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Conserved domains on  [gi|1370456167|ref|XP_024303533|]
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transforming acidic coiled-coil-containing protein 2 isoform X41 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
863-1063 8.49e-101

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: 315.46  E-value: 8.49e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  863 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 942
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  943 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 1022
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1370456167 1023 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1063
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
243-630 2.79e-05

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.53  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  243 SGENLASETKTESAKTEGPSpalleETPLEPAVGPKAacPLDSESAEGVVPPASGggrvQNSPPVGRKtlPLTTapEAGE 322
Cdd:PTZ00449   492 SKKKLAPIEEEDSDKHDEPP-----EGPEASGLPPKA--PGDKEGEEGEHEDSKE----SDEPKEGGK--PGET--KEGE 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  323 VTPSDSGGQEDSPAK--GLSVRLEFDySEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPeKLDNTPASP--PR 398
Cdd:PTZ00449   557 VGKKPGPAKEHKPSKipTLSKKPEFP-KDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIP-KSPKRPESPksPK 634
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  399 SPAEPNDiPIAKgtytfdidkwDDPNFNPFSSTSKMQESPKLPqqsynFDPDTCDESVDPFktssktpsspskspasfei 478
Cdd:PTZ00449   635 RPPPPQR-PSSP----------ERPEGPKIIKSPKPPKSPKPP-----FDPKFKEKFYDDY------------------- 679
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  479 pasameangvdgdgLNKPAKKKKTPLKTMVEDVMSVCSLFDTFRVKKSPKRSPLSDPPSQdPTPAATPETPPVISavvha 558
Cdd:PTZ00449   680 --------------LDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKL-PRDEEFPFEPIGDP----- 739
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370456167  559 tdeeklavtnqkwtcmTVDLEADKQDYPQPSDLSTFVNETKFSSPTEGKQLCSQLDPHSASENPAPREPKAR 630
Cdd:PTZ00449   740 ----------------DAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEAMKR 795
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
863-1063 8.49e-101

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: 315.46  E-value: 8.49e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  863 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 942
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  943 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 1022
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1370456167 1023 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1063
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
796-1064 4.66e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  796 AQKLQEELEfaimRIEALKLARQIALASRSHQDAKREAAhptdvsisktalysrigtaevekpagllfqqpDLDSALQIA 875
Cdd:COG1196    215 YRELKEELK----ELEAELLLLKLRELEAELEELEAELE--------------------------------ELEAELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  876 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVEKSLAD 955
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  956 LfrrYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQ 1035
Cdd:COG1196    335 L---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                          250       260
                   ....*....|....*....|....*....
gi 1370456167 1036 LRVDALERTLEQKNKEIEELTKICDELIA 1064
Cdd:COG1196    411 ALLERLERLEEELEELEEALAELEEEEEE 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
868-1061 9.47e-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: 53.14  E-value: 9.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  868 LDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQMIEDEQREKsvshqtvQQLVLEKEQALA 944
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQK-------QILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  945 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVH---AEEKLDRANAEIAQVRGKAQ 1021
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIA 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370456167 1022 qeqaahqaSLRKEQLRVDA----LERTLEQKNKEIEELTKICDE 1061
Cdd:TIGR02168  397 --------SLNNEIERLEArlerLEDRRERLQQEIEELLKKLEE 432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
861-1057 6.21e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  861 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSV--SHQTVQQLVLE 938
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  939 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 1011
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370456167 1012 ----------EIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 1057
Cdd:PRK03918   343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
243-630 2.79e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.53  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  243 SGENLASETKTESAKTEGPSpalleETPLEPAVGPKAacPLDSESAEGVVPPASGggrvQNSPPVGRKtlPLTTapEAGE 322
Cdd:PTZ00449   492 SKKKLAPIEEEDSDKHDEPP-----EGPEASGLPPKA--PGDKEGEEGEHEDSKE----SDEPKEGGK--PGET--KEGE 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  323 VTPSDSGGQEDSPAK--GLSVRLEFDySEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPeKLDNTPASP--PR 398
Cdd:PTZ00449   557 VGKKPGPAKEHKPSKipTLSKKPEFP-KDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIP-KSPKRPESPksPK 634
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  399 SPAEPNDiPIAKgtytfdidkwDDPNFNPFSSTSKMQESPKLPqqsynFDPDTCDESVDPFktssktpsspskspasfei 478
Cdd:PTZ00449   635 RPPPPQR-PSSP----------ERPEGPKIIKSPKPPKSPKPP-----FDPKFKEKFYDDY------------------- 679
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  479 pasameangvdgdgLNKPAKKKKTPLKTMVEDVMSVCSLFDTFRVKKSPKRSPLSDPPSQdPTPAATPETPPVISavvha 558
Cdd:PTZ00449   680 --------------LDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKL-PRDEEFPFEPIGDP----- 739
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370456167  559 tdeeklavtnqkwtcmTVDLEADKQDYPQPSDLSTFVNETKFSSPTEGKQLCSQLDPHSASENPAPREPKAR 630
Cdd:PTZ00449   740 ----------------DAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEAMKR 795
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
863-1063 8.49e-101

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: 315.46  E-value: 8.49e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  863 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 942
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  943 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 1022
Cdd:pfam05010   81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1370456167 1023 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1063
Cdd:pfam05010  161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
796-1064 4.66e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  796 AQKLQEELEfaimRIEALKLARQIALASRSHQDAKREAAhptdvsisktalysrigtaevekpagllfqqpDLDSALQIA 875
Cdd:COG1196    215 YRELKEELK----ELEAELLLLKLRELEAELEELEAELE--------------------------------ELEAELEEL 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  876 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVEKSLAD 955
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEE 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  956 LfrrYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQ 1035
Cdd:COG1196    335 L---EEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                          250       260
                   ....*....|....*....|....*....
gi 1370456167 1036 LRVDALERTLEQKNKEIEELTKICDELIA 1064
Cdd:COG1196    411 ALLERLERLEEELEELEEALAELEEEEEE 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
868-1061 9.47e-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: 53.14  E-value: 9.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  868 LDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQMIEDEQREKsvshqtvQQLVLEKEQALA 944
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQK-------QILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  945 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVH---AEEKLDRANAEIAQVRGKAQ 1021
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIA 396
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370456167 1022 qeqaahqaSLRKEQLRVDA----LERTLEQKNKEIEELTKICDE 1061
Cdd:TIGR02168  397 --------SLNNEIERLEArlerLEDRRERLQQEIEELLKKLEE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
868-1066 2.09e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.69  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  868 LDSALQIARAEIITKE-REVSEWKDKYEESRREVMEMRKIVAEYEKtiaqmIEDEQREKSVSHQTVQQLVLEKEQALADL 946
Cdd:COG4717     47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  947 nSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 1026
Cdd:COG4717    122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQD 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1370456167 1027 HQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKM 1066
Cdd:COG4717    197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
797-1065 2.94e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  797 QKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAhptdvsisKTALYSRigTAEVEkpagllfqqpDLDSALQIAR 876
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELEEL--ELELE----------EAQAEEYELL 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  877 AEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVEKSLADL 956
Cdd:COG1196    295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELAEAEEALLEA 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  957 FRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAHQASLRKE 1034
Cdd:COG1196    371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEAAEE 450
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1370456167 1035 QLRVDALERTLEQKNKEIEELTKICDELIAK 1065
Cdd:COG1196    451 EAELEEEEEALLELLAELLEEAALLEAALAE 481
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
861-1057 6.21e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  861 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSV--SHQTVQQLVLE 938
Cdd:PRK03918   184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  939 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 1011
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370456167 1012 ----------EIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 1057
Cdd:PRK03918   343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
PTZ00121 PTZ00121
MAEBL; Provisional
816-1061 8.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  816 ARQIALASRSHQDAKREAAHPTD----VSISKTALYSRigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEW 889
Cdd:PTZ00121  1139 ARKAEEARKAEDAKRVEIARKAEdarkAEEARKAEDAK--KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEE 1216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  890 KDKYEESRR-----EVMEMRKIVAEYEKTIAQMIEDEQR---EKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFR 958
Cdd:PTZ00121  1217 ARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNEEIRkfeEARMAHFARRQAAIkaeEARKADELKKAEEKKKADEAK 1296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  959 RYEKMKEVLEGFRKNEEvlKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQeqaahqasLRKEQLRV 1038
Cdd:PTZ00121  1297 KAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKA 1366
                          250       260
                   ....*....|....*....|...
gi 1370456167 1039 DALERTLEQKNKEIEELTKICDE 1061
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEE 1389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
864-1065 9.45e-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: 49.38  E-value: 9.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  864 QQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIaqmiedEQREKSVSHQTVQQLVLEKEQAL 943
Cdd:COG4942     49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------EAQKEELAELLRALYRLGRQPPL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  944 ADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRyqalkvhAEEKLDRANAEIAQVRGKAQQE 1023
Cdd:COG4942    123 ALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEA-------ERAELEALLAELEEERAALEAL 193
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1370456167 1024 QAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1065
Cdd:COG4942    194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
882-1055 1.24e-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: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  882 KEREVSEWKDKYEESRREVMEMRKIVAEYEktiaQMIEDEQREKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFR 958
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  959 RYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaahqasLRKEQLRV 1038
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAEL 367
                          170
                   ....*....|....*..
gi 1370456167 1039 DALERTLEQKNKEIEEL 1055
Cdd:TIGR02168  368 EELESRLEELEEQLETL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
856-1048 1.44e-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: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  856 EKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMiEDEQREKSVSHQTVQQL 935
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-ESRLEELEEQLETLRSK 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  936 VLEKEQALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 1010
Cdd:TIGR02168  388 VAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1370456167 1011 AEIAQVRgkaqQEQAAHQASLRKEQLRVDALERTLEQK 1048
Cdd:TIGR02168  468 EELEEAE----QALDAAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
876-1057 1.95e-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: 48.90  E-value: 1.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  876 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKS 952
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  953 LADLfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLR 1032
Cdd:TIGR02168  756 LTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
                          170       180
                   ....*....|....*....|....*...
gi 1370456167 1033 K---EQLRVDALERTLEQKNKEIEELTK 1057
Cdd:TIGR02168  832 RiaaTERRLEDLEEQIEELSEDIESLAA 859
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
243-630 2.79e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.53  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  243 SGENLASETKTESAKTEGPSpalleETPLEPAVGPKAacPLDSESAEGVVPPASGggrvQNSPPVGRKtlPLTTapEAGE 322
Cdd:PTZ00449   492 SKKKLAPIEEEDSDKHDEPP-----EGPEASGLPPKA--PGDKEGEEGEHEDSKE----SDEPKEGGK--PGET--KEGE 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  323 VTPSDSGGQEDSPAK--GLSVRLEFDySEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPeKLDNTPASP--PR 398
Cdd:PTZ00449   557 VGKKPGPAKEHKPSKipTLSKKPEFP-KDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIP-KSPKRPESPksPK 634
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  399 SPAEPNDiPIAKgtytfdidkwDDPNFNPFSSTSKMQESPKLPqqsynFDPDTCDESVDPFktssktpsspskspasfei 478
Cdd:PTZ00449   635 RPPPPQR-PSSP----------ERPEGPKIIKSPKPPKSPKPP-----FDPKFKEKFYDDY------------------- 679
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  479 pasameangvdgdgLNKPAKKKKTPLKTMVEDVMSVCSLFDTFRVKKSPKRSPLSDPPSQdPTPAATPETPPVISavvha 558
Cdd:PTZ00449   680 --------------LDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKL-PRDEEFPFEPIGDP----- 739
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370456167  559 tdeeklavtnqkwtcmTVDLEADKQDYPQPSDLSTFVNETKFSSPTEGKQLCSQLDPHSASENPAPREPKAR 630
Cdd:PTZ00449   740 ----------------DAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEAMKR 795
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
875-1064 4.58e-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: 4.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  875 ARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIED-----EQREKSVSHQTVQQ---------LVLEKE 940
Cdd:TIGR02169  154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEKE 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  941 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRGK 1019
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLERS 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1370456167 1020 AQQEQAAHQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 1064
Cdd:TIGR02169  310 IAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
861-1054 5.70e-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: 47.37  E-value: 5.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  861 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQ-------REKSVSHQTVQ 933
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekiGELEAEIASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  934 QLVLEKEQALADLnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEE---KLDRAN 1010
Cdd:TIGR02169  308 RSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETR 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370456167 1011 AEIAQVRgKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEE 1054
Cdd:TIGR02169  385 DELKDYR-EKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
PTZ00121 PTZ00121
MAEBL; Provisional
816-1065 9.61e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 9.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  816 ARQIALASRSHQDAKREAAHPTDVSISKTALYSRigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSewkdKYEE 895
Cdd:PTZ00121  1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK----KAEE 1568
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  896 SRREvmEMRKIVAEYEKTIAQMIEdEQREKSVSHQTVQQLVLEKEQALADlnSVEKSLADLFRRYEKMKEVLEGFRKNEE 975
Cdd:PTZ00121  1569 AKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  976 VLKRCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQAAHQASLRKEQlrvdALERTLEQKNKeIEEL 1055
Cdd:PTZ00121  1644 EEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAE----ALKKEAEEAKK-AEEL 1707
                          250
                   ....*....|
gi 1370456167 1056 TKICDELIAK 1065
Cdd:PTZ00121  1708 KKKEAEEKKK 1717
PTZ00121 PTZ00121
MAEBL; Provisional
807-1057 9.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 9.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  807 IMRIEALKLARQIALASRSHQDAKREAAHPTDVSISKTALYSRIgtAEVEKpaglLFQQPDLDSALQIARAEiitKEREV 886
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMK----LYEEEKKMKAEEAKKAE---EAKIK 1621
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  887 SEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMK 964
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEA 1701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  965 EVLEGFRKNEEVLKRCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAHQASLRKEQLR 1037
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEA 1779
                          250       260
                   ....*....|....*....|..
gi 1370456167 1038 V--DALERTLEQKNKEIEELTK 1057
Cdd:PTZ00121  1780 VieEELDEEDEKRRMEVDKKIK 1801
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
871-1055 1.14e-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: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  871 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKI----------------VAEYEKTIAQmIEDEQREKSVSHQTVQQ 934
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  935 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 1014
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1370456167 1015 QvrgkaqqeqaahqaSLRKeqlRVDALERTLEQKNKEIEEL 1055
Cdd:COG4913    769 E--------------NLEE---RIDALRARLNRAEEELERA 792
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
799-1017 1.40e-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: 46.21  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  799 LQEELEFAIMRIEALKlaRQIALASRSHQDAKREAAHpTDVSISKT-----ALYSRIGTAEVEKPAgllfqqpdLDSALQ 873
Cdd:TIGR02169  292 VKEKIGELEAEIASLE--RSIAEKERELEDAEERLAK-LEAEIDKLlaeieELEREIEEERKRRDK--------LTEEYA 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  874 IARAEIITKEREVSEWKDKYEESRREVMEMRKivaEYEKTIAQMiEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSL 953
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREI-NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370456167  954 ADLfrrYEKMKEVLEGFRKNEEVLKRCAQEylsrVKKEEQRYQALKvhaeEKLDRANAEIAQVR 1017
Cdd:TIGR02169  437 NEL---EEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLK----EEYDRVEKELSKLQ 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
873-1037 5.37e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  873 QIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQ-TVQQLVLEKEQALADLNSVEK 951
Cdd:COG4717     67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPE 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  952 SLADLFRRYEKMKEVLEGFRKNEEVLKRCAQE--------------YLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVR 1017
Cdd:COG4717    147 RLEELEERLEELRELEEELEELEAELAELQEEleelleqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
                          170       180
                   ....*....|....*....|
gi 1370456167 1018 GKAQQEQAAHQASLRKEQLR 1037
Cdd:COG4717    227 EELEQLENELEAAALEERLK 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
786-989 6.16e-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: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  786 DLAEKNPPLFAQKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAHPTDvsiSKTALYSRIGTAEvEKPAGLLFQQ 865
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE---ELQRLSEELADLN-AAIAGIEAKI 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  866 PDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQA 942
Cdd:TIGR02169  437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqreLAEAEAQARASEERVRGGRAVEEVL 516
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370456167  943 LADLNSVEKSLADLFR---RYEKMKEVLEGFR------KNEEVLKRCAqEYLSRVK 989
Cdd:TIGR02169  517 KASIQGVHGTVAQLGSvgeRYATAIEVAAGNRlnnvvvEDDAVAKEAI-ELLKRRK 571
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
854-1062 9.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  854 EVEKPAGLLFQQPdldSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQ 933
Cdd:PRK03918   311 EIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  934 QLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLK----RCA-----------QEYLSRVKKEEQRYQAL 998
Cdd:PRK03918   388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgKCPvcgrelteehrKELLEEYTAELKRIEKE 467
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370456167  999 KVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 1062
Cdd:PRK03918   468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
876-1062 9.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 9.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  876 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAE------YEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSV 949
Cdd:PRK03918   458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  950 EKSLADLFRRYEKMKE-------VLEGFRKNEE----VLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 1018
Cdd:PRK03918   538 KGEIKSLKKELEKLEElkkklaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1370456167 1019 kaqQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 1062
Cdd:PRK03918   612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
872-1013 3.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  872 LQIARAEIITKEREVSEWKDKYEESRREVMEMRKI--VAEYEKtiaqmIEDEQREKSVSHQTVQQlvlEKEQALADLNSV 949
Cdd:PRK03918   621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370456167  950 EKSLADLFRRYEKMKEVlegfRKNEEVLKRcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 1013
Cdd:PRK03918   693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
932-1056 5.08e-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: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  932 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVLKRC---AQEYLS-RVKKEEQRYQALKVH---AEE 1004
Cdd:COG4913    213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLEPIrelAERYAAaRERLAELEYLRAALRlwfAQR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370456167 1005 KLDRANAEIAQVRGKaqqeqaahqasLRKEQLRVDALERTLEQKNKEIEELT 1056
Cdd:COG4913    289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
PTZ00121 PTZ00121
MAEBL; Provisional
809-1065 6.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  809 RIEALKLARQialASRSHQDAKR--------EAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEII 880
Cdd:PTZ00121  1225 KAEAVKKAEE---AKKDAEEAKKaeeernneEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  881 TKEREV---SEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNSVEKSLAD 955
Cdd:PTZ00121  1302 KKADEAkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekKKEEAKKKAD 1381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  956 LFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRgKAQQEQAAHQASLRK 1033
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAK-KADEAKKKAEEAKKA 1459
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1370456167 1034 EQLRVDALERTLEQKNKEIEELTKICDELIAK 1065
Cdd:PTZ00121  1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
862-1054 7.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 7.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  862 LFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEyektIAQMIEDEQREKSVSHQTVQQLVLEKEQ 941
Cdd:COG4372     37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----LNEQLQAAQAELAQAQEELESLQEEAEE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  942 ALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEIAQV---- 1016
Cdd:COG4372    113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELlkea 192
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1370456167 1017 -RGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEE 1054
Cdd:COG4372    193 nRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
790-982 7.17e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  790 KNPPLFAQKLqEELEfaimriEALKLARQIALASRSHQDAKREA-AHPTDVSISKTALYSRIGTAEVEKPAGLLFQQpdl 868
Cdd:COG4717     64 RKPELNLKEL-KELE------EELKEAEEKEEEYAELQEELEELeEELEELEAELEELREELEKLEKLLQLLPLYQE--- 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  869 dsaLQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNS 948
Cdd:COG4717    134 ---LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370456167  949 VEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQ 982
Cdd:COG4717    211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
868-1062 7.43e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 7.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  868 LDSALQIARAEIitkeREVSEW-KDKYEESRREVMEMRKIVAEYEKtiAQMIEDEQREKSVSHQTVQQLVLEKEQALADL 946
Cdd:COG3206    162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  947 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkrcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 1023
Cdd:COG3206    236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1370456167 1024 QAAHQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 1062
Cdd:COG3206    311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
879-1064 7.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  879 IITKEREVSEWKDKYE-----ESRREVMEMRKIVA---EYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNS 948
Cdd:PRK03918   488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDE 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456167  949 VEKSLADLFRRYEKmkevlEGFRKNEEV------LKRCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANAEI 1013
Cdd:PRK03918   568 LEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEKRL 642
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1370456167 1014 AQVRGK----AQQEQAAHQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 1064
Cdd:PRK03918   643 EELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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