|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
329-536 |
1.98e-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: 322.49 E-value: 1.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 329 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 408
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 409 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 488
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131298189 489 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 536
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-407 |
5.98e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 239
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 240 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 319
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 320 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 399
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 1131298189 400 RILALEAD 407
Cdd:COG1196 472 AALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-415 |
7.04e-09 |
|
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: 59.70 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 190 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQ 269
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 270 LFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 347
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298189 348 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnvSEYNAAAlMEILREKEERILALEADMTKWEQKY 415
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-509 |
1.71e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 215 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 287
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 288 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 367
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 368 LRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 447
Cdd:COG1196 321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131298189 448 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 509
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-511 |
5.03e-08 |
|
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: 56.99 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 191 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQL 270
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 271 FAKNKESQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 350
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 351 EQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 430
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 431 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 510
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 1131298189 511 S 511
Cdd:TIGR02168 428 K 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-423 |
6.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 154 PADPF--AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAM 223
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 224 RNKLEG---EIRRMHDFNRDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRR 300
Cdd:PRK03918 199 EKELEEvlrEINEISSELPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 301 HIEirdqalsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacekreQLEHRLrTRLERELESLRIQQRQGNSQPT 380
Cdd:PRK03918 274 EIE-------ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRL-SRLEEEINGIEERIKELEEKEE 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1131298189 381 NVSEynaaaLMEILREKEERILALEADMTKWEQ-KYLEENVMRH 423
Cdd:PRK03918 339 RLEE-----LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-368 |
6.59e-04 |
|
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: 43.24 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 164 AQQMVEILSDENRNLRQElegcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 242
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 243 ERLETANKQLAEKEYE------GSEDTRKTISQLFAKNKESQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 309
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131298189 310 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 368
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
42-109 |
1.21e-03 |
|
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.
Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 40.54 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298189 42 SQPHSPTSSLTSGGSLPLLqsPPSTRLSPaQHPLVPNQGDHS--------AHLPRPQQHFLPNQAHQGDHYRLPQP 109
Cdd:smart00818 43 SQQHPPTHTLQPHHHIPVL--PAQQPVVP-QQPLMPVPGQHSmtptqhhqPNLPQPAQQPFQPQPLQPPQPQQPMQ 115
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
187-368 |
9.23e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.49 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 187 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrerletANKQLAEKEYEGSEDTRKT 266
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 267 ISQLFAK-NKESQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 328
Cdd:cd07596 66 LSKLGKAaEELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1131298189 329 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 368
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
329-536 |
1.98e-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: 322.49 E-value: 1.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 329 YVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADM 408
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 409 TKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALeariqkeEEEILMANKRCLDMEGRIKTLHAQIIEK 488
Cdd:pfam12240 81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSF-------NEELLLANRRCQEMENRIKNLHAQILEK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1131298189 489 DAMIKVLQQRSRKEPSKTEQlSSMRPAKSLMSISNAGSGLLSHSSTLT 536
Cdd:pfam12240 154 DAMIKVLQQRSRKDPGKTDQ-QSLRPARSVPSISAAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-407 |
5.98e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNR 239
Cdd:COG1196 236 ELEAELEELEAELEELEAELE---ELEAELAELEAELEELRLELEELeleLEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 240 DLRERLETANKQLAEKEYEGSEDTRKtISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKL 319
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 320 EEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEE 399
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
....*...
gi 1131298189 400 RILALEAD 407
Cdd:COG1196 472 AALLEAAL 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-415 |
7.04e-09 |
|
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: 59.70 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 190 ARLQKVETEIQRVSEAYENLvkssSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQ 269
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 270 LFAKNKESQREKEKLEAELatarstnedQRRHIEIRD--QALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAAC 347
Cdd:TIGR02169 397 LKREINELKRELDRLQEEL---------QRLSEELADlnAAIAGIEAKINELEEEKEDKA---LEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298189 348 EKREQLEHRLRT---RLERELESL-----RIQQRQGNSQPTnvSEYNAAAlMEILREKEERILALEADMTKWEQKY 415
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKELSKLqrelaEAEAQARASEER--VRGGRAV-EEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-509 |
1.71e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 215 KREALEK--AMRNKLEgeirRMHDFNRDLRERLETANKQlAEK-----EYEGSEDTRKtISQLFAKNKESQREKEKLEAE 287
Cdd:COG1196 174 KEEAERKleATEENLE----RLEDILGELERQLEPLERQ-AEKaeryrELKEELKELE-AELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 288 LATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKREQLEHRLRTRLERELES 367
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------AEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 368 LRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNT 447
Cdd:COG1196 321 LEEELAELEEE--------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131298189 448 SYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQL 509
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-410 |
2.82e-08 |
|
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: 57.76 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQR--------VSEAYENLVKSSSKREALEKAMRNkLEGEIRRM 234
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqISALRKDLARLEAEVEQLEERIAQ-LSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 235 HDFNRDLRERLETANKQLAEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 314
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 315 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEK-REQLEHRL--RTRLERELESLRIQQRQgnsqptnvseynaaaLM 391
Cdd:TIGR02168 839 RLEDLEEQIEELS---EDIESLAAEIEELEELIEElESELEALLneRASLEEALALLRSELEE---------------LS 900
|
250
....*....|....*....
gi 1131298189 392 EILREKEERILALEADMTK 410
Cdd:TIGR02168 901 EELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-511 |
5.03e-08 |
|
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: 56.99 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 191 RLQKVETEiQRVSEAYENLVKSSSKREALEKAMrNKLEGEIRRMHDFnRDLRERLETANKQLAEKEYEgseDTRKTISQL 270
Cdd:TIGR02168 171 KERRKETE-RKLERTRENLDRLEDILNELERQL-KSLERQAEKAERY-KELKAELRELELALLVLRLE---ELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 271 FAKNKESQREKEKLEAELATArstnedqrrhieirDQALSNAQAKVVKLEEELKKKQvyvdkveKMQQALVQLQAACEKR 350
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQEL--------------EEKLEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 351 EQLEHRLRTRLERELESLRIQQRQGNSQPtNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEenvmrhfaldaaa 430
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELESLEAELEELEAELEE------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 431 tvaaqrdttvishspntsydtaLEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLS 510
Cdd:TIGR02168 370 ----------------------LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
.
gi 1131298189 511 S 511
Cdd:TIGR02168 428 K 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-423 |
6.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 154 PADPF--AIVSRAQQMVEIL-SDENRN--LRQ-----ELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAM 223
Cdd:PRK03918 122 PYHVFlnAIYIRQGEIDAILeSDESREkvVRQilgldDYENAYK---NLGEVIKEIKRRIERLEKFIKRTENIEELIKEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 224 RNKLEG---EIRRMHDFNRDLRERLETAnkqlaEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRR 300
Cdd:PRK03918 199 EKELEEvlrEINEISSELPELREELEKL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 301 HIEirdqalsNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQaacekreQLEHRLrTRLERELESLRIQQRQGNSQPT 380
Cdd:PRK03918 274 EIE-------ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRL-SRLEEEINGIEERIKELEEKEE 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1131298189 381 NVSEynaaaLMEILREKEERILALEADMTKWEQ-KYLEENVMRH 423
Cdd:PRK03918 339 RLEE-----LKKKLKELEKRLEELEERHELYEEaKAKKEELERL 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-376 |
7.71e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 156 DPFAIVSRAQQMVEILSDENRnLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE----KAMRNKLEGEI 231
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 232 RRmhdfnrdLRERLETANKQLAEKEyEGSEDTRKTISQLF-AKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALS 310
Cdd:COG4913 298 EE-------LRAELARLEAELERLE-ARLDALREELDELEaQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131298189 311 NAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACE--------KREQLEHRLRtRLERELESLRiqQRQGN 376
Cdd:COG4913 370 ALGLPLPASAEEFAALR---AEAAALLEALEEELEALEealaeaeaALRDLRRELR-ELEAEIASLE--RRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-359 |
9.85e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 180 QELEGCYEKVARLQKVETEIQrvsEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDF--NRDLRERLETANKQLAE--K 255
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAE-LEELREELEKLEKLlqLLPLYQELEALEAELAElpE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 256 EYEGSEDTRKTISQLFAKNKESQREKEKLEAELATA-RSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVE 334
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 1131298189 335 KMQQALVQLQAACEKREQLEHRLRT 359
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-419 |
4.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 249 NKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQ--AKVVKLEEELKKK 326
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 327 QVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT---NVSEYNAAALMEILREKEERILA 403
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 1131298189 404 LEADMTKWEQKYLEEN 419
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-417 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 177 NLRQELEGCYEKVARLQKVETEIQRVSEAYEnlvkssSKREALEKAMRnKLEGEIRRMHDFNRDLRERLETANKQlAEKE 256
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELR------KELEELEEELE-QLRKELEELSRQISALRKDLARLEAE-VEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 257 YEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 336
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 337 QQALVQLQAACEKR-EQLEHRLR------TRLERELESLRIQ------QRQGNSQPTNVSEYNAAALMEILREKEERILA 403
Cdd:TIGR02168 826 LESLERRIAATERRlEDLEEQIEelsediESLAAEIEELEELieelesELEALLNERASLEEALALLRSELEELSEELRE 905
|
250
....*....|....
gi 1131298189 404 LEADMTKWEQKYLE 417
Cdd:TIGR02168 906 LESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-408 |
2.27e-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: 51.60 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 158 FAIVSRAQQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRM 234
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLE---ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERlanLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 235 HDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQA 314
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 315 KVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKREQLEHRLR-TRLERELESLRIQQRQGNSQptnvseynAAALMEI 393
Cdd:TIGR02168 401 EIERLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEA--------LEELREE 469
|
250
....*....|....*
gi 1131298189 394 LREKEERILALEADM 408
Cdd:TIGR02168 470 LEEAEQALDAAEREL 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-414 |
3.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 190 ARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklegeirrmhdfnRDLRERLETANKQLAEKEYEgsedtRKTISQ 269
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPI----------------RELAERYAAARERLAELEYL-----RAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 270 LFAknkesQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELkkKQVYVDKVEKMQQALVQLQAACEK 349
Cdd:COG4913 284 WFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298189 350 REqlehRLRTRLERELESLriqqrqGNSQPTNVSEY--NAAALMEILREKEERILALEADMTKWEQK 414
Cdd:COG4913 357 RE----RRRARLEALLAAL------GLPLPASAEEFaaLRAEAAALLEALEEELEALEEALAEAEAA 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-374 |
4.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 172 SDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQ 251
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 252 LAEKEYEGSEDTR---KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQV 328
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131298189 329 YVDKVEKMQQALVQLQAaceKREQLEHRLRTRLERELESLRIQQRQ 374
Cdd:COG4942 179 LLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-503 |
7.46e-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: 49.67 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 178 LRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE-KAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKE 256
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 257 YEGSEDtRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKM 336
Cdd:TIGR02168 274 LEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 337 QQALV-QLQAACEKREQLEHRLRTrLERELESLRIQQRQGNSQptnvseynAAALMEILREKEERILALEADMTKWEQKY 415
Cdd:TIGR02168 353 LESLEaELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 416 LEENvmRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIiekdAMIKVL 495
Cdd:TIGR02168 424 EELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERL 497
|
....*...
gi 1131298189 496 QQRSRKEP 503
Cdd:TIGR02168 498 QENLEGFS 505
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
165-516 |
1.04e-05 |
|
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: 49.05 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 165 QQMVEILSDENRNLRQELEGCYEKVARLQK----VETEIQRVSEAY-------ENLvkssskREALEKAMRNKLEgEIRR 233
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTdssnTDTALTTLEEALsekeriiERL------KEQREREDRERLE-ELES 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 234 MHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKE-------------KLEAELATARSTNEDQRR 300
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSleiaveqkkeecsKLENQLKKAHNAEEAVRT 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 301 HIEIRDQaLSNAQAKVVKLEEELKKKQVyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPT 380
Cdd:pfam10174 553 NPEINDR-IRLLEQEVARYKEESGKAQA---EVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQ 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 381 NVSEYNAAALMEILREKEERilaleadMTKWEQKYLEENVMRHFALDAAATVAAQR-DTTVISHSPNTSYDTALEARIQK 459
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNL-------ADNSQQLQLEELMGALEKTRQELDATKARlSSTQQSLAEKDGHLTNLRAERRK 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298189 460 EEEEILmankrcldmEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAK 516
Cdd:pfam10174 702 QLEEIL---------EMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK 749
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-409 |
3.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 169 EILSDENRNLRQELEGCYEkvaRLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNK---LEGEIRRMHDFNRDLRERL 245
Cdd:PRK02224 310 EAVEARREELEDRDEELRD---RLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 246 ETANKQL--AEKEYEGSEDTR---KTISQLFAKNKESQREKEK-LEAELATARSTNEDQRRHIE----------IRD--- 306
Cdd:PRK02224 387 EELEEEIeeLRERFGDAPVDLgnaEDFLEELREERDELREREAeLEATLRTARERVEEAEALLEagkcpecgqpVEGsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 307 -QALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAAC-------EKREQLEHRL---RTRLERE---LESLRIQQ 372
Cdd:PRK02224 467 vETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierleERREDLEELIaerRETIEEKrerAEELRERA 546
|
250 260 270
....*....|....*....|....*....|....*..
gi 1131298189 373 RQGNSQpTNVSEYNAAALMEILREKEERILALEADMT 409
Cdd:PRK02224 547 AELEAE-AEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
160-363 |
3.90e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 160 IVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmrnklEGEIRRmhdfNR 239
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAE----LE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 240 DLRERLETANKQLAEKEyEGSEDTRKTISQLFAKNKESQREKEKLEAELATArstnEDQRRHIEIRDQALSNAQAKVVKL 319
Cdd:COG4913 675 AELERLDASSDDLAALE-EQLEELEAELEELEEELDELKGEIGRLEKELEQA----EEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1131298189 320 EEELKKKQVYVDKVEK-MQQALV-QLQAACEKREQLEHRLRTRLER 363
Cdd:COG4913 750 LLEERFAAALGDAVEReLRENLEeRIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-368 |
5.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 180 QELEGCYEKVARLQKVETEIQRVSEAYENLvkssskREALEKA--MRNKLEGEIRRmhdfnrdLRERLETANKQLAEKEY 257
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKAfeELAETEKRLEE-------LRKELEELEKKYSEEEY 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 258 EGSEDtrktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHieiRDQALSNAQakvvKLEEELKKKQVYVDKVEKMQ 337
Cdd:PRK03918 662 EELRE-----------------EYLELSRELAGLRAELEELEKR---REEIKKTLE----KLKEELEEREKAKKELEKLE 717
|
170 180 190
....*....|....*....|....*....|.
gi 1131298189 338 QALVQLQAACEKREQLEHRLRTRLERELESL 368
Cdd:PRK03918 718 KALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-407 |
7.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 171 LSDENRNLRQELEGCYEKVARLQ-KVETEIQRVSEAYENL-----------VKSSSKREALE--KAMRNKLEGEIRRMHD 236
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEaTLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEedRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 237 FNRDLRERLETANK-QLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRhiEIRDQAlsnaqak 315
Cdd:PRK02224 490 EVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE--EKREAA------- 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 316 vVKLEEELKKKQVYVDKVEKmqqalvQLQAACEKREQLEhRLRTRL------ERELESLRIQQRQGNSQPTNVSEYnaaa 389
Cdd:PRK02224 561 -AEAEEEAEEAREEVAELNS------KLAELKERIESLE-RIRTLLaaiadaEDEIERLREKREALAELNDERRER---- 628
|
250
....*....|....*...
gi 1131298189 390 lmeiLREKEERILALEAD 407
Cdd:PRK02224 629 ----LAEKRERKRELEAE 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
171-315 |
8.22e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 171 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALE------KAMRNKLEgEIRRMHDFNRDLRER 244
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperlEELEERLE-ELRELEEELEELEAE 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131298189 245 LETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAK 315
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
164-405 |
8.51e-05 |
|
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: 46.10 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 164 AQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIR------RMHDF 237
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElsksseELDSF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 238 N---RDLRERLETANKQLAEKEYEGSEDTRKTIsqlfaknKESQREKEKLEAELATARSTNEDQRRHIeirdQALSNAQA 314
Cdd:COG5185 383 KdtiESTKESLDEIPQNQRGYAQEILATLEDTL-------KAADRQIEELQRQIEQATSSNEEVSKLL----NELISELN 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 315 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTrLERELESLRIQ-QRQGNSQPTNVSEYNAAALMEI 393
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST-LKATLEKLRAKlERQLEGVRSKLDQVAESLKDFM 530
|
250
....*....|..
gi 1131298189 394 LREKEERILALE 405
Cdd:COG5185 531 RARGYAHILALE 542
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
191-374 |
1.34e-04 |
|
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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 191 RLQKVETEIQRVseayenlvkssskrealeKAMRNKLEGEIrrmhdfnRDLRERLETANKQLAEKEyEGSEDTRKTISQL 270
Cdd:COG1579 11 DLQELDSELDRL------------------EHRLKELPAEL-------AELEDELAALEARLEAAK-TELEDLEKEIKRL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 271 FAKNKESQREKEKLEAELATARSTNEdqrrhIEIRDQALSNAQAKVVKLEEELKKKQvyvDKVEKMQQALVQLQAACEKR 350
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELM---ERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....
gi 1131298189 351 EQLEHRLRTRLERELESLRIQQRQ 374
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEE 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
213-410 |
1.53e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 213 SSKREALEKamrnkLEGEIRRMHDfnRDLRERLETANKQLAE-----KEYEGSED----TRKTISQLFAKNKESQREKEK 283
Cdd:PRK02224 183 SDQRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREqareTRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 284 LEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKkkqvyvDKVEKMQQALVQLQAACEKREQLEHRlRTRLER 363
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD------DLLAEAGLDDADAEAVEARREELEDR-DEELRD 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1131298189 364 ELESLRIQQRQGNSQPTNVSEyNAAALMEILREKEERILALEADMTK 410
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
196-303 |
1.95e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 196 ETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEgSEDTRKTISQLFAKNK 275
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE-LSEARSEERREIRKDR 465
|
90 100 110
....*....|....*....|....*....|.
gi 1131298189 276 E---SQREKEKLEAELATARSTNEDQRRHIE 303
Cdd:COG2433 466 EisrLDREIERLERELEEERERIEELKRKLE 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
164-368 |
6.59e-04 |
|
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: 43.24 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 164 AQQMVEILSDENRNLRQElegcYEKVARLQKVETEIQRV-SEAYENLVKSSSKREALEKAMRnKLEGEIRRMHDFNRDLR 242
Cdd:pfam01576 154 RKLLEERISEFTSNLAEE----EEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKR-KLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 243 ERLETANKQLAEKEYE------GSEDTRKTISQLFAKNKESQRE----KEKLEAELAtARSTNEDQRRHIEIRDQAL--- 309
Cdd:pfam01576 229 AQIAELRAQLAKKEEElqaalaRLEEETAQKNNALKKIRELEAQiselQEDLESERA-ARNKAEKQRRDLGEELEALkte 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131298189 310 -------SNAQAKV-VKLEEELKKKQVYVDKVEKMQQALVQ------LQAACEKREQLEH--RLRTRLERELESL 368
Cdd:pfam01576 308 ledtldtTAAQQELrSKREQEVTELKKALEEETRSHEAQLQemrqkhTQALEELTEQLEQakRNKANLEKAKQAL 382
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
178-325 |
8.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 178 LRQELEGCYEKVAR---LQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFN------RDLRERLETA 248
Cdd:PRK03918 271 LKKEIEELEEKVKElkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKKLKEL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 249 NKQLAE-----KEYEGSEDTRKTISQLfaKNKESQREKEKLEAEL---ATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 320
Cdd:PRK03918 351 EKRLEEleerhELYEEAKAKKEELERL--KKRLTGLTPEKLEKELeelEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
....*
gi 1131298189 321 EELKK 325
Cdd:PRK03918 429 EELKK 433
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
171-418 |
9.00e-04 |
|
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: 42.75 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 171 LSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL------VKSSSKREALEKAMRNKLEGEIRRMHDfnrdLRER 244
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLgdlrrqVKLLEERNAEYMQRTLQLEEELKKANA----LRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 245 LETANKQLAEKEYEGSEDTRKTISQLF------AKNKESQREKEKLEAELATARSTNED------QRRHIEIRDQALS-- 310
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKADKLEFeykkleEKLEALQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSps 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 311 -----NAQA---------KVVKLEEE-----LKKKQVYVDKVEKMQQalvQLQAACEKREQLEHRLRTRLERELE-SLRI 370
Cdd:pfam05622 265 sdpgdNLAAeimpaeireKLIRLQHEnkmlrLGQEGSYRERLTELQQ---LLEDANRRKNELETQNRLANQRILElQQQV 341
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1131298189 371 QQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKwEQKYLEE 418
Cdd:pfam05622 342 EELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQK-KKEQIEE 388
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
250-368 |
9.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 250 KQLAEKEYEGSEDTRKTIsqLFAKNKESQREKEKLEAElatARSTNEDQRRHIE----IRDQALSNAQAKVVKLEEELKK 325
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLE---AKEEIHKLRNEFEkelrERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1131298189 326 KQVYVDK----VEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 368
Cdd:PRK12704 101 KLELLEKreeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
215-465 |
9.88e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 215 KREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKEsQREKEKLEAELATARST 294
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL-KLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 295 NEDQRRHIEIRDQALSNAQAKVVKLEEELKKKqvyvdKVEKMQQALVQLQAACEKREQLEHRLRTRLEREleslriqqrq 374
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAKEEEELKSELLKLERRKVDDEE---------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 375 gnsqPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALE 454
Cdd:pfam02463 315 ----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250
....*....|.
gi 1131298189 455 ARIQKEEEEIL 465
Cdd:pfam02463 391 KLKEEELELKS 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-498 |
1.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 173 DENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAmRNKLEGEIRRMHDFN-------------R 239
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEerleelreleeelE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 240 DLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIE-IRDQALSNAQAKVVK 318
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 319 LEE-----------------ELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHR---LRTRLERELESLRIQQRQGNSQ 378
Cdd:COG4717 247 EARlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGkeaEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 379 PTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDT-------------------- 438
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleqaeeyqelkeelee 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131298189 439 ---------TVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQI--IEKDAMIKVLQQR 498
Cdd:COG4717 407 leeqleellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQE 477
|
|
| Amelogenin |
smart00818 |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
42-109 |
1.21e-03 |
|
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.
Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 40.54 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298189 42 SQPHSPTSSLTSGGSLPLLqsPPSTRLSPaQHPLVPNQGDHS--------AHLPRPQQHFLPNQAHQGDHYRLPQP 109
Cdd:smart00818 43 SQQHPPTHTLQPHHHIPVL--PAQQPVVP-QQPLMPVPGQHSmtptqhhqPNLPQPAQQPFQPQPLQPPQPQQPMQ 115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
277-506 |
1.26e-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: 42.06 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 277 SQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQAL-VQLQAACEKREQLEH 355
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 356 RLRTRLERELESLRIQQRQGNSQPTNV---------SEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFAL 426
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 427 DAAATVAAQRdttvishspntsydTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKT 506
Cdd:COG4942 178 ALLAELEEER--------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
163-369 |
1.30e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEGCYEKVarlqkveteIQRVSEAYENLVKSSSKREALEKAMRNKlEGEIRRMHDFNRDLR 242
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEF---------IQKGDEVKCKLDKSEENARSIEYEVLKK-EKQMKILENKCNNLK 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 243 ERLETANKQLAEKEYEGSEDTRKTIsqlfAKNKE---SQREKEKLEAELATARSTNED--QRRHIEIRDQALSNAqakvv 317
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGS----AENKQlnaYEIKVNKLELELASAKQKFEEiiDNYQKEIEDKKISEE----- 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 318 KLEEELKKKQVYVDKVEKMQQ--------ALVQLQAACEK---------------------REQLEHRLRTRLERELESL 368
Cdd:pfam05483 672 KLLEEVEKAKAIADEAVKLQKeidkrcqhKIAEMVALMEKhkhqydkiieerdselglyknKEQEQSSAKAALEIELSNI 751
|
.
gi 1131298189 369 R 369
Cdd:pfam05483 752 K 752
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-413 |
1.50e-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: 42.13 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 159 AIVSRAQQMVEILSDENRNLRQE-LEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGE-IRRMHD 236
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 237 FNRDLRERLETANKQLAEKE--YEGSEDTRKtiSQLFAKNKESQREKEKLEAELATARSTnedqrrhieirdqalsnaQA 314
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEddLQALESELR--EQLEAGKLEFNEEEYRLKSRLGELKLR------------------LN 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 315 KVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNVSEynaaaLMEIL 394
Cdd:pfam12128 455 QATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE-----LELQL 529
|
250 260
....*....|....*....|
gi 1131298189 395 REKEERILA-LEADMTKWEQ 413
Cdd:pfam12128 530 FPQAGTLLHfLRKEAPDWEQ 549
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-343 |
2.01e-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: 41.54 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 165 QQMVEILSDENRNLRQELEgcyEKVARLQKVETEIQRVSEAYENL---VKSSSKREALEKAMRNKLEGEIRRMHDFNRDL 241
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLE---QKQKELKSKEKELKKLNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 242 RERLETANKQLAEKEYEGSEDTR-KTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 320
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKnKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
170 180
....*....|....*....|...
gi 1131298189 321 EELKKKQVYVDKVEKMQQALVQL 343
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQE 646
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-365 |
2.01e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREAL---------EKAMRNKLEGEIRR 233
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELdgfergpfsERQIKNFHTLVIER 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 234 MHDFNR-------DLRERLETANKQLAEKEYEGSEDTRkTISQLFAKNKESQREKEKLEAELATARSTNEDqrrhIEIRD 306
Cdd:TIGR00606 403 QEDEAKtaaqlcaDLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFVIKELQQLEGSSDR----ILELD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131298189 307 QALSNAQAKVVKLEE----ELKKKQVYVDKVEKMqQALVQLQAACEKREQLEHRLRTRLEREL 365
Cdd:TIGR00606 478 QELRKAERELSKAEKnsltETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-415 |
2.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 198 EIQRVSEAY-ENLVKSS--SKREALEKAmRNKLEGEIRRmhdfnrdLRERLETANKQLAE-KEYEGSEDTRKTISQLFAK 273
Cdd:COG3206 149 LAAAVANALaEAYLEQNleLRREEARKA-LEFLEEQLPE-------LRKELEEAEAALEEfRQKNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 274 NKESQREKEKLEAELATARSTNEDQRRHIE---------IRDQALSNAQAKVVKLEEEL-KKKQVYVDKVEKMQQALVQL 343
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGsgpdalpelLQSPVIQQLRAQLAELEAELaELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131298189 344 QAACEKREQLEHRLRTRLERELESLRIQQRQGNSQptnVSEYNAAALMeiLREKEERILALEADMTKWEQKY 415
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQ---LAQLEARLAE--LPELEAELRRLEREVEVARELY 367
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-324 |
2.25e-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: 41.58 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 161 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRD 240
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 241 LRERLETANKQLAEkeyegSEDTRKTISQLFAKNKESQREKEKLEAELATArstnedqrrHIEIRDQALSNAQAKVVKLE 320
Cdd:TIGR02168 913 LRRELEELREKLAQ-----LELRLEGLEVRIDNLQERLSEEYSLTLEEAEA---------LENKIEDDEEEARRRLKRLE 978
|
....
gi 1131298189 321 EELK 324
Cdd:TIGR02168 979 NKIK 982
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-445 |
2.91e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 161 VSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVE-------TEIQRVSEAY--------------ENLVKSSSKREaL 219
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEeaekarqAEMDRQAAIYaeqermamererelERIRQEERKRE-L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 220 EKAMRNKLEGEIRRMHDF----------NRDLRERLETANKQ-LAEKEYEGSEDTRKTISQLFAKNKESQREKEkleael 288
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELerlqmerqqkNERVRQELEAARKVkILEEERQRKIQQQKVEMEQIRAEQEEARQRE------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 289 atARSTNEDQRRHIEIRDQALSNAQAKVVKL---EEELKKKQVYVDKVEKMQQALVQ-----LQAACEKREQL---EHRL 357
Cdd:pfam17380 437 --VRRLEEERAREMERVRLEEQERQQQVERLrqqEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAmieEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 358 RTRLERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRD 437
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*...
gi 1131298189 438 TTVISHSP 445
Cdd:pfam17380 595 TPITTIKP 602
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-351 |
3.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSS--KREALEKAMRNkLEGEIRRMhdfnRD 240
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdRLEQLEREIER-LERELEER----ER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 241 LRERLETANKQLAEKEYEGSEDtrktisqlFAKN-KESQREKEKLEAELATARstnEDQRRHieirDQALSNAQAKVVKL 319
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEE--------FAALrAEAAALLEALEEELEALE---EALAEA----EAALRDLRRELREL 424
|
170 180 190
....*....|....*....|....*....|....*
gi 1131298189 320 EEE---LKKKQVYVDkvEKMQQALVQLQAACEKRE 351
Cdd:COG4913 425 EAEiasLERRKSNIP--ARLLALRDALAEALGLDE 457
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
261-559 |
3.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 261 EDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQ----VYVDKVEKM 336
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 337 QQALVQLQAACEKREQLEHRLRTRL---ERELESLRIQQRQGNSQPTNVSEYNAAALMEILREKEERILALEADMTKWEQ 413
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 414 KYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIK 493
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131298189 494 VLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLSHSSTLTGTPIMEEKRDDKSWKGSLGILLG 559
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
177-410 |
3.85e-03 |
|
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: 40.87 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 177 NLRQELEGCYEKVARLQKV----ETEIQRVSEayENLVKSSSKREALEKAmrNKLEGEIRRMHDFNRDLRERLETANKQL 252
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALlkamKSECQGQME--RQMAAIQGKNESLEKV--SSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 253 aekeyegsEDTRKTISQLFAKNKESQREKEKLEAELATARSTNE---DQRRHIEIRDQALSNAQAKVVKLEEELKKK--- 326
Cdd:pfam15921 492 --------ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKdkv 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 327 -QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRTRlERELESLRIQQRQGNSQptnvseynaaalmeiLREKEERI 401
Cdd:pfam15921 564 iEILRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKDAK---------------IRELEARV 627
|
....*....
gi 1131298189 402 LALEADMTK 410
Cdd:pfam15921 628 SDLELEKVK 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-350 |
3.98e-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: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 163 RAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKreALEKAMRNKLEGEIRRMHDFNRDLR 242
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 243 --ERLETANKQLAEKEyegsEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLE 320
Cdd:COG4942 137 rlQYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
170 180 190
....*....|....*....|....*....|
gi 1131298189 321 EELKKKQVYVDKVEKMQQALVQLQAACEKR 350
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
168-422 |
4.15e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 168 VEILSDENRNLRQELEgcyekvARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLET 247
Cdd:pfam00038 20 VRFLEQQNKLLETKIS------ELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 248 --ANKQLAEKEYEGsedTRKTISQLFAKNKESQREKEKL-----------EAELATARSTNEDQRRHIEI---RDQALSN 311
Cdd:pfam00038 94 elNLRTSAENDLVG---LRKDLDEATLARVDLEAKIESLkeelaflkknhEEEVRELQAQVSDTQVNVEMdaaRKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 312 AQAKVVKLEEELKKK------QVYVDKVEKMQQALVQ----LQAACEKREQLEHRLRtRLERELESLRIQqrqgnsqptn 381
Cdd:pfam00038 171 ALAEIRAQYEEIAAKnreeaeEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQ-SLEIELQSLKKQ---------- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1131298189 382 vseynAAALMEILREKEERiLALEADMTKWEQKYLEENVMR 422
Cdd:pfam00038 240 -----KASLERQLAETEER-YELQLADYQELISELEAELQE 274
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-401 |
4.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 187 EKVARLQKVEtEIQRVSEAY---ENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANK-QLAEKEYEGSED 262
Cdd:PTZ00121 1552 KKAEELKKAE-EKKKAEEAKkaeEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 263 TRKTISQLFAKNKESQREKEKLEAELAT--------ARSTNEDQRRHIEIRdqalsNAQAKVVKLEEELKKKQVYVDKVE 334
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEEnkikaaeeAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEEAKKAE 1705
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131298189 335 KMQQALV-------QLQAACEKREQLEHRLRTRLE---RELESLRIQQRQGNSQPTNVSEYNAAAlMEILREKEERI 401
Cdd:PTZ00121 1706 ELKKKEAeekkkaeELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA-EEIRKEKEAVI 1781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
239-410 |
5.39e-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: 40.13 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 239 RDLRERLETANKQLAEKEyegsedtrKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVK 318
Cdd:COG4942 23 AEAEAELEQLQQEIAELE--------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 319 LEEELKK-KQVYVDKVEKMQ----QALVQLQAACEKREQLEHRLR------TRLERELESLRIQQRQGNSQPTNVSEyNA 387
Cdd:COG4942 95 LRAELEAqKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEA-ER 173
|
170 180
....*....|....*....|...
gi 1131298189 388 AALMEILREKEERILALEADMTK 410
Cdd:COG4942 174 AELEALLAELEEERAALEALKAE 196
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-513 |
5.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 166 QMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENL-VKSSSKREALEKAMRNKLEGEIRRmhdfnrDLRER 244
Cdd:TIGR02169 146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 245 LEtankqlaekEYEGSEDTRktisqlfaknkesqrEKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELK 324
Cdd:TIGR02169 220 KR---------EYEGYELLK---------------EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 325 KKQVYVDKVEKMQQALVQLQAA--CEKREQLEHRLRTrLERELESLRIQQRQGnsqptnVSEYNaaALMEILREKEERIL 402
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIAE-KERELEDAEERLAKL------EAEID--KLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 403 ALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSpntSYDTALEARIQKEEE-----EILMANKRCLDMEGR 477
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREKLEKLKREINElkrelDRLQEELQRLSEELA 423
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1131298189 478 -----IKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMR 513
Cdd:TIGR02169 424 dlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-304 |
8.88e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 171 LSDENRNLRQELEgcyEKVARLQKVETEIQRVSEayenlvKSSSKREALEKAMR--NKLEGEIRRMHDFNRDLRERLETA 248
Cdd:TIGR02169 355 LTEEYAELKEELE---DLRAELEEVDKEFAETRD------ELKDYREKLEKLKReiNELKRELDRLQEELQRLSEELADL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 249 NKQLA----------------------------------EKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARST 294
Cdd:TIGR02169 426 NAAIAgieakineleeekedkaleikkqewkleqlaadlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
170
....*....|
gi 1131298189 295 NEDQRRHIEI 304
Cdd:TIGR02169 506 VRGGRAVEEV 515
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
187-368 |
9.23e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 38.49 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 187 EKVARLQKVETEIQRVSEAYENLVKsssKREALEKAMrnklegeirrmHDFNRdlrerletANKQLAEKEYEGSEDTRKT 266
Cdd:cd07596 8 EAKDYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-----------GEFGK--------ALIKLAKCEEEVGGELGEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131298189 267 ISQLFAK-NKESQREKEKLEAELATARSTNEDQ-----------------RRHIEIRDQALSNAQAKVVKLEEELKKKQv 328
Cdd:cd07596 66 LSKLGKAaEELSSLSEAQANQELVKLLEPLKEYlrycqavketlddradaLLTLQSLKKDLASKKAQLEKLKAAPGIKP- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1131298189 329 yvDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESL 368
Cdd:cd07596 145 --AKVEELEEELEEAESALEEARKRYEEISERLKEELKRF 182
|
|
| |
