|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
868-1071 |
1.41e-98 |
|
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: 309.68 E-value: 1.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 868 FQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIgkpEDEQREKSISHQTVQQLVLEK 947
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMI---EEKQKQKELEHAEIQKVLEEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 948 EQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGK 1027
Cdd:pfam05010 78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907183027 1028 AQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1071
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
801-1073 |
2.63e-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: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 801 AQKLQEELEfaVMRIEALKLARQIALASRSRQDTKREAahppdvsisktalysrigstevekppgllfqqpdLDSALQVA 880
Cdd:COG1196 215 YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE----------------------------------LEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 881 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 960
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 961 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLR 1040
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270
....*....|....*....|....*....|...
gi 1907183027 1041 KEQLRVDALERTLEQKNKEIEELTKICDELIAK 1073
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
866-1065 |
1.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 866 LLFQQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKT---IAQMigKPEDEQREKSIshQTVQQ 942
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEEL--EKELESLEGSK--RKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 943 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA--- 1019
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkee 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 1020 --------------EIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTK 1065
Cdd:PRK03918 339 rleelkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
927-1074 |
6.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 927 EDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADL---FRRYEKMKEVLEGFRKNEEvLKKCAQEYLSRVKKEEQRY 1003
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLLPLYQELEA-LEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 1004 QALKvHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIA 1072
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
..
gi 1907183027 1073 KM 1074
Cdd:COG4717 235 EL 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
812-1065 |
6.90e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 812 VMRIEALKLARQIALASRSRQDTKREAAHPPDVSISKTALYSRIGSTEVEKPPGLLFQQPDLDSALQV-ARAEVIAKERE 890
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 891 ----VSEWRDKYEESRREVVEMRKiVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSLADLFR 966
Cdd:PTZ00121 1631 ekkkVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 967 RYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKldranAEIAQVrgKAQQEQAAYQASLRKEQLRV 1046
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHL--KKEEEKKAEEIRKEKEAVIE 1782
|
250
....*....|....*....
gi 1907183027 1047 DALERTLEQKNKEIEELTK 1065
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
872-1073 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 872 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksishqtVQQLVLEKEQAL 951
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-------LTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 952 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKkcaqeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 1031
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907183027 1032 QAAYQaslRKEQLRVDalertLEQKNKEIEELTKICDELIAK 1073
Cdd:TIGR02168 841 EDLEE---QIEELSED-----IESLAAEIEELEELIEELESE 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1073 |
1.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 876 ALQVARAEVIAKErevSEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD-- 953
Cdd:PTZ00121 1453 AEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADea 1527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 954 LNSVEKSLADLFRRYEKMKEVLEgFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQA 1033
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907183027 1034 AYQASLRK-EQLRVDALE-RTLEQKNKEIEELTKICDELIAK 1073
Cdd:PTZ00121 1607 MKAEEAKKaEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
869-1073 |
1.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 869 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIaqmigkpedEQREKSISHQTVQQLVLEKE 948
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 949 QALADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKA 1028
Cdd:COG4942 120 PPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907183027 1029 QQEqaayqasLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1073
Cdd:COG4942 198 QKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
879-1072 |
2.55e-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: 48.53 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 879 VARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIA---QMIGKPEDEqREKSISHQTVQQ---------LVLE 946
Cdd:TIGR02169 153 VERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDekrQQLERLRRE-REKAERYQALLKekreyegyeLLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 947 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVR 1025
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLE 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907183027 1026 GKAQQEQAAYQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 1072
Cdd:TIGR02169 308 RSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
863-1065 |
3.00e-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: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 863 PPGLLFQQPDLDSALQVARAEVIAK-EREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQ 941
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEElEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 942 QLVLEKEQALADLNSVEKSLADLfrrYEKMKEVLEGFRKNEEVLKKCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEI 1021
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907183027 1022 AQVRGKAQQEQAAYQASLRK---EQLRVDALERTLEQKNKEIEELTK 1065
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1056 |
3.33e-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: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 869 QQPDLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREksisHQTVQQLVLEKE 948
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ----LETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 949 QALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQ 1023
Cdd:TIGR02168 393 LQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
170 180 190
....*....|....*....|....*....|...
gi 1907183027 1024 VRgkaqQEQAAYQASLRKEQLRVDALERTLEQK 1056
Cdd:TIGR02168 473 AE----QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
904-1063 |
3.71e-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: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 904 EVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVL---EKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRK 980
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 981 NEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEI 1060
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELESRLEELEEQL 381
|
...
gi 1907183027 1061 EEL 1063
Cdd:TIGR02168 382 ETL 384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
862-1065 |
7.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 862 KPPGLLFQQPDLDSALQVARAEV---IAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAqmigkpedeqreksishq 938
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 939 tVQQLVLEKEQAladlnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 1018
Cdd:COG4717 127 -LLPLYQELEAL-------EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907183027 1019 AEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELTK 1065
Cdd:COG4717 199 EELEELQQR-----------LAELEEELEEAQEELEELEEELEQLEN 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
802-1073 |
1.29e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 802 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsisKTALYsrigstevekppgllfqqpDLDSALQVAR 881
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELE-------------------ELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 882 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKSL 961
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 962 ADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAYQASL 1039
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|....
gi 1907183027 1040 RKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1073
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PRK13335 |
PRK13335 |
superantigen-like protein SSL3; Reviewed; |
202-313 |
1.83e-04 |
|
superantigen-like protein SSL3; Reviewed;
Pssm-ID: 139494 [Multi-domain] Cd Length: 356 Bit Score: 45.12 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 202 EAGTLTTDACGTGSNSASSTLKRTKKTRPPSLKK-------KQATKKPTETPPVKETQQEPGEESPVPSEEHLAPETKTE 274
Cdd:PRK13335 45 KAERLAMINITAGANSATTQAANTRQERTPKLEKapntneeKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907183027 275 SATPEGAGCT---LSDDTPLESPAVPTATCPLTLESAEDVSP 313
Cdd:PRK13335 125 STTPKTKVTTppsTNTPQPMQSTKSDTPQSPTIKQAQTDMTP 166
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
802-1071 |
5.96e-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: 43.90 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 802 QKLQEELEFAVMRIEALKLARQIALASRSRQDTKREAAhppdvsISKTALYSRIGSTEVEKppgLLFQQPDLDSALQVAR 881
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEKREYEGYE---LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 882 AEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMigkPEDEQRE--KSISHQTVQQLVLEKEQALADLN--SV 957
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRvkEKIGELEAEIASLERSIAEKEREleDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 958 EKSLADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEkLDRANAEiaqvrgkaqqeqaayqa 1037
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAE----------------- 382
|
250 260 270
....*....|....*....|....*....|....
gi 1907183027 1038 sLRKEQlrvDALERTLEQKNKEIEELTKICDELI 1071
Cdd:TIGR02169 383 -TRDEL---KDYREKLEKLKREINELKRELDRLQ 412
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
888-1076 |
9.73e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 888 EREVSEWRDKYEESRREVVEMRKIVAEYE--KTIAQMIGKPEDEQREKSIshqtvqqlvleKEQALADLNSVEKSLADLF 965
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKkaKGKCPVCGRELTEEHRKEL-----------LEEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 966 RRYEKMKEV---LEGFRKNEEVLKKcAQEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAAYQaSLRKE 1042
Cdd:PRK03918 473 EKERKLRKElreLEKVLKKESELIK-LKELAEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIK-SLKKE 547
|
170 180 190
....*....|....*....|....*....|....
gi 1907183027 1043 QLRVDALERTLEQKNKEIEELTKICDELIAKMGK 1076
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
884-1072 |
9.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 884 VIAKEREVSEWRDKYE-----ESRREVVEMRKIVA---EYEKTIAQMIG-KPEDEQREKSISHqtVQQLVLEKEQALADL 954
Cdd:PRK03918 488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKlKGEIKSLKKELEK--LEELKKKLAELEKKL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 955 NSVEKSLADLFRRYEKmkevlEGFRKNEEV------LKKCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANA 1019
Cdd:PRK03918 566 DELEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEK 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907183027 1020 EIAQVRGK----AQQEQAAYQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 1072
Cdd:PRK03918 641 RLEELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1073 |
1.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 872 DLDSALQVARAEVIAKEREV--SEWRDKYEESRREvvEMRKIVAEYEKTIAQMIgkpeDEQREKSISHQTVQQLVLEKEQ 949
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKA--EEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEE 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 950 AladlnsveksladlfRRYEKMKEVLEGFRKNEEVLKKCAQeylSRVKKEEQRYQALKVHAEEKLDRANAEIAQvrgKAQ 1029
Cdd:PTZ00121 1612 A---------------KKAEEAKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKA 1670
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907183027 1030 QEQAAYQASLRKEQ----LRVDALERTLEQKNKeIEELTKICDELIAK 1073
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEedekKAAEALKKEAEEAKK-AEELKKKEAEEKKK 1717
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
872-1076 |
2.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 872 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQAL 951
Cdd:COG4372 63 QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 952 ADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKKcaQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQE 1031
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907183027 1032 QAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGK 1076
Cdd:COG4372 221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
801-1059 |
2.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 801 AQKLQEELEfavmriealKLARQIALASRSRQDTKREAAhppdvsisktalysrigstevekppGLLFQQPDLDSALQVA 880
Cdd:COG4942 22 AAEAEAELE---------QLQQEIAELEKELAALKKEEK-------------------------ALLKQLAALERRIAAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 881 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALADLNSVEKS 960
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 961 LADLFRRYEKMKEVLEGFRKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRgKAQQEQAAYQASLR 1040
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELE 226
|
250
....*....|....*....
gi 1907183027 1041 KEqlrVDALERTLEQKNKE 1059
Cdd:COG4942 227 AL---IARLEAEAAAAAER 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
872-1073 |
4.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 872 DLDSALQVARAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYEKTIAQMIGKPEDEQR-EKSISH-----QTvQQLVL 945
Cdd:COG1340 54 ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlRKEIERlewrqQT-EVLSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 946 EKEQALadlnsVEKsLADLFRRYEKMKEVLEGFRKNEEVLKKcAQEYLSRVKKEEQRYQALKvhaeEKLDRANAEIAQVR 1025
Cdd:COG1340 133 EEEKEL-----VEK-IKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELA----EEAQELHEEMIELY 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907183027 1026 GKAQqeqaayqaSLRKE-----------QLRVDALERTLEQKNKEIEELTKICDELIAK 1073
Cdd:COG1340 202 KEAD--------ELRKEadelhkeiveaQEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
940-1064 |
5.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 940 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVL---KKCAQEYLS-RVKKEEQRYQALKVH---AEE 1012
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLepiRELAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907183027 1013 KLDRANAEIAQVRGKaqqeqaayqasLRKEQLRVDALERTLEQKNKEIEELT 1064
Cdd:COG4913 289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1064 |
5.66e-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: 40.82 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 919 IAQMIGKPEDEQRE--KSIShqTVQQLVLEKEQALADLNSVEKSLadlfrryEKMKEVLEGFRKNEEVLKK---CAQEYL 993
Cdd:TIGR02169 144 VTDFISMSPVERRKiiDEIA--GVAEFDRKKEKALEELEEVEENI-------ERLDLIIDEKRQQLERLRRereKAERYQ 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907183027 994 SRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELT 1064
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
969-1073 |
6.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 969 EKMKEVLEGFRKNEEVLKKcaqEYLSRVKKEEQRyqaLKVHAEEKLDRANAEIAQVRGKAQQEQAA---YQASLRKEQLR 1045
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1907183027 1046 VDALERTLEQKNKEIEELTKICDELIAK 1073
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
881-1070 |
7.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 881 RAEVIAKEREVSEWRDKYEESRREVVEMRKIVAEYE-----KTIAQMIGKPE--------DEQREKSISHQTVQQLVLEK 947
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklKELAEQLKELEeklkkynlEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 948 EQALADLNSVEKSLADLFRRYEKMKEVLEGF-RKNEEVLKKCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 1026
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELeEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907183027 1027 kaqQEQAAYQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 1070
Cdd:PRK03918 612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1069 |
7.87e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 876 ALQVARAEVIAKEREV--SEWRDKYEESRREVVEMRKivAEYEKTIAQMIGKPEDEQREKSISHQTVQQLVLEKEQALAD 953
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907183027 954 L--NSVEKSLADLFRRYEKmkevlegfRKNEEVLKKCAQEylsrVKKEEQryqaLKVHAEEklDRANAEiaQVRGKAQQE 1031
Cdd:PTZ00121 1358 EaeAAEEKAEAAEKKKEEA--------KKKADAAKKKAEE----KKKADE----AKKKAEE--DKKKAD--ELKKAAAAK 1417
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907183027 1032 QAAYQASLRKEQLR-VDALERTLEQKNKEiEELTKICDE 1069
Cdd:PTZ00121 1418 KKADEAKKKAEEKKkADEAKKKAEEAKKA-DEAKKKAEE 1455
|
|
| |
