAEIAQVRGKAQQEQ 2726
Cdd:PRK01156 427 SLNQRIRALRENLDELSRNMEMLNgqsVCpvcgttlGEEKSNHIINH---YNEKKSRLEEKIREIEIEVKDIDEKIVDLK 503
|
170 180 190
....*....|....*....|....*....|
gi 1039779444 2727 AAYQASLRKEQLRVDALERTLEQKNKEIEE 2756
Cdd:PRK01156 504 KRKEYLESEEINKSINEYNKIESARADLED 533
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2663-2767 |
9.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779444 2663 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 2739
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1039779444 2740 VDALERTLEQKNKEIEELTKICDELIAK 2767
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| |
