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Conserved domains on  [gi|125821657|ref|XP_683317|]
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protein GOLM2 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-233 5.33e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKdgdysALQNKLQARDALVKTCTDDKNKLQndvs 117
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSDDLA---- 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  118 aqmseihRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEyeslQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:COG4913   689 -------ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 125821657  198 RNADSVVQHVDLDLDQSNKR-KEKEDTAERHTVAARR 233
Cdd:COG4913   758 ALGDAVERELRENLEERIDAlRARLNRAEEELERAMR 794
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-233 5.33e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKdgdysALQNKLQARDALVKTCTDDKNKLQndvs 117
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSDDLA---- 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  118 aqmseihRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEyeslQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:COG4913   689 -------ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 125821657  198 RNADSVVQHVDLDLDQSNKR-KEKEDTAERHTVAARR 233
Cdd:COG4913   758 ALGDAVERELRENLEERIDAlRARLNRAEEELERAMR 794
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
41-191 7.83e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 7.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    41 RLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCT-------DDKNKLQ 113
Cdd:pfam15921  696 KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKNKLS 775
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125821657   114 NDVSAQMSEIHRLKEQVKELRQevirqedQQREVRKNSTNLEKKLEYESLQCgrqiaelkAEYEESKKRVEEEAAKLR 191
Cdd:pfam15921  776 QELSTVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALDKASLQF--------AECQDIIQRQEQESVRLK 838
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-234 4.91e-04

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: 42.74  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    35 VSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDA-------LVKTCTD 107
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeELAEAEA 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   108 DKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGR----------QIAELKAEYE 177
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqieelseDIESLAAEIE 862
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 125821657   178 ESKKRVEEEAAKLrQSLLENRnaDSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRN 234
Cdd:TIGR02168  863 ELEELIEELESEL-EALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRE 916
PTZ00121 PTZ00121
MAEBL; Provisional
44-226 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKT-----------CTDDKNK- 111
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkAEEDKNMa 1579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  112 ------LQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQR----------EVRKNSTNLEKKLEYESlqcgRQIAELKAE 175
Cdd:PTZ00121 1580 lrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeEEKKKVEQLKKKEAEEK----KKAEELKKA 1655
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 125821657  176 YEESKKRVEEEAAKLRQsllENRNADSVVQHVDLDLDQSNKRKEKEDTAER 226
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
38-267 1.65e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.97  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQidLKDGDYSALQNKLQA-RDALVKTctddknklQNDV 116
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALETNGQAqRDAILEE--------SRAV 1618
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNS--TNLEKKLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSL 194
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGllDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125821657  195 LenrNADSVVQHVDLDLDQS-NKRKEKEDTAerhtvAARRNDVPVLKDDLGKPGSDAGMPGIEDSEVGKIDDSQ 267
Cdd:NF012221 1699 A---QGEQNQANAEQDIDDAkADAEKRKDDA-----LAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
12-151 7.10e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 37.95  E-value: 7.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  12 RLPSFILIALLVVIVILSF-----NYWSVSTkharllDELAEVQTQVkrtDAARSRLEKRNSELmmQVDTHRKQID--LK 84
Cdd:NF038305  77 RFLSWILSLLLGLLFLLLIplhlnNTRRLST------QALQQINQQA---GQQETQLQQQLNQL--QAQTSPQQLNqlLK 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125821657  85 DGDYSALQNKLQARDALVKtctDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQedQQREVRKNS 151
Cdd:NF038305 146 SEQKQGQALASGQLPEEQK---EQLQQFKSNPQALDKFLAQQLTQIRTQAEEAEKQ--ARLEALKSS 207
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
38-233 5.33e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKdgdysALQNKLQARDALVKTCTDDKNKLQndvs 117
Cdd:COG4913   618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSDDLA---- 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  118 aqmseihRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEyeslQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:COG4913   689 -------ALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 125821657  198 RNADSVVQHVDLDLDQSNKR-KEKEDTAERHTVAARR 233
Cdd:COG4913   758 ALGDAVERELRENLEERIDAlRARLNRAEEELERAMR 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-219 3.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  40 ARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESlqcgRQIAELKAEYEESKKRVEEEAAKLRQSLLENRN 199
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
                        170       180
                 ....*....|....*....|
gi 125821657 200 ADSVVQHVDLDLDQSNKRKE 219
Cdd:COG1196  475 LEAALAELLEELAEAAARLL 494
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
41-191 7.83e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.58  E-value: 7.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    41 RLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCT-------DDKNKLQ 113
Cdd:pfam15921  696 KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANkekhflkEEKNKLS 775
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125821657   114 NDVSAQMSEIHRLKEQVKELRQevirqedQQREVRKNSTNLEKKLEYESLQCgrqiaelkAEYEESKKRVEEEAAKLR 191
Cdd:pfam15921  776 QELSTVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALDKASLQF--------AECQDIIQRQEQESVRLK 838
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-248 2.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  40 ARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLE 196
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 125821657 197 NRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRNDVPVLKDDLGKPGS 248
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
21-231 3.95e-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: 45.53  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  21 LLVVIVILSFNYWSVSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDA 100
Cdd:COG4942    4 LLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 101 LVKTCTDDKNKLQNDVSAQMSEI--------------------------------HRLKEQVKELRQEVIRQEDQQREVR 148
Cdd:COG4942   84 ELAELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 149 KNSTNLEKKL-EYESLQcgRQIAELKAEYEESKKRVEEEAAKLRQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERH 227
Cdd:COG4942  164 ALRAELEAERaELEALL--AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                 ....
gi 125821657 228 TVAA 231
Cdd:COG4942  242 RTPA 245
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
40-234 4.17e-05

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: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  40 ARLLDELAEVQTQVKRTDAARSRLEKRNsELMMQVDTHRKQIDLKDgdYSALQNKLQARDALVKTCTDDKNKLQNDVSAQ 119
Cdd:COG1196  189 ERLEDILGELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAEL 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 120 MSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESL---QCGRQIAELKAEYEESKKRVEEEAAKLRQSLLE 196
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEE 345
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 125821657 197 NRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRN 234
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
38-226 5.24e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  38 KHARLLDELAEVQTQVKRTDAARSR---LEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKtctddKNKLQN 114
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 115 DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAEYEEskkrVEEEAAKLRQSL 194
Cdd:COG4717  140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----LQQRLAELEEEL 215
                        170       180       190
                 ....*....|....*....|....*....|..
gi 125821657 195 LENRNAdsvVQHVDLDLDQSNKRKEKEDTAER 226
Cdd:COG4717  216 EEAQEE---LEELEEELEQLENELEAAALEER 244
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
38-196 7.17e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQN--- 114
Cdd:COG1579    4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 115 ------DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKL-----EYESLQCGRQ--IAELKAEYEESKK 181
Cdd:COG1579   84 nvrnnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELaeleaELEEKKAELDeeLAELEAELEELEA 163
                        170
                 ....*....|....*
gi 125821657 182 RVEEEAAKLRQSLLE 196
Cdd:COG1579  164 EREELAAKIPPELLA 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-196 1.35e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   30 FNYWSVSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGD-YSALQNKLQARDALVKTCTDD 108
Cdd:COG4913   281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERR 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  109 KNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAE---YEESKKRVEE 185
Cdd:COG4913   361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiasLERRKSNIPA 440
                         170
                  ....*....|.
gi 125821657  186 EAAKLRQSLLE 196
Cdd:COG4913   441 RLLALRDALAE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-234 4.91e-04

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: 42.74  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    35 VSTKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDA-------LVKTCTD 107
Cdd:TIGR02168  703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeELAEAEA 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   108 DKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGR----------QIAELKAEYE 177
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqieelseDIESLAAEIE 862
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 125821657   178 ESKKRVEEEAAKLrQSLLENRnaDSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRN 234
Cdd:TIGR02168  863 ELEELIEELESEL-EALLNER--ASLEEALALLRSELEELSEELRELESKRSELRRE 916
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
40-220 5.08e-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: 42.75  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    40 ARLLDELAEVQTQVKRTDA--ARSRLEKRNSELMMQVDTHRK---QIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQN 114
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   115 DVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLR 191
Cdd:TIGR02169  848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 125821657   192 ------QSLLENRNADSVVQHVDLDLDQSNKRKEK 220
Cdd:TIGR02169  928 aleeelSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
45-233 5.31e-04

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: 42.35  E-value: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    45 ELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQardalvktctddknKLQNDVSAQMSEIH 124
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE--------------ELKEELESLEAELE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   125 RLKEQVKELrqevirqEDQQREVRKNSTNLEKKLeyesLQCGRQIAELKAE---YEESKKRVEEEAAKLRQSLLENRNAD 201
Cdd:TIGR02168  362 ELEAELEEL-------ESRLEELEEQLETLRSKV----AQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKL 430
                          170       180       190
                   ....*....|....*....|....*....|..
gi 125821657   202 SVVQHVDLDLDQSNKRKEKEDTAERHTVAARR 233
Cdd:TIGR02168  431 EEAELKELQAELEELEEELEELQEELERLEEA 462
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-233 5.85e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  37 TKHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDV 116
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLE----------YESLQCGRQIAELKAEYEESKKRVEEE 186
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaeeeleelaEELLEALRAAAELAAQLEELEEAEEAL 412
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 125821657 187 AAKLRQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARR 233
Cdd:COG1196  413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
45-243 6.46e-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: 42.36  E-value: 6.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    45 ELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDK-NKLQNDVSAQMSEI 123
Cdd:TIGR02169  224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   124 HRLKEQVKELRQEVIRQEDQQRE-------VRKNSTNLEKKLEYESL---QCGRQIAELKAEYEESKKRVEEEAAK---L 190
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEERKrrdKLTEEYAELKEELEDLRAELEEVDKEfaeT 383
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 125821657   191 RQSLLENRNADSVVQHVDLDLDQSNKRKEKEDTAERHTVAARRNDVPVLKDDL 243
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
37-192 1.17e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657    37 TKHArLLDELAEVQTQVKRTDAARSRLEKRNSELMMQV--------DTHRKQIDLKDgDYSALQNKLQARDALVKTCTDD 108
Cdd:pfam01576  378 AKQA-LESENAELQAELRTLQQAKQDSEHKRKKLEGQLqelqarlsESERQRAELAE-KLSKLQSELESVSSLLNEAEGK 455
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   109 KNKLQNDVSAQMSEIHrlkeQVKELRQEVIRQE----DQQREVRKNSTNLEKKLEYESL---QCGRQIAELKAEYEESKK 181
Cdd:pfam01576  456 NIKLSKDVSSLESQLQ----DTQELLQEETRQKlnlsTRLRQLEDERNSLQEQLEEEEEakrNVERQLSTLQAQLSDMKK 531
                          170
                   ....*....|.
gi 125821657   182 RVEEEAAKLRQ 192
Cdd:pfam01576  532 KLEEDAGTLEA 542
PTZ00121 PTZ00121
MAEBL; Provisional
44-226 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKT-----------CTDDKNK- 111
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakkAEEDKNMa 1579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  112 ------LQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQR----------EVRKNSTNLEKKLEYESlqcgRQIAELKAE 175
Cdd:PTZ00121 1580 lrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeEEKKKVEQLKKKEAEEK----KKAEELKKA 1655
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 125821657  176 YEESKKRVEEEAAKLRQsllENRNADSVVQHVDLDLDQSNKRKEKEDTAER 226
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
38-267 1.65e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 40.97  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   38 KHARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQidLKDGDYSALQNKLQA-RDALVKTctddknklQNDV 116
Cdd:NF012221 1549 KHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALETNGQAqRDAILEE--------SRAV 1618
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNS--TNLEKKLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSL 194
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGllDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125821657  195 LenrNADSVVQHVDLDLDQS-NKRKEKEDTAerhtvAARRNDVPVLKDDLGKPGSDAGMPGIEDSEVGKIDDSQ 267
Cdd:NF012221 1699 A---QGEQNQANAEQDIDDAkADAEKRKDDA-----LAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
42-192 2.20e-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: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  42 LLDELAEVQTQVKRTDAARSRLEKRN---------SELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKL 112
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 113 QNDVSAQM--SEIHRLKEQVKELRQ-------EVIRQEDQQREVRKNSTNLEKKL------EYESLQcgRQIAELKAEYE 177
Cdd:COG3206  260 LQSPVIQQlrAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIlasleaELEALQ--AREASLQAQLA 337
                        170
                 ....*....|....*
gi 125821657 178 ESKKRVEEEAAKLRQ 192
Cdd:COG3206  338 QLEARLAELPELEAE 352
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
42-189 2.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  42 LLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDgDYSALQNKLQARDALVKTCTDDKNKLQND-----V 116
Cdd:COG4717  342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELlgeleE 420
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125821657 117 SAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKLEYesLQCGRQIAELKAEYEESKKRVEEEAAK 189
Cdd:COG4717  421 LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEE 491
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
40-196 2.33e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.12  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   40 ARLLDELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQI--------DLKDgDYSALQNKLQARDALVKTCTDDKNK 111
Cdd:pfam15619  28 EELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVrvlrerlrRLQE-KERDLERKLKEKEAELLRLRDQLKR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  112 LQNDVSAQ-MSEIHRLKEQVKELRQEVirqEDQQREVRknstNLEKKLEYESLQCGRQIAELKAEYEESKKRV---EEEA 187
Cdd:pfam15619 107 LEKLSEDKnLAEREELQKKLEQLEAKL---EDKDEKIQ----DLERKLELENKSFRRQLAAEKKKHKEAQEEVkilQEEI 179

                  ....*....
gi 125821657  188 AKLRQSLLE 196
Cdd:pfam15619 180 ERLQQKLKE 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
121-235 2.44e-03

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: 40.43  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   121 SEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEK---KLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQSLLEN 197
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 125821657   198 RNADSVVQHVDLDLDQSNKRKeKEDTAERHTVAARRND 235
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEEL-AEAEAEIEELEAQIEQ 793
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
113-192 2.61e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.23  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 113 QNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKKL------EYESLQCGRQIAELKAEYEESKKRVEEE 186
Cdd:COG2433  405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELsearseERREIRKDREISRLDREIERLERELEEE 484

                 ....*.
gi 125821657 187 AAKLRQ 192
Cdd:COG2433  485 RERIEE 490
PRK12704 PRK12704
phosphodiesterase; Provisional
16-185 2.71e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  16 FILIALLVVIVILSFNYW---SVSTKHARLLDELAEVQTQVKRTDAARSRLEKR---NSELMMQVDTHRKQIDLKDGDYS 89
Cdd:PRK12704   6 IILIALVALVVGAVIGYFvrkKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALleaKEEIHKLRNEFEKELRERRNELQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  90 ALQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKNSTNL-------------EK 156
Cdd:PRK12704  86 KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaeeakeillekvEE 165
                        170       180
                 ....*....|....*....|....*....
gi 125821657 157 KLEYESLQCGRQIaELKAEyEESKKRVEE 185
Cdd:PRK12704 166 EARHEAAVLIKEI-EEEAK-EEADKKAKE 192
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
73-232 3.09e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  73 QVDTHRKQIDLKDGDysaLQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQEDQQREVRKN-- 150
Cdd:COG1579   14 ELDSELDRLEHRLKE---LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657 151 STNLEKKLEYESlqcgRQIAELKAEYEESKKRVEEEAAKLR--QSLLENRNADSVVQHVDLDLDQSNKRKEKED-TAERH 227
Cdd:COG1579   91 YEALQKEIESLK----RRISDLEDEILELMERIEELEEELAelEAELAELEAELEEKKAELDEELAELEAELEElEAERE 166

                 ....*
gi 125821657 228 TVAAR 232
Cdd:COG1579  167 ELAAK 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
44-185 4.83e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKtctddknKLQNDVSAQMSEI 123
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-------KLKKENQSYKQEI 386
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125821657  124 HRLKEQVKELRQEVIRQEDQQREVRKNSTNLEKklEYESLQcgRQIAELKAEYEESKKRVEE 185
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ--EKELLE--KEIERLKETIIKNNSEIKD 444
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
12-151 7.10e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 37.95  E-value: 7.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  12 RLPSFILIALLVVIVILSF-----NYWSVSTkharllDELAEVQTQVkrtDAARSRLEKRNSELmmQVDTHRKQID--LK 84
Cdd:NF038305  77 RFLSWILSLLLGLLFLLLIplhlnNTRRLST------QALQQINQQA---GQQETQLQQQLNQL--QAQTSPQQLNqlLK 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125821657  85 DGDYSALQNKLQARDALVKtctDDKNKLQNDVSAQMSEIHRLKEQVKELRQEVIRQedQQREVRKNS 151
Cdd:NF038305 146 SEQKQGQALASGQLPEEQK---EQLQQFKSNPQALDKFLAQQLTQIRTQAEEAEKQ--ARLEALKSS 207
PTZ00121 PTZ00121
MAEBL; Provisional
54-235 7.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657   54 KRTDAARSRLEKRNSELMMQVDTHRKQIDLKDGDYSALQNKLQARDALVKTCTDDKNKLQNDVSAQMSEIHRLKEQVKEl 133
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  134 RQEVIRQEDQQREVRKNSTNLEKKLEYESLQCGRQIAELKAEYEESKKRVEEEAAKLRQ----SLLENRNADSVVQHVDL 209
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkEAEEKKKAEELKKAEEE 1727
                         170       180
                  ....*....|....*....|....*.
gi 125821657  210 DLDQSNKRKEKEDTAERHTVAARRND 235
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDE 1753
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
44-148 7.75e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 37.50  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125821657  44 DELAEVQTQVKRTDAARSRLEKRNSELMMQVDTHRKQIDLkdgdysALQnklQARDALVKTCTDDKNKLQNDVSAQMSEI 123
Cdd:COG1842   37 EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL------ALE---KGREDLAREALERKAELEAQAEALEAQL 107
                         90       100
                 ....*....|....*....|....*
gi 125821657 124 HRLKEQVKELRQEVIRQEDQQREVR 148
Cdd:COG1842  108 AQLEEQVEKLKEALRQLESKLEELK 132
 
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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