|
Name |
Accession |
Description |
Interval |
E-value |
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
591-732 |
2.42e-75 |
|
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.
Pssm-ID: 463310 Cd Length: 143 Bit Score: 245.62 E-value: 2.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 591 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 670
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907189183 671 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVP 732
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1088-1251 |
1.11e-64 |
|
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.
Pssm-ID: 465655 Cd Length: 166 Bit Score: 216.51 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 1088 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1164
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 1165 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1244
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 1907189183 1245 LRSVYEQ 1251
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-404 |
4.51e-13 |
|
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: 74.32 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 101 RLGRDVEmeemIEQLQEKVHELERQNEVLKNRLISAKQQLQ---------VQGHRQTSYSRVQARVNTGRRRASASAGSQ 171
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 172 ECPGKGLRFQNVDEAETVQptltkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENeiELSLLQLR 251
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 252 EQQATDQRSNIRDNVETIK-----LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCS 326
Cdd:TIGR02168 819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189183 327 LEKQLHSLQDRINDLEKERELLKEnydklynsafsaaHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTER 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELRE-------------KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-480 |
1.18e-12 |
|
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: 72.78 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 106 VEMEEMIEQLQEKVHELERQnevlknrlisaKQQLQVQGHRQTSYSRVQARVNTGRRRASAsagsqecpgkgLRFQN-VD 184
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERYKELKAELRELELALLV-----------LRLEElRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 185 EAETVQPTLTKYsNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSN 261
Cdd:TIGR02168 240 ELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 262 IRDNVETIKLHKQLVEKSNALSviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDL 341
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 342 EKERELLK---ENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERGPLINQNEKLVQEN 418
Cdd:TIGR02168 392 ELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189183 419 RDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALLLIKAQKEQKNGD---LSFLEKVDSK 480
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-492 |
1.63e-12 |
|
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: 72.40 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------QRLKCCSLEKQLHSLQDRINDLEKERELLKENYD 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 354 KLynsafSAAHEEQWKLKEQqmkvqiAQLETALKSDLTDKTEV-LDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRL 432
Cdd:TIGR02168 856 SL-----AAEIEELEELIEE------LESELEALLNERASLEEaLALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907189183 433 HELQSRLKFFNQESDINADDLSEAL-LLIKAQKEQKNGDLSFLEKVDSKInKDLDRSMKEL 492
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRL-KRLENKIKEL 984
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
786-885 |
5.80e-12 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 63.24 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 786 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDT 865
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 1907189183 866 QENIYMGKVNVPLISLAHDK 885
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-566 |
9.05e-11 |
|
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: 66.62 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 197 SNSLLEEARgEIRNLENviqsqrgQIEELEHLAEILKTQLKRKEneielsllqlreqqatDQRSNIRDNVEtiKLHKQLV 276
Cdd:TIGR02168 669 NSSILERRR-EIEELEE-------KIEELEEKIAELEKALAELR----------------KELEELEEELE--QLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 277 EKSNALSVIEGKFIQLQEKQRTLRishdALMANGDELNKQLKEQRLkccSLEKQLHSLQDRINDLEKERELLKENYDKLy 356
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLE----ERIAQLSKELTELEAEIE---ELEERLEEAEEELAEAEAEIEELEAQIEQL- 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 357 nsafsaahEEQWKLKEQQMKVQIAQLeTALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQ 436
Cdd:TIGR02168 795 --------KEELKALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 437 SRLKffNQESDINA-----DDLSEALLLIKAQKEQKNGDlsfLEKVDSKiNKDLDRSMKELQATHAETVQELEKTRNMLI 511
Cdd:TIGR02168 866 ELIE--ELESELEAllnerASLEEALALLRSELEELSEE---LRELESK-RSELRRELEELREKLAQLELRLEGLEVRID 939
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189183 512 -MQHKINKDYQMEVETVtQKMENLQQDYELKVEQyvhlldiraaRIQKLEAQLKDI 566
Cdd:TIGR02168 940 nLQERLSEEYSLTLEEA-EALENKIEDDEEEARR----------RLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-466 |
1.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQR--SNIRDNVETIK-LHKQLVE 277
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARleQDIARLEERRReLEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccslEKQLHSLQDRINDLEKERELLKENYDKLYN 357
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 358 SAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQS 437
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|....*....
gi 1907189183 438 RLKFFNQESDINADDLSEALLLIKAQKEQ 466
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-507 |
2.41e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLKRKEneIELSLLQLREQQATDQRsnirdnvetikLHKQ 274
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 275 LVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDK 354
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 355 LynsafsAAHEEQWKLKEQQMKVQIAQLETALKS---DLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQR 431
Cdd:COG1196 328 L------EEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189183 432 LHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKdLDRSMKELQATHAETVQELEKTR 507
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLE 476
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
207-592 |
1.23e-09 |
|
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: 62.73 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 207 EIRNLENVIQSQRGQIEELEHLAEILKTqLKRKENEIELSLLQLREQQatdqrSNIRDNVEtiKLHKQLVEKSNALSVIE 286
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISELKKQN-----NQLKDNIE--KKQQEINEKTTEISNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 287 GKFIQLQEKQrtlrishdalmangDELNKQLKEQRL-------KCCSLEKQLHSLQDRINDLEKEREllkENYDKLYNSA 359
Cdd:TIGR04523 253 TQLNQLKDEQ--------------NKIKKQLSEKQKeleqnnkKIKELEKQLNQLKSEISDLNNQKE---QDWNKELKSE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 360 FSAAHEEQWKLKEQ---------QMKVQIAQLET----------ALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRD 420
Cdd:TIGR04523 316 LKNQEKKLEEIQNQisqnnkiisQLNEQISQLKKeltnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 421 LQLQCLQQKQRLHELQSRLKFFNQESDInaddLSEALLLIKAQKEQKNGDLSFLEKVDS----KIN-------------K 483
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKEL----LEKEIERLKETIIKNNSEIKDLTNQDSvkelIIKnldntresletqlK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 484 DLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQdyelKVEQYVHLLDIRAARIQKLEAQL 563
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE----KIEKLESEKKEKESKISDLEDEL 547
|
410 420
....*....|....*....|....*....
gi 1907189183 564 KDIAYGTKQYKFKPEImpddsvDEFDETI 592
Cdd:TIGR04523 548 NKDDFELKKENLEKEI------DEKNKEI 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-373 |
1.25e-09 |
|
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: 62.77 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRfqnvDEA 186
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE----AEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 187 ETVQPTLTKYSNSL------LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQA--TDQ 258
Cdd:TIGR02168 785 EELEAQIEQLKEELkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIEslAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 259 RSNIRDNVEtiKLHKQLVEKSN-------ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQL 331
Cdd:TIGR02168 861 IEELEELIE--ELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907189183 332 HSLQDRINDLEK-ERELLKENYDKLYNSaFSAAHEEQWKLKEQ 373
Cdd:TIGR02168 939 DNLQERLSEEYSlTLEEAEALENKIEDD-EEEARRRLKRLENK 980
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
193-594 |
1.38e-09 |
|
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: 62.35 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 193 LTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA---TDQRSNIRDNVETI 269
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeieKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 270 KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLK 349
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 350 ENYDKLYNSAFSAAHEEQWKLKEqqmkvqiaqletalksdLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQK 429
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKE-----------------LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 430 QRLHELQSRLKffNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDLDRSMKELQathaETVQELEKTRNM 509
Cdd:TIGR04523 531 SEKKEKESKIS--DLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----QKSLKKKQEEKQ----ELIDQKEKEKKD 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 510 LIMQHKInkdYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYkfKPEIMPD--DSVDE 587
Cdd:TIGR04523 601 LIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK--WPEIIKKikESKTK 674
|
....*..
gi 1907189183 588 FDETIHL 594
Cdd:TIGR04523 675 IDDIIEL 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-566 |
1.51e-09 |
|
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: 62.83 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 116 QEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNtgrrraSASAGSQECPGKGLRFQnvDEAETVQ-PTLT 194
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR------SILVDFEEASGKKIYEH--DSMSTMHfRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEEL----EHLAEILKTQLKRK------ENEIELSLLQLREQQATDQRSNIRD 264
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRieqlisEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 265 NVETIklhKQLVEKSNA-----LSVIEGKFIQLQEKQRTL-RISHDALMANGDEL---NKQLKEQRL-------KCCSLE 328
Cdd:pfam15921 300 QLEII---QEQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKIEELEKQLvlaNSELTEARTerdqfsqESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 329 KQLHSLQDRINDLEKERELLKENYDKLYN----SAFSAAHEEQwKLKEQQMKVQiaQLETALKsdlTDKTEVLDKLKTER 404
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQ--RLEALLK---AMKSECQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 405 GPLINQNEKLVQENR---DLQLQCLQQKQRLHELQSRlKFFNQESDINADDLSEALLLIKAQKEQKNGDLsflekvdSKI 481
Cdd:pfam15921 451 AAIQGKNESLEKVSSltaQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKERAIEATNAEI-------TKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 482 NKDLDRSMKELQ-----ATHAETVQ-ELEKTRNMLIMQHKINKDYQMEVETVTQ-----------------KMENLQQDY 538
Cdd:pfam15921 523 RSRVDLKLQELQhlkneGDHLRNVQtECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvekaQLEKEINDR 602
|
570 580
....*....|....*....|....*...
gi 1907189183 539 ELKVEQYVHLLDIRAARIQKLEAQLKDI 566
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-567 |
1.01e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLH-KQLVEKS 279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 280 NALSVIEGKFIQLQEKQRTLRISHDALMAngdelnKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLYNSA 359
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 360 FSAAHEEQWKLKEQQMKV--QIAQLETALKSDLTDKTEVLDKLKTERGPLI-------NQNEKLVQENRDLQLQCLQQKQ 430
Cdd:COG4717 237 EAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 431 RLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQkngdLSFLEKVDSKInkDLDRSMKELQATHAETVQELEKTRNML 510
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 511 IMQHKINKDYQMEVETVTQKMENLqqDYELKVEQYVHLLDIRAARIQKLEAQLKDIA 567
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-404 |
1.79e-08 |
|
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: 59.31 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrf 180
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEE-------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEhlaeilktqlkRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLE-----------EALNDLEARLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 261 NIRDNVETI---------KLHKQLVEKSNALSVIEGK---FIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLE 328
Cdd:TIGR02169 802 KLEEEVSRIearlreieqKLNRLTLEKEYLEKEIQELqeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189183 329 KQLHSLQDRINDLEKERELLKENYDKLYNSAFSAAHE-EQWKLKEQQMKVQIAQLETALKSDLTDKTEVLD--KLKTER 404
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAEL 960
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-420 |
2.52e-08 |
|
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: 57.47 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 197 SNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLR--EQQATDQRSNIRDNVETI-KLHK 273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 274 QLVEKSNALSviegkfIQLQEKQRTLRISHDALMANGDELNKQLKEQRLkccsLEKQLHSLQDRINDLEKERELLKENYD 353
Cdd:COG4942 98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 354 KLynsafsaaheEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRD 420
Cdd:COG4942 168 EL----------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-562 |
5.58e-08 |
|
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: 57.34 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKnklEVELNKLEKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 272 HKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEK--QLH-SLQDRINDLEKERELL 348
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiQKNkSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 349 KENYDKLyNSAFSAAhEEQWKLKEQQMKvQIAQLETALKSDLTDKTEVLDKLKTergpLINQNEKLVQenrdlqlqclqq 428
Cdd:TIGR04523 231 KDNIEKK-QQEINEK-TTEISNTQTQLN-QLKDEQNKIKKQLSEKQKELEQNNK----KIKELEKQLN------------ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 429 kqrlhELQSRLKFFNQESDINAD-DLSEALLLIKAQKEQKNGDLSFLEKVDSKIN---KDLDRSMKELQATHAETVQELE 504
Cdd:TIGR04523 292 -----QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELE 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189183 505 KTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIraaRIQKLEAQ 562
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDE---QIKKLQQE 420
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
43-552 |
6.49e-08 |
|
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: 57.44 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 43 SRVSREELEDRFLRLHDE--NILLKQHARKQEDKIKRMatklirlvNDKKRYERvgggpkRLGRDVEMEEMIEQLQEKVH 120
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQlqKLLADLHKREKELSLEKE--------QNKRLWDR------DTGNSITIDHLRRELDDRNM 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 121 ELERQNEVLKnrliSAKQQLQVQGHRQTSysRVQARvNTGRRRASASAGSQECPGKGLRfQNVDEA-------ETVQPTL 193
Cdd:pfam15921 427 EVQRLEALLK----AMKSECQGQMERQMA--AIQGK-NESLEKVSSLTAQLESTKEMLR-KVVEELtakkmtlESSERTV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 194 TKYSNSLLEEARG-EIRNLEnvIQSQRGQI----EELEHL-------------AEILKTQLKRKENEIEL------SLLQ 249
Cdd:pfam15921 499 SDLTASLQEKERAiEATNAE--ITKLRSRVdlklQELQHLknegdhlrnvqteCEALKLQMAEKDKVIEIlrqqieNMTQ 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 250 LREQQAtdqRSNIRDNVETIKLHKQLVEKSNALSVI-------EGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRL 322
Cdd:pfam15921 577 LVGQHG---RTAGAMQVEKAQLEKEINDRRLELQEFkilkdkkDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 323 KCCSLEKQLHSLQDRINDLEKERELLKENYdklynsafsaaheeqwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKT 402
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNF----------------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 403 ERGplinQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQKNGDLSFLEKVDSKIN 482
Cdd:pfam15921 718 MEG----SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEKNKLSQELSTVATEKN 786
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 483 KdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvHLLDIR 552
Cdd:pfam15921 787 K----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---HTLDVK 846
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
786-881 |
8.37e-08 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 51.33 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 786 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHD--TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDS 863
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 1907189183 864 DTQENIYMGKVNVPLISL 881
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| C2 |
pfam00168 |
C2 domain; |
786-893 |
1.32e-07 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 786 LHVTVKCCTGLQSRASYLQPHAYV-VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSD 864
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 1907189183 865 TQENIYMGKVNVPLISLAHDKCISGIFEL 893
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-321 |
1.94e-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: 55.83 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 126 NEVLKNRLISAKQQLQVQghrQTSYSRVQARVntgrrrASASAGSQECPGKglrfqnVDEAETVQPTLTKYSNSL---LE 202
Cdd:TIGR02168 318 LEELEAQLEELESKLDEL---AEELAELEEKL------EELKEELESLEAE------LEELEAELEELESRLEELeeqLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 203 EARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETI-KLHKQLVEKSNA 281
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeELQEELERLEEA 462
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907189183 282 LSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQR 321
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
198-510 |
2.74e-07 |
|
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: 55.36 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 198 NSLLEEARGEIRNLENViqsQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQ 274
Cdd:pfam02463 197 LQELKLKEQAKKALEYY---QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqvLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 275 LVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELlkenydk 354
Cdd:pfam02463 274 NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 355 lynsafsaaheeqWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHE 434
Cdd:pfam02463 347 -------------LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 435 LQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNML 510
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDeLELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-582 |
1.64e-06 |
|
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: 52.42 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 223 EELEHLAEILKTQLKRKENEIELSLLQLREQQAT---------DQRSNIRDNVETIKLH----KQLVEKSNAL-SVIEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 289 FIQLQEKQRTLRISHDALMANGDELNK--QLKEQRLKCCSLEKQLHSLQdrINDLEKE----RELLKENYDKLYNsafsa 362
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQltEEKEAQMEELNKAKAAHSFV--VTEFEATtcslEELLRTEQQRLEK----- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 363 aHEEQWKLKEQQMKVQIAQLETALKsdLTDKTEV-LDKLKTergpLINQNEKLVQENRDLQLQCLQQKQRLHE----LQS 437
Cdd:pfam05483 375 -NEDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKK----ILAEDEKLLDEKKQFEKIAEELKGKEQEliflLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 438 RLK-FFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNMLIMQHK 515
Cdd:pfam05483 448 REKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 516 INKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPD 582
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-590 |
2.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 34 RTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndKKRYERVGGGPKRLGRDVEME-EMI 112
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA---QAEEYELLAELARLEQDIARLeERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 113 EQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrfqnvDEAETVQPT 192
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELE---ELEEELEEAEEELEEAEAELAEAEEALL-----------EAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 193 LTKYSNSL--LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVE 267
Cdd:COG1196 378 EEELEELAeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALaelEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 268 TIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccSLEKQLHSLQDRINDLEKEREL 347
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIG 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 348 LKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDktEVLDKLKTERgplinqnekLVQENRDLQLQCLQ 427
Cdd:COG1196 532 VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF--LPLDKIRARA---------ALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 428 QKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEkVDSKINKDLDRSMKELQATHAETVQELEKTR 507
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 508 NMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDE 587
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
...
gi 1907189183 588 FDE 590
Cdd:COG1196 760 PDL 762
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
192-545 |
2.58e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 192 TLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKL 271
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 272 HKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQrlkccslEKQLHSLQDRINDLEKERELLKEN 351
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 352 YDKL----YNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQ 427
Cdd:COG4372 173 LQALseaeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 428 QKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAETVQELEKTR 507
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907189183 508 NMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQY 545
Cdd:COG4372 333 AILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-417 |
3.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 48 EELEDRFLRLH------DENILLKQHARKQEDKIKRMATKLIRLvndkkrYERVGGGPKRLGRDVEMEEMIEQLQEKVHE 121
Cdd:PRK03918 276 EELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRL------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 122 LERQNEVLKNRLisakqqlqvqghrqTSYSRVQARVNTGRRRASASAGsqECPGKGLRfqNVDEAETVQPTLTKYsnslL 201
Cdd:PRK03918 350 LEKRLEELEERH--------------ELYEEAKAKKEELERLKKRLTG--LTPEKLEK--ELEELEKAKEEIEEE----I 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 202 EEARGEIRNLENVIQSQRGQIEEL----------------EHLAEILK--------------------TQLKRKENEIEL 245
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEeytaelkriekelkeieekeRKLRKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 246 SLLQ----LREQQATDQRSNIRDNVETIKLHKqLVEKSNALSVIEGKFIQLQEKQRTLRIShdalMANGDELNKQLKEQR 321
Cdd:PRK03918 488 VLKKeselIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 322 LKCCSLEKQLHSLQDRI--------NDLEKERELLKENYDKlYNSAFSAAHEEQWKLKEQQmkvqiaqletALKSDLTDK 393
Cdd:PRK03918 563 KKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNE-YLELKDAEKELEREEKELK----------KLEEELDKA 631
|
410 420
....*....|....*....|....
gi 1907189183 394 TEVLDKLKTERGPLINQNEKLVQE 417
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKK 655
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-350 |
4.02e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQR--SNIRDNVETIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189183 276 VEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccsLEKQLHSLQDRINDLEKERELLKE 350
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAA 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-404 |
4.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169 176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 124 RQNEVLKnRLISAKQQlqvqghrqtSYSRVQARVNTGRRRASASAGsqecpgkglrfqnvDEAETVQPTLtkysnsllEE 203
Cdd:TIGR02169 251 EELEKLT-EEISELEK---------RLEEIEQLLEELNKKIKDLGE--------------EEQLRVKEKI--------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-----TDQRSNIRDNVETIKLHKQLVEK 278
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 279 SNALSVIEGKfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKEREllkenydklyns 358
Cdd:TIGR02169 379 EFAETRDELK--DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE------------ 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907189183 359 afsAAHEEQWKlKEQQMKVQIAQLETAlKSDLTDKTEVLDKLKTER 404
Cdd:TIGR02169 445 ---DKALEIKK-QEWKLEQLAADLSKY-EQELYDLKEEYDRVEKEL 485
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
5.81e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLKRKENEIELSLLQLRE--QQATDQRSNIRDNVETIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189183 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
312-592 |
7.54e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 312 ELNKQLKEQRLKCCSLEKQLHSLQDRINDLEK----ERELLKENYDKLYNSAfsaaheeqwklkeQQMKVQIAQLETALK 387
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEA-------------KTIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 388 ---SDLTDKTEVLDKLKTERGPLINQNEKL----------------VQENRDLQLQCLQQKQRLHELQSRLKFFN----- 443
Cdd:PHA02562 245 nlvMDIEDPSAALNKLNTAAAKIKSKIEQFqkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDtaide 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 444 -QESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiNKDLDRSMKELQATHAETVQELEKTRNMLImqhKINKDYQm 522
Cdd:PHA02562 325 lEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS- 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189183 523 evETVTQKME-----NLQQDYELKveqyvhlldiraARIQKleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 592
Cdd:PHA02562 397 --ELVKEKYHrgivtDLLKDSGIK------------ASIIK-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-563 |
1.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELERQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 127 EVLKNRLISAKQQLQVQGHRQtsysrvqaRVNTGRRRASASAGSQECPGKGLRFQnVDEAETVQPTLTKYSN-------- 198
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYE--------EYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKklkelekr 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 199 --------SLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLKRKEnEIELSLLQLREQQAT--DQRSNIRDNVET 268
Cdd:PRK03918 354 leeleerhELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 269 IKLHK----------------QLVEKSNA-LSVIEGKFIQLQEKQRTLRishdalmANGDELNKQLKEQR--LKCCSLEK 329
Cdd:PRK03918 431 LKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELAE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 330 QLHSLQDRIN--DLEK------ERELLKENYDKLyNSAFSAAHEEQWKLKEqqMKVQIAQLETALKSDLTDKTEVLDKLK 401
Cdd:PRK03918 504 QLKELEEKLKkyNLEElekkaeEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 402 TERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDiNADDLSEALLLIKAQKEQKNGDLSFLEKV-DSK 480
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKySEE 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 481 INKDLDRSMKELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLD 550
Cdd:PRK03918 660 EYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVKKYKALLK 738
|
570
....*....|....
gi 1907189183 551 IRA-ARIQKLEAQL 563
Cdd:PRK03918 739 ERAlSKVGEIASEI 752
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
34-350 |
1.97e-04 |
|
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: 45.88 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 34 RTVKTRQAVSRVSREELEdRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGggpkrLGRDVEMEEMie 113
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQE-RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA-----MERERELERI-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 114 QLQEKVHELE--RQNEVLKNrlISAKQQLQ-VQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAEtvQ 190
Cdd:pfam17380 354 RQEERKRELEriRQEEIAME--ISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--Q 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 191 PTLTKYSNSLLEEARGeiRNLENViqsqRGQIEELEHLAEILKTQ-LKRKENEIELSLLQLREQQATDQRSNIRDNvETI 269
Cdd:pfam17380 430 EEARQREVRRLEEERA--REMERV----RLEEQERQQQVERLRQQeEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 270 KLHKQLVEKSNALSVIEGkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLK 349
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEK---EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
.
gi 1907189183 350 E 350
Cdd:pfam17380 580 Q 580
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
108-355 |
2.51e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 108 MEEMIEQ-LQEKVHELERQNEVLKNRLISAKQQLQvqghrqtsysRVQARVNTGRRRASASAGSQEcpgKGLRFQNVDEA 186
Cdd:COG3206 158 AEAYLEQnLELRREEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKNGLVDLSEE---AKLLLQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 187 ETvqpTLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEIlkTQLKRKENEIELSLLQLReQQATDQrsnirdnv 266
Cdd:COG3206 225 ES---QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELS-ARYTPN-------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 267 etiklHKQLVEKSNALSVIEGKF-IQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccSLEKQLHSLQDRINDLEKER 345
Cdd:COG3206 290 -----HPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLE----ARLAELPELEAELRRLEREV 360
|
250
....*....|
gi 1907189183 346 ELLKENYDKL 355
Cdd:COG3206 361 EVARELYESL 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-389 |
4.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELsllQLREQQATDQRS 260
Cdd:COG3883 27 ELQAELEAAQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 261 NIRDNVETIKLHKQLVEKSNALSVIEG----KFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQD 336
Cdd:COG3883 103 SYLDVLLGSESFSDFLDRLSALSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907189183 337 RINDLEKERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQIAQLETALKSD 389
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-350 |
5.03e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSysrvqARVNTGRRRASASAGSQEcpgkglRFQNVDEA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEAR------REELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 187 ETVQPTltkysnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatDQRSNIRDNV 266
Cdd:PRK02224 324 EELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 267 ETiklhkqlveksnalsvIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccsLEKQLHSLQDRIndlEKERE 346
Cdd:PRK02224 394 EE----------------LRERFGDAPVDLGNAEDFLEELREERDELREREAE-------LEATLRTARERV---EEAEA 447
|
....
gi 1907189183 347 LLKE 350
Cdd:PRK02224 448 LLEA 451
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-579 |
6.10e-04 |
|
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: 44.33 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 200 LLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----LQLREQQATDQRSNIRDNVETI--KLH 272
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMstqkaLEEDLQIATKTICQLTEEKEAQmeELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 273 KQLVEKSNALSVIEGKFIQLQEkqrTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENY 352
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 353 DKLYNSAFSAAHEEQWKLKEQQ--------------MKVQIAQLETA----------LKSDLTDKTEVLDKLKTERGPLI 408
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQElifllqarekeihdLEIQLTAIKTSeehylkevedLKTELEKEKLKNIELTAHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 409 NQNEKLVQENRDLQlqclqqkqrlhelqsrLKFFNQESDINADdlseallliKAQKEQKNGDLSFLEKVDSKINKDLDRS 488
Cdd:pfam05483 499 LENKELTQEASDMT----------------LELKKHQEDIINC---------KKQEERMLKQIENLEEKEMNLRDELESV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 489 MKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI-A 567
Cdd:pfam05483 554 REEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnA 633
|
410
....*....|..
gi 1907189183 568 YGTKQYKFKPEI 579
Cdd:pfam05483 634 YEIKVNKLELEL 645
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-400 |
7.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 112 IEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGsqecpgkglrfqnVDEAETVQP 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-------------IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 192 TLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKEneielsllqlREQQATDQRSNIRDNVETIKL 271
Cdd:COG4913 679 RLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE----------EELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 272 HKQLveksnalsviEGKFIQLQEKQRTLRIShDALMANGDELNKQLKEQRLKccsLEKQLHS--------LQDRINDLEK 343
Cdd:COG4913 748 RALL----------EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMRAfnrewpaeTADLDADLES 813
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189183 344 ERELLKEnYDKLYNSAFsAAHEEQWK-LKEQQMKVQIAQLETALKSDLTDKTEVLDKL 400
Cdd:COG4913 814 LPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
109-563 |
7.32e-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: 44.04 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 109 EEMIEQLQEKVHELERQN-------EVLKNRLiSAKQQlqvqghrqtSYSRVQARVNTGRRRasasagsqecpgkglrfq 181
Cdd:pfam10174 302 ESELLALQTKLETLTNQNsdckqhiEVLKESL-TAKEQ---------RAAILQTEVDALRLR------------------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 182 nVDEAETVQPTLTKYSNSLLEEA---RGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQ-QATD 257
Cdd:pfam10174 354 -LEEKESFLNKKTKQLQDLTEEKstlAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA----GLKERvKSLQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 258 QRSNIRDNVETiKLHKQLVEKSNalsVIEgkfiQLQE-KQRTLRISHDALmangDELNKQLKEQRLKCCSLEKQLHSLQD 336
Cdd:pfam10174 429 TDSSNTDTALT-TLEEALSEKER---IIE----RLKEqREREDRERLEEL----ESLKKENKDLKEKVSALQPELTEKES 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 337 RINDLEKE------RELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDK----LKTERGP 406
Cdd:pfam10174 497 SLIDLKEHasslasSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQevarYKEESGK 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 407 LINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEalllikAQKEQKNGDLSFLEKVdSKINKDLD 486
Cdd:pfam10174 577 AQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKH------GQQEMKKKGAQLLEEA-RRREDNLA 649
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 487 RSMKELQAthAETVQELEKTRNmlimqhkinkdyqmEVETVTQKMENLQQDYElkvEQYVHLLDIRAARIQKLEAQL 563
Cdd:pfam10174 650 DNSQQLQL--EELMGALEKTRQ--------------ELDATKARLSSTQQSLA---EKDGHLTNLRAERRKQLEEIL 707
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-400 |
7.84e-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: 42.60 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 221 QIEELEHLAEILKTQLKRKENEIElsllqlreqQATDQRSNIRDNVETIKlhKQLVEKSNALSVIEGKFIQLQEKQRTLR 300
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELA---------ALEARLEAAKTELEDLE--KEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 301 iSHDALMAngdeLNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENYDKLynsafsaahEEQWKLKEQQMKVQIA 380
Cdd:COG1579 87 -NNKEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL---------EAELEEKKAELDEELA 152
|
170 180
....*....|....*....|
gi 1907189183 381 QLETALKSDLTDKTEVLDKL 400
Cdd:COG1579 153 ELEAELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-566 |
8.59e-04 |
|
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: 43.21 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 358 SAFSAAHEEQWKLKEQ--QMKVQIAQLETALKSDLTDKTEVLDKLKTERGpLINQNEKLVQENRDLQLQCLQQKQrlhEL 435
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELA---EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 436 QSRLKFFNQESDINADDLSEalLLIKAQKEQKNGDLSFLEKVDS--------KINKDLDRSMKELQATHAETVQELEKTR 507
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189183 508 NMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI 566
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-558 |
8.95e-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: 43.63 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 209 RNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQAtdQRSNIRDNVEtiKLHKQLVEKSNALSVIEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 289 FIQLQEKQRTLrishdalmanGDELN--KQLKEQRLKCCSLEKQLHSLQdrindlEKERELLKEnydklynsafsaAHEE 366
Cdd:pfam01576 287 RNKAEKQRRDL----------GEELEalKTELEDTLDTTAAQQELRSKR------EQEVTELKK------------ALEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 367 QWKLKEQQMKvQIAQLETALKSDLTDKTEV-------LDK----LKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHEL 435
Cdd:pfam01576 339 ETRSHEAQLQ-EMRQKHTQALEELTEQLEQakrnkanLEKakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 436 QSRLkffnQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQAThaetvQEL--EKTRNMLIMQ 513
Cdd:pfam01576 418 QARL----SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQKLNLS 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907189183 514 HKINkdyQMEVETvTQKMENLQQDYELK--VEQYVHLLDIRAARIQK 558
Cdd:pfam01576 489 TRLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
107-563 |
1.24e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQnvDEA 186
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH--PNP 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 187 ETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEiELSLLQLReQQATDQRSNIRDNV 266
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCD-NRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 267 ETIK--LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDalmangdELNKQLKEQRLKCCSLEKQLHSLQDRIndleKE 344
Cdd:TIGR00618 594 VRLQdlTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH-------LQQCSQELALKLTALHALQLTLTQERV----RE 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 345 RELLKENYDKLYNSAFSAAHEEQWKLKEQ--QMKVQIAQLETALKSDLTdKTEVLDKLKTE-------RGPLINQNEKLV 415
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQltYWKEMLAQCQTLLRELET-HIEEYDREFNEienasssLGSDLAAREDAL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 416 QENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADD-LSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQA 494
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNL 821
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189183 495 THAETVQELEKTRNML----IMQHKINKDYQMEVETVTQKMENLQQDYEL-----KVEQY-VHLLDIRAARIQKLEAQL 563
Cdd:TIGR00618 822 QCETLVQEEEQFLSRLeeksATLGEITHQLLKYEECSKQLAQLTQEQAKIiqlsdKLNGInQIKIQFDGDALIKFLHEI 900
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-563 |
1.25e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 15 KDTGLNLFGVGGLQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQ--EDKIKRMA------------- 79
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvlEKELKHLRealqqtqqshayl 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 80 TKLIRLVNDKKRYERVGGgpKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISaKQQLQVQGHRQTSYSRVQARVNt 159
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHTELQSKMR- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 160 grRRASASAGSQecpgkGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQrgQIEELEHLAEI--LKTQLK 237
Cdd:TIGR00618 322 --SRAKLLMKRA-----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLqqQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 238 RKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQLVEKSNALSVIEgKFIQLQEKQRTLRISHDALMANGDELN 314
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaKKQQELQQRYAELCA-AAITCTAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 315 KQLKEQRLKCCSLEKQLHSLQD-RINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKsdltDK 393
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE----DV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 394 TEVLDKLKTERGPLINQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSF 473
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 474 LEKV--DSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKIN---------KDYQMEVETVTQKMENLQQDYELKV 542
Cdd:TIGR00618 628 QDVRlhLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
570 580 590
....*....|....*....|....*....|.
gi 1907189183 543 EQYVHLLDIR----------AARIQKLEAQL 563
Cdd:TIGR00618 708 ELETHIEEYDrefneienasSSLGSDLAARE 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-355 |
1.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQqatdQRSNIRDNVETIKlhKQLVEKSN 280
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQ----IRGNGGDRLEQLE--REIERLER 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907189183 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLkccSLEKQLHSLQDRINDLEKERELLKENYDKL 355
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE---ALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
113-534 |
1.45e-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: 42.90 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 113 EQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQA---RVNTGRRRASA-------------SAGSQECP-- 174
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEApdwEQSIGKVISPEllhrtdldpevwdGSVGGELNly 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 175 GKGLRFQNVDEAETVQPTltkysnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQ 254
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASE---------EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 255 ATDQRSNIRDNVETIKLHKQLVEKsnalsviegkfIQLQEKQRTlrishdalmangdELNKQLK--EQRLKCCSLEKQLH 332
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAER-----------KDSANERLN-------------SLEAQLKqlDKKHQAWLEEQKEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 333 SLQDRINDLEKERELLKENYDKLynsafsAAHEEQWKLKEQQMKVQIAQLETALKSDLTDK---TEVLDKLKTERGPLIN 409
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALDAQL------ALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 410 ------------------QNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDL 471
Cdd:pfam12128 783 kieriavrrqevlryfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907189183 472 SFLEKVDSKINK-DLDRSMKELQATHAETVQELEktrnmlimQHKINKDYqmEVETVTQKMENL 534
Cdd:pfam12128 863 RGLRCEMSKLATlKEDANSEQAQGSIGERLAQLE--------DLKLKRDY--LSESVKKYVEHF 916
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
185-389 |
1.82e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 185 EAETVQPTLTKYSNSLL---EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLK-----RKENEIELSLLQLREQQAt 256
Cdd:pfam07888 105 ELSASSEELSEEKDALLaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKkagaqRKEEEAERKQLQAKLQQT- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 257 dqrsnirdNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDAlmangdelnKQLKEQRLKccSLEKQLHSLQD 336
Cdd:pfam07888 184 --------EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT---------AHRKEAENE--ALLEELRSLQE 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189183 337 RINDLEKERELLKENYDKLyNSAFSAAHEE--QWKLKEQQMKVQIAQLETALKSD 389
Cdd:pfam07888 245 RLNASERKVEGLGEELSSM-AAQRDRTQAElhQARLQAAQLTLQLADASLALREG 298
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-536 |
1.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 49 ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIR-------LVNDKKRYERVGGGPK-RLGRD----VEMEEMIEQLQ 116
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEeeekaksLSKLKNKHEAMISDLEeRLKKEekgrQELEKAKRKLE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 117 EKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVN-TGRRRASASAGSQECPGKGLRFQNVDEAETVQPT-LT 194
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLA---KKEEELQAALARLEeETAQKNNALKKIRELEAQISELQEDLESERAARNkAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 195 KYSNSLLEEARGEIRNLENVIQSQRGQiEELEHLAEILKTQLKR------KENEIELSLLQLREQQATDQrsnIRDNVET 268
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQ-QELRSKREQEVTELKKaleeetRSHEAQLQEMRQKHTQALEE---LTEQLEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 269 IKLHKQLVEKSNAlsVIEGKFIQLQEKQRTLRIShdalmangdelnKQLKEQRLKccSLEKQLHSLQDRINDLEKERELL 348
Cdd:pfam01576 368 AKRNKANLEKAKQ--ALESENAELQAELRTLQQA------------KQDSEHKRK--KLEGQLQELQARLSESERQRAEL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 349 KENYDKL------YNSAFSAA-------HEEQWKLKEQQMKVQ-IAQLETALKSDLTDKtevLDKLKTERGPLINQNEKl 414
Cdd:pfam01576 432 AEKLSKLqselesVSSLLNEAegkniklSKDVSSLESQLQDTQeLLQEETRQKLNLSTR---LRQLEDERNSLQEQLEE- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 415 vqenrdlqlqclqqkqrlhELQSRLKFFNQESDINAddlseALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQa 494
Cdd:pfam01576 508 -------------------EEEAKRNVERQLSTLQA-----QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907189183 495 THAETVQELEKTRNMLimqhkinkdyQMEVETVTQKMENLQQ 536
Cdd:pfam01576 563 EKAAAYDKLEKTKNRL----------QQELDDLLVDLDHQRQ 594
|
|
| C2B_RasGAP |
cd08675 |
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ... |
786-893 |
2.59e-03 |
|
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.
Pssm-ID: 176057 [Multi-domain] Cd Length: 137 Bit Score: 39.66 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 786 LHVTVKCCTGLQ----------SRASYLQPHAYVVYKffdfpdhdTAIVPSSNDPQFDDHMCFPVPMNMDLDRY---LKS 852
Cdd:cd08675 1 LSVRVLECRDLAlksngtcdpfARVTLNYSSKTDTKR--------TKVKKKTNNPRFDEAFYFELTIGFSYEKKsfkVEE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907189183 853 ESLSFY-----VFDDSDTQENIYMGKVNVPLISLAHDKCISGIFEL 893
Cdd:cd08675 73 EDLEKSelrveLWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFL 118
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-352 |
3.30e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 35 TVKTRQAVSRVSREELEDRFLRLHDENiLLKQHARKQEDKIKRMAT------KLIRLVNDKKRYerVGGGPKrLGRDVEM 108
Cdd:PRK04863 760 VVKIADRQWRYSRFPEVPLFGRAAREK-RIEQLRAEREELAERYATlsfdvqKLQRLHQAFSRF--IGSHLA-VAFEADP 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 109 EEMIEQLQEKVHELER-------QNEVLKNRLISAKQQLQvQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGL--- 178
Cdd:PRK04863 836 EAELRQLNRRRVELERaladhesQEQQQRSQLEQAKEGLS-ALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRfvq 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 179 RFQN-VDEAETVQPTLT-------------KYSNSLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQ 235
Cdd:PRK04863 915 QHGNaLAQLEPIVSVLQsdpeqfeqlkqdyQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQR 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 236 LKRKENEIELSLLQLREQQATDQRSNirdnvetiKLHKQLVeksnalSVIEGKFIQLQEKQR-----TLRISHDA---LM 307
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYN--------QVLASLK------SSYDAKRQMLQELKQelqdlGVPADSGAeerAR 1059
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907189183 308 ANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLKENY 352
Cdd:PRK04863 1060 ARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-414 |
4.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILK------TQLKRKENEIELSL------LQLREQQATDQRSNIRDNVET 268
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKrkleekIRELEERIEELKKEIEELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 269 IKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccSLEKQLHSLQDRINDLEKERELL 348
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189183 349 KEnYDKLYNSAfSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEV---LDKLKTERGPLINQNEKL 414
Cdd:PRK03918 358 EE-RHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIeeeISKITARIGELKKEIKEL 424
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-363 |
4.09e-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: 40.90 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLqvqghrqtsySRVQARVNTGRRRasasagsqecpgkglrfqnvdea 186
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRI----------AALARRIRALEQE----------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 187 etvqptltkysnslLEEARGEIRNLENVIQSQRGQIEELEH-LAEILKTQLKRKENEIELSLLQLREQQATDQRS----- 260
Cdd:COG4942 78 --------------LAALEAELAELEKEIAELRAELEAQKEeLAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylky 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 261 ---NIRDNVETIKLHKQLVEKSNAlsviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDR 337
Cdd:COG4942 144 lapARREQAEELRADLAELAALRA---------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
250 260
....*....|....*....|....*.
gi 1907189183 338 INDLEKERELLKENYDKLYNSAFSAA 363
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAA 240
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
201-404 |
5.82e-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: 41.19 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKEN-EIELSLLQLREQQATDQRSNIrdnvetiklhKQLVEKS 279
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKI----------AQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 280 NALSvIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQrlkccslEKQLHSLQDRINDLEKERELLKENYDK---LY 356
Cdd:TIGR00606 816 QGSD-LDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-------QEQIQHLKSKTNELKSEKLQIGTNLQRrqqFE 887
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907189183 357 NSAFSAAHEEQWKLKE-QQMKVQIAQLETALKSDLTDKTEVLDKLKTER 404
Cdd:TIGR00606 888 EQLVELSTEVQSLIREiKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
207-397 |
6.10e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIelsllqlreQQATDQRSNIrdnvetiklhKQLVEKSNalsvie 286
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKENRLLKRLQKRQEKAL---------GKYEGTESEL----------PQLIARHN------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 287 gkfiqlqEKQRTLRISHDALMANGDELNKQLKE------------QRLKCCS----------LEKQLHSLQDRINDLEKE 344
Cdd:pfam15619 67 -------EEVRVLRERLRRLQEKERDLERKLKEkeaellrlrdqlKRLEKLSedknlaereeLQKKLEQLEAKLEDKDEK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907189183 345 RELLkENYDKLYNSAFSAA-HEEQWKLKEQQMKVQIAQLE-TALKSDLTDKTEVL 397
Cdd:pfam15619 140 IQDL-ERKLELENKSFRRQlAAEKKKHKEAQEEVKILQEEiERLQQKLKEKEREL 193
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
201-417 |
6.19e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 201 LEEARGEIRNLENVIQSQRGQIEElehlaeiLKTQLKRKENEIELSLLQLREQQAtdqrsnirdnvetiKLHKQLVEKSN 280
Cdd:pfam09787 49 LEELRQERDLLREEIQKLRGQIQQ-------LRTELQELEAQQQEEAESSREQLQ--------------ELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 281 ALSVIEGKFIQLQEKQRTLRishdalmangDElnkqlkeqrlkccsLEKQLHSLQDRINDLEKERELLKenyDKLYNSAF 360
Cdd:pfam09787 108 ARREAEAELERLQEELRYLE----------EE--------------LRRSKATLQSRIKDREAEIEKLR---NQLTSKSQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 361 SAAHEEQWklkEQQMKvqiaqletALKSDLTDKTEVLDKLKTERGPLINQNEKLVQE 417
Cdd:pfam09787 161 SSSSQSEL---ENRLH--------QLTETLIQKQTMLEALSTEKNSLVLQLERMEQQ 206
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-467 |
6.52e-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: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 270 KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSLQDRINDLEKERELLK 349
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 350 ENYDKLYNSAFSAAHEEQWKLK----------------EQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERGPLINQNEK 413
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLlspedfldavrrlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907189183 414 LVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDI---NADDLSEALLLIKAQKEQK 467
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| C2B_RasA3 |
cd04010 |
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ... |
786-881 |
7.58e-03 |
|
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.
Pssm-ID: 175977 [Multi-domain] Cd Length: 148 Bit Score: 38.53 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 786 LHVTVKCCTGLQSRASYLQPHAYV--VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDLDRYLK---SESLSFY-- 858
Cdd:cd04010 2 LSVRVIECSDLALKNGTCDPYASVtlIYSNKKQDTKRTKVKKKTNNPQFDEAFYFDVTIDSSPEKKQFempEEDAEKLel 81
|
90 100
....*....|....*....|....*.
gi 1907189183 859 ---VFDDSDTQENIYMGKVNVPLISL 881
Cdd:cd04010 82 rvdLWHASMGGGDVFLGEVRIPLRGL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-361 |
7.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 151 SRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETVQptltKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAE 230
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG----SRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 231 ILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFI--QLQEKQRTLRIS------ 302
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDleELERELERLEREiealgp 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907189183 303 --------HDALMANGDELNKQLKEqrlkccsLEKQLHSLQDRINDLEKE-RELLKENYDKLyNSAFS 361
Cdd:COG1196 782 vnllaieeYEELEERYDFLSEQRED-------LEEARETLEEAIEEIDREtRERFLETFDAV-NENFQ 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
107-258 |
9.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHR----QTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQN 182
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189183 183 V-----------DEAETVQpTLTKYSNSLLEE---ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLL 248
Cdd:COG3883 107 VllgsesfsdflDRLSALS-KIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170
....*....|
gi 1907189183 249 QLREQQATDQ 258
Cdd:COG3883 186 QLSAEEAAAE 195
|
|
| |
