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Conserved domains on  [gi|1131298191|ref|XP_019811297|]
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PREDICTED: angiomotin isoform X4 [Bos indicus]

Protein Classification

Smc and Angiomotin_C domain-containing protein( domain architecture ID 10573751)

Smc and Angiomotin_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 190-397 2.10e-105

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


:

Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 318.64  E-value: 2.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 190 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 269
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 270 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 349
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131298191 350 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 397
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-268 4.42e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  24 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 100
Cdd:COG1196   236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 101 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 180
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 181 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 260
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471


                  ....*...
gi 1131298191 261 RILALEAD 268
Cdd:COG1196   472 AALLEAAL 479
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 190-397 2.10e-105

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 318.64  E-value: 2.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 190 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 269
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 270 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 349
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131298191 350 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 397
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-268 4.42e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  24 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 100
Cdd:COG1196   236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 101 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 180
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 181 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 260
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471


                  ....*...
gi 1131298191 261 RILALEAD 268
Cdd:COG1196   472 AALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 76-370 1.46e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  76 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 148
Cdd:COG1196   174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 149 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 228
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 229 LRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 308
Cdd:COG1196   321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131298191 309 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 370
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 51-276 1.61e-07

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: 54.69  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   51 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQ 130
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  131 LFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 208
Cdd:TIGR02169  397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298191  209 EKREQLEHRLRT---RLERELESLRIQQRQGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQKY 276
Cdd:TIGR02169  465 SKYEQELYDLKEeydRVEKELSKLQRELAEAEAQARASEERvrGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-372 1.12e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   52 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQL 131
Cdd:TIGR02168  171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  132 FAKNKESQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 211
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  212 EQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 291
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEE------------- 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  292 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 371
Cdd:TIGR02168  370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427


                   .
gi 1131298191  372 S 372
Cdd:TIGR02168  428 K 428
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-284 8.68e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  20 AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEG- 90
Cdd:PRK03918  129 AIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  91 --EIRRMHDFNRDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEirdq 168
Cdd:PRK03918  206 lrEINEISSELPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE---- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 169 alsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacekreQLEHRLrTRLERELESLRIQQRQGNSQPTNVSEyna 248
Cdd:PRK03918  277 ---ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRL-SRLEEEINGIEERIKELEEKEERLEE--- 342

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1131298191 249 aaLMEILREKEERILALEADMTKWEQ-KYLEENVMRH 284
Cdd:PRK03918  343 --LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-274 5.03e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   20 AIVSRAQQMVEILSDENRNLRQE-LEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRRMHD 97
Cdd:pfam12128  315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAG 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   98 FNRDLRERLETANKQLAEKE--YEGSEDTRKtiSQLFAKNKESQREKEKLEAELATARSTnedqrrhieirdqalsnaQA 175
Cdd:pfam12128  395 IKDKLAKIREARDRQLAVAEddLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLR------------------LN 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  176 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEynaaaLMEIL 255
Cdd:pfam12128  455 QATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQL 529

                          250       260
                   ....*....|....*....|
gi 1131298191  256 REKEERILA-LEADMTKWEQ 274
Cdd:pfam12128  530 FPQAGTLLHfLRKEAPDWEQ 549
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 190-397 2.10e-105

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 318.64  E-value: 2.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 190 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 269
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 270 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 349
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1131298191 350 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 397
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-268 4.42e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  24 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 100
Cdd:COG1196   236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 101 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 180
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 181 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 260
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471


                  ....*...
gi 1131298191 261 RILALEAD 268
Cdd:COG1196   472 AALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 76-370 1.46e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  76 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 148
Cdd:COG1196   174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 149 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 228
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 229 LRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 308
Cdd:COG1196   321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131298191 309 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 370
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 51-276 1.61e-07

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: 54.69  E-value: 1.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   51 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQ 130
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  131 LFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 208
Cdd:TIGR02169  397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298191  209 EKREQLEHRLRT---RLERELESLRIQQRQGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQKY 276
Cdd:TIGR02169  465 SKYEQELYDLKEeydRVEKELSKLQRELAEAEAQARASEERvrGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-237 3.45e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   17 DPFAIVSRAQQMVEILSDENRnLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 92
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   93 RRmhdfnrdLRERLETANKQLAEKEyEGSEDTRKTISQLF-AKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALS 171
Cdd:COG4913    298 EE-------LRAELARLEAELERLE-ARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131298191  172 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 237
Cdd:COG4913    370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-271 3.91e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   24 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 95
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   96 HDFNRDLRERLETANKQLAEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 175
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  176 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQgnsqptnvseynaaaLM 252
Cdd:TIGR02168  839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEE---------------LS 900

                          250
                   ....*....|....*....
gi 1131298191  253 EILREKEERILALEADMTK 271
Cdd:TIGR02168  901 EELRELESKRSELRRELEE 919
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
41-220 1.04e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  41 QELEGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRERLETANKQLAE--K 116
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 117 EYEGSEDTRKTISQLFAKNKESQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 195
Cdd:COG4717   147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226

                         170       180
                  ....*....|....*....|....*
gi 1131298191 196 KMQQALVQLQAACEKREQLEHRLRT 220
Cdd:COG4717   227 EELEQLENELEAAALEERLKEARLL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-372 1.12e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   52 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQL 131
Cdd:TIGR02168  171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  132 FAKNKESQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 211
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  212 EQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 291
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEE------------- 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  292 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 371
Cdd:TIGR02168  370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427


                   .
gi 1131298191  372 S 372
Cdd:TIGR02168  428 K 428
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
110-280 2.69e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 110 NKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 187
Cdd:COG4717    65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 188 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NVSEYNAAALMEILREKEERILA 264
Cdd:COG4717   145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224

                         170
                  ....*....|....*.
gi 1131298191 265 LEADMTKWEQKYLEEN 280
Cdd:COG4717   225 LEEELEQLENELEAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-284 8.68e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  20 AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEG- 90
Cdd:PRK03918  129 AIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  91 --EIRRMHDFNRDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEirdq 168
Cdd:PRK03918  206 lrEINEISSELPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE---- 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 169 alsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacekreQLEHRLrTRLERELESLRIQQRQGNSQPTNVSEyna 248
Cdd:PRK03918  277 ---ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRL-SRLEEEINGIEERIKELEEKEERLEE--- 342

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1131298191 249 aaLMEILREKEERILALEADMTKWEQ-KYLEENVMRH 284
Cdd:PRK03918  343 --LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 33-235 1.24e-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: 47.84  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  33 SDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQ 112
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 113 LAEKEYEGSEDTR---KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 189
Cdd:COG4942    99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1131298191 190 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 235
Cdd:COG4942   179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-275 1.50e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   51 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRERLETANKQLAEKEYEgsedtRKTISQ 130
Cdd:COG4913    225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYL-----RAALRL 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  131 LFAknkesQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 210
Cdd:COG4913    284 WFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298191  211 REqlehRLRTRLERELESLriqqrqGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQK 275
Cdd:COG4913    357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-278 1.58e-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: 48.51  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   38 NLRQELEGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQlAEKE 117
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELE-QLRKELEELSRQISALRKDLARLEAE-VEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  118 YEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 197
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  198 QQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNVSEYNAAALMEILREKEERILA 264
Cdd:TIGR02168  826 LESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEELRE 905

                          250
                   ....*....|....
gi 1131298191  265 LEADMTKWEQKYLE 278
Cdd:TIGR02168  906 LESKRSELRRELEE 919
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 19-235 1.91e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   19 FAIVSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRM 95
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   96 HDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 175
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131298191  176 KVVKLEEELKKKQVYVDKVEKMQQALVQ---------LQAACEKREQLEHRLRTRLERELESLRIQQRQ 235
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEELREE 469
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-364 6.46e-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: 46.20  E-value: 6.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   39 LRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKE 117
Cdd:TIGR02168  194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  118 YEGSEDtRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 197
Cdd:TIGR02168  274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  198 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKY 276
Cdd:TIGR02168  353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  277 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 356
Cdd:TIGR02168  424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497


                   ....*...
gi 1131298191  357 QQRSRKEP 364
Cdd:TIGR02168  498 QENLEGFS 505
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 26-377 1.01e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.58  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  26 QQMVEILSDENRNLRQELEGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 94
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  95 MHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKE-------------KLEAELATARSTNEDQRR 161
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 162 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 241
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 242 NVSEYNAAALMEILREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 320
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298191 321 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 377
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-224 1.07e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   21 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklEGEIRRmhdfNR 100
Cdd:COG4913    604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LE 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  101 DLRERLETANKQLAEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQAKVVKL 180
Cdd:COG4913    675 AELERLDASSDDLAALE-EQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRA 749

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1131298191  181 EEELKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 224
Cdd:COG4913    750 LLEERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-176 3.80e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  32 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE------KAMRNKLEgEIRRMHDFNRDLRER 105
Cdd:COG4717    93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperlEELEERLE-ELRELEEELEELEAE 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131298191 106 LETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAK 176
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
57-164 4.44e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  57 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNK 136
Cdd:COG2433   387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE-LSEARSEERREIRKDR 465

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1131298191 137 E---SQREKEKLEAELATARSTNEDQRRHIE 164
Cdd:COG2433   466 EisrLDREIERLERELEEERERIEELKRKLE 496
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
30-270 7.56e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  30 EILSDENRNLRQELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRERL 106
Cdd:PRK02224  310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 107 ETANKQL--AEKEYEGSEDTR---KTISQLFAKNKESQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 167
Cdd:PRK02224  387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 168 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRL---RTRLERE---LESLRIQQ 233
Cdd:PRK02224  467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIaerRETIEEKrerAEELRERA 546

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1131298191 234 RQGNSQpTNVSEYNAAALMEILREKEERILALEADMT 270
Cdd:PRK02224  547 AELEAE-AEEKREAAAEAEEEAEEAREEVAELNSKLA 582
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
74-271 1.36e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  74 SSKREALEKamrnkLEGEIRRMHDfnRDLRERLETANKQLAE-----KEYEGSED----TRKTISQLFAKNKESQREKEK 144
Cdd:PRK02224  183 SDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqareTRDEADEVLEEHEERREELET 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 145 LEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREqlehrlrTRLER 224
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-------EELRD 328

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1131298191 225 ELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTK 271
Cdd:PRK02224  329 RLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-268 1.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  32 LSDENRNLRQELEGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 97
Cdd:PRK02224  410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  98 FNRDLRERLETANK-QLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 176
Cdd:PRK02224  490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 177 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNVSEYnaaa 250
Cdd:PRK02224  561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628

                         250
                  ....*....|....*...
gi 1131298191 251 lmeiLREKEERILALEAD 268
Cdd:PRK02224  629 ----LAEKRERKRELEAE 642
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-229 1.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  41 QELEGCYEKVARLQKVETEIQRVSEAYENLvkssskREALEKA--MRNKLEGEIRRmhdfnrdLRERLETANKQLAEKEY 118
Cdd:PRK03918  595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKAfeELAETEKRLEE-------LRKELEELEKKYSEEEY 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 119 EGSEDtrktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHieiRDQALSNAQakvvKLEEELKKKQVYVDKVEKMQ 198
Cdd:PRK03918  662 EELRE-----------------EYLELSRELAGLRAELEELEKR---REEIKKTLE----KLKEELEEREKAKKELEKLE 717

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1131298191 199 QALVQLQAACEKREQLEHRLRTRLERELESL 229
Cdd:PRK03918  718 KALERVEELREKVKKYKALLKERALSKVGEI 748
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 25-266 1.84e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  25 AQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE------IRRMHDF 98
Cdd:COG5185   303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEvelsksSEELDSF 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  99 N---RDLRERLETANKQLAEKEYEGSEDTRKTIsqlfaknKESQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 175
Cdd:COG5185   383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 176 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEIL 255
Cdd:COG5185   452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531

                         250
                  ....*....|.
gi 1131298191 256 REKEERILALE 266
Cdd:COG5185   532 ARGYAHILALE 542
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-367 3.03e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 138 SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQAL-VQLQAACEKREQLEH 216
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 217 RLRTRLERELESLRIQQRQGNSQPTNV---------SEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFAL 287
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 288 DAAATVAAQRdttvishspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKT 367
Cdd:COG4942   178 ALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
PRK12704 PRK12704
phosphodiesterase; Provisional
 107-229 3.13e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 107 ETANKQLAEKEYEGSEDTRKTISQLfakNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKK 186
Cdd:PRK12704   38 EEAKRILEEAKKEAEAIKKEALLEA---KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1131298191 187 KQvyvDKVEKMQQALVQLQAACEKreqlehrLRTRLERELESL 229
Cdd:PRK12704  115 KE---KELEQKQQELEKKEEELEE-------LIEEQLQELERI 147
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 52-235 3.67e-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: 39.52  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  52 RLQKVETEIQRVseayenlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRERLETANKQLAEKEyEGSEDTRKTISQL 131
Cdd:COG1579    11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 132 FAKNKESQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 211
Cdd:COG1579    65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136

                         170       180
                  ....*....|....*....|....
gi 1131298191 212 EQLEHRLRTRLERELESLRIQQRQ 235
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEE 160
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 20-274 5.03e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   20 AIVSRAQQMVEILSDENRNLRQE-LEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRRMHD 97
Cdd:pfam12128  315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAG 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   98 FNRDLRERLETANKQLAEKE--YEGSEDTRKtiSQLFAKNKESQREKEKLEAELATARSTnedqrrhieirdqalsnaQA 175
Cdd:pfam12128  395 IKDKLAKIREARDRQLAVAEddLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLR------------------LN 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  176 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEynaaaLMEIL 255
Cdd:pfam12128  455 QATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQL 529

                          250       260
                   ....*....|....*....|
gi 1131298191  256 REKEERILA-LEADMTKWEQ 274
Cdd:pfam12128  530 FPQAGTLLHfLRKEAPDWEQ 549
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
75-276 5.57e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  75 SKREALEKAmRNKLEGEIRRmhdfnrdLRERLETANKQLAE-KEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATAR 153
Cdd:COG3206   168 LRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 154 STNEDQRRHIE---------IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLE 223
Cdd:COG3206   240 ARLAALRAQLGsgpdalpelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1131298191 224 RELESLRIQQRQGNSQptnVSEYNAAALMeiLREKEERILALEADMTKWEQKY 276
Cdd:COG3206   320 AELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 32-279 6.38e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 39.67  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  32 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRER 105
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 106 LETANKQLAEKEYEGSEDTRKTISQLF------AKNKESQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 171
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191 172 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 231
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1131298191 232 QQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKwEQKYLEE 279
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 22-185 8.00e-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: 39.65  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191   22 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 101
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298191  102 LRERLETANKQLAEkeyegSEDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVKLE 181
Cdd:TIGR02168  913 LRRELEELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKRLE 978


                   ....
gi 1131298191  182 EELK 185
Cdd:TIGR02168  979 NKIK 982
 
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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