|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
790-990 |
6.28e-102 |
|
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: 317.39 E-value: 6.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 790 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 869
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 870 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 949
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45827753 950 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 990
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
794-991 |
5.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 794 DLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADL 873
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 874 NSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 953
Cdd:COG1196 326 AELEEELEEL---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190
....*....|....*....|....*....|....*...
gi 45827753 954 HQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIA 991
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
795-988 |
6.28e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 795 LDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQMIEDEQREKsvshqtvQQLVLEKEQALA 871
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQK-------QILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 872 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVH---AEEKLDRANAEIAQVRGKAQ 948
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIA 396
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45827753 949 qeqaahqaSLRKEQLRVDA----LERTLEQKNKEIEELTKICDE 988
Cdd:TIGR02168 397 --------SLNNEIERLEArlerLEDRRERLQQEIEELLKKLEE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
795-993 |
1.30e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 795 LDSALQIARAEIITKE-REVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQReksvsHQTVQQLVLEKEQALADL 873
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 874 nSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 953
Cdd:COG4717 122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45827753 954 HQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKM 993
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
788-984 |
5.45e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 788 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSV--SHQTVQQLVLE 865
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 866 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 938
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45827753 939 ----------EIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 984
Cdd:PRK03918 343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-992 |
6.45e-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: 49.76 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 791 QQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIaqmiedEQREKSVSHQTVQQLVLEKEQAL 870
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------EAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 871 ADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 950
Cdd:COG4942 123 ALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45827753 951 qaahqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 992
Cdd:COG4942 201 -------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
809-982 |
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: 50.06 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 809 KEREVSEWKDKYEESRREVMEMRKIVAEYEktiaQMIEDEQREKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFR 885
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 886 RYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaahqasLRKEQLRV 965
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAEL 367
|
170
....*....|....*..
gi 45827753 966 DALERTLEQKNKEIEEL 982
Cdd:TIGR02168 368 EELESRLEELEEQLETL 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
783-975 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 783 EKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMiEDEQREKSVSHQTVQQL 862
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-ESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 863 VLEKEQALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 937
Cdd:TIGR02168 388 VAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
170 180 190
....*....|....*....|....*....|....*...
gi 45827753 938 AEIAQVRgkaqQEQAAHQASLRKEQLRVDALERTLEQK 975
Cdd:TIGR02168 468 EELEEAE----QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
803-984 |
1.29e-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: 49.28 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 803 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKS 879
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 880 LADLfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLR 959
Cdd:TIGR02168 756 LTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180
....*....|....*....|....*...
gi 45827753 960 K---EQLRVDALERTLEQKNKEIEELTK 984
Cdd:TIGR02168 832 RiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
802-991 |
3.34e-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: 48.14 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 802 ARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIED-----EQREKSVSHQTVQQ---------LVLEKE 867
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 868 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRGK 946
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLERS 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45827753 947 AQQEQAAHQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 991
Cdd:TIGR02169 310 IAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
798-992 |
3.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 798 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVE 877
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 878 KSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAHQ 955
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEAL 444
|
170 180 190
....*....|....*....|....*....|....*..
gi 45827753 956 ASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 992
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
788-981 |
3.99e-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: 47.76 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 788 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQ-------REKSVSHQTVQ 860
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekiGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 861 QLVLEKEQALADLnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEE---KLDRAN 937
Cdd:TIGR02169 308 RSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETR 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45827753 938 AEIAQVRgKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEE 981
Cdd:TIGR02169 385 DELKDYR-EKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
780-984 |
5.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 780 AEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEWKDKYEESR----REVMEMRKIVAEYEKTIAQMIEDEQREKS 853
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKnmalRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 854 VSHQTVQQLVLEKEQaLADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLK-RCAQEylsRVKKEEQRYQALKVHAEEK 932
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEE-LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEE---AKKAEEDKKKAEEAKKAEE 1685
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827753 933 LDRANAE-----------IAQVRgKAQQEQAAHQASLRKEQ----LRVDALERTLEQKNKEIEELTK 984
Cdd:PTZ00121 1686 DEKKAAEalkkeaeeakkAEELK-KKEAEEKKKAEELKKAEeenkIKAEEAKKEAEEDKKKAEEAKK 1751
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
755-988 |
6.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 755 KLQREAAHPTDVSISKTALYSRigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEWKDKYEESRR-----EV 827
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAK--KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEEARKAEDAKKaeavkKA 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 828 MEMRKIVAEYEKTIAQMIEDEQR---EKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNE 901
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRkfeEARMAHFARRQAAIkaeEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 902 EvlKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQeqaahqasLRKEQLRVDALERTLEQKNKEIEE 981
Cdd:PTZ00121 1313 E--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKAEAAEKKKEEAKKKADA 1382
|
....*..
gi 45827753 982 LTKICDE 988
Cdd:PTZ00121 1383 AKKKAEE 1389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
798-982 |
7.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 798 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKI----------------VAEYEKTIAQmIEDEQREKSVSHQTVQQ 861
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 862 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 941
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45827753 942 QvrgkaqqeqaahqaSLRKeqlRVDALERTLEQKNKEIEEL 982
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
794-992 |
1.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 794 DLDSALQIARAEIITKEREV--SEWKDKYEESRREvmEMRKIVAEYEKTIAQMIEdEQREKSVSHQTVQQLVLEKEQALA 871
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 872 DlnSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQ 951
Cdd:PTZ00121 1615 A--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAK 1681
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45827753 952 AAHQASLRKEQlrvdALERTLEQKNKeIEELTKICDELIAK 992
Cdd:PTZ00121 1682 KAEEDEKKAAE----ALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
751-964 |
2.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 751 LFAQKLQREAAhptdvsisktALYSRIGtaevEKPAGLLFQQPDLDSALQIAR---AEIITKEREVSEWKDKYEESRREV 827
Cdd:COG4717 46 MLLERLEKEAD----------ELFKPQG----RKPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 828 MEMRKIVAEYEKTIaQMIEDEQREKSVSHQTVQ-QLVLEK-EQALADLNSVEKSLADLFRRYEKMKEVLEgfrkneEVLK 905
Cdd:COG4717 112 EELREELEKLEKLL-QLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQEELE------ELLE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45827753 906 RCAQEYLSRVKKEEQRYQAL---KVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLR 964
Cdd:COG4717 185 QLSLATEEELQDLAEELEELqqrLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
789-984 |
4.24e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 789 LFQQPDLDSALQIARAEiitKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQ 868
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 869 A--LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-- 944
Cdd:PTZ00121 1677 AeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDee 1754
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45827753 945 -----GKAQQEQAAHQASLRKEQLRV--DALERTLEQKNKEIEELTK 984
Cdd:PTZ00121 1755 ekkkiAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
781-989 |
7.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 781 EVEKPAGLLFQQPdldSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQ 860
Cdd:PRK03918 311 EIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 861 QLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLK----RCA-----------QEYLSRVKKEEQRYQAL 925
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgKCPvcgrelteehrKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45827753 926 KVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 989
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
803-989 |
8.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 803 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAE------YEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSV 876
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 877 EKSLADLFRRYEKMKE-------VLEGFRKNEE----VLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 945
Cdd:PRK03918 538 KGEIKSLKKELEKLEElkkklaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45827753 946 kaqQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 989
Cdd:PRK03918 612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
205-538 |
1.35e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 205 TKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPsgenlASETKTESAKTEGPSPAlleeTPLEPAVGPKAACPLD 284
Cdd:PHA03247 2680 PQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS-----ATPLPPGPAAARQASPA----LPAAPAPPAVPAGPAT 2750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 285 SESAEGVVPPASGGGRVQNSPPVGRKTLP---LTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENP 361
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPprrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 362 PPTKKIGKKPVAKMPL-----------------RRPKMKKTPEKldntPASPPRSPAEPNDIPIAKgtytfdidkwddPN 424
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPppslplggsvapggdvrRRPPSRSPAAK----PAAPARPPVRRLARPAVS------------RS 2894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 425 FNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPL 504
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974
|
330 340 350
....*....|....*....|....*....|....
gi 45827753 505 KTdtFRVkkspkrsplsdPPSQDPTPAATPETPP 538
Cdd:PHA03247 2975 PR--FRV-----------PQPAPSREAPASSTPP 2995
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
794-944 |
1.93e-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: 42.36 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 794 DLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQAL 870
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYrekLEKLKREINELKRELDRLQEELQRLS 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45827753 871 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 944
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
799-940 |
2.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 799 LQIARAEIITKEREVSEWKDKYEESRREVMEMRKI--VAEYEKtiaqmIEDEQREKSVSHQTVQQlvlEKEQALADLNSV 876
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827753 877 EKSLADLFRRYEKMKEVlegfRKNEEVLKRcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 940
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-983 |
3.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 859 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVLKRC---AQEYLS-RVKKEEQRYQALKVH---AEE 931
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLEPIrelAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45827753 932 KLDRANAEIAQVRGKaqqeqaahqasLRKEQLRVDALERTLEQKNKEIEELT 983
Cdd:COG4913 289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
795-989 |
5.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 795 LDSALQIARAEIitkeREVSEW-KDKYEESRREVMEMRKIVAEYEKtiAQMIEDEQREKSVSHQTVQQLVLEKEQALADL 873
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 874 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkrcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 950
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45827753 951 QAAHQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 989
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
806-991 |
6.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 806 IITKEREVSEWKDKYE-----ESRREVMEMRKIVA---EYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNS 875
Cdd:PRK03918 488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 876 VEKSLADLFRRYEKmkevlEGFRKNEEV------LKRCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANAEI 940
Cdd:PRK03918 568 LEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEKRL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45827753 941 AQVRGK----AQQEQAAHQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 991
Cdd:PRK03918 643 EELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
821-984 |
7.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 821 EESRREVMEMRKIVAEYEKTIAQmIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKN 900
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 901 EEVLkrcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgkaqqeqaahqaslRKEQLRvdALERTLEQKNKEIE 980
Cdd:COG4372 110 AEEL----QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE----------------REEELK--ELEEQLESLQEELA 167
|
....
gi 45827753 981 ELTK 984
Cdd:COG4372 168 ALEQ 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
789-985 |
8.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 789 LFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM----------IEDEQREKSVSHQT 858
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAqaelaqaqeeLESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 859 VQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLkrcaQEYLSRVKKEEQRYQALKVHAE--EKLDRA 936
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL----QEELAALEQELQALSEAEAEQAldELLKEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45827753 937 NAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKI 985
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
775-946 |
9.01e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 775 SRIGTAEVEKpagllfqqpdlDSALQIARAEiitKEREVSEwkdkyEESRREVMEMRkiVAEYEKTIAQMIEDEQREKsv 854
Cdd:COG2268 201 ARIAEAEAER-----------ETEIAIAQAN---REAEEAE-----LEQEREIETAR--IAEAEAELAKKKAEERREA-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 855 shqtvqqlvlEKEQALADLnSVEKsladlfRRYEKMKEV---LEGFRKNEEVLkrcAQEylSRVKKEEQRYQA---LKVH 928
Cdd:COG2268 258 ----------ETARAEAEA-AYEI------AEANAEREVqrqLEIAEREREIE---LQE--KEAEREEAELEAdvrKPAE 315
|
170 180
....*....|....*....|..
gi 45827753 929 AE----EKLDRANAEIAQVRGK 946
Cdd:COG2268 316 AEkqaaEAEAEAEAEAIRAKGL 337
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
803-992 |
9.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 803 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMiEDEQreksvshQTvQQLVLEKEQALadlnsVEKsLAD 882
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERL-EWRQ-------QT-EVLSPEEEKEL-----VEK-IKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827753 883 LFRRYEKMKEVLEGFRKNEEVLKrcaqEYLSRVKKEEQRYQALKVHAEEkLDRANAEIAQVRGKAQqeqaahqaSLRKE- 961
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKELRA----ELKELRKEAEEIHKKIKELAEE-AQELHEEMIELYKEAD--------ELRKEa 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45827753 962 ----------QLRVDALERTLEQKNKEIEELTKICDELIAK 992
Cdd:COG1340 212 delhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| |
