|
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 ... |
597-738 |
3.32e-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: 245.23 E-value: 3.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 597 TIHLERGENLFEIHINKVTFSSEVLRASGDKELVTFCTYAFYDFELQTTPIVRGLYPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145976944 677 TVTLELHQAHSTDYETIAACQLRFHEILEK-SGRIFCTTSLVGTKGDIPNFGTVEYWFRLRVP 738
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1094-1257 |
1.65e-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: 215.74 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 1094 PSEEIRIEIIALNL-NDSQITREDTIQRLFIECRFYSLPAE--ETPMSLPKPQSGQWVYYNYSNVIYLDKENNPAVRDIL 1170
Cdd:pfam18111 1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 1171 KAILQRRELPHRSVRFTVVSDPPeDEQDLECEDIGVAHVDLADLFQKGRDIIEQDIDVLDARTDGGTIGKLKVTVEALHA 1250
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 145976944 1251 LRSVYEQ 1257
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-498 |
5.31e-14 |
|
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: 77.40 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRSNIRDNVETIKLHKQLVEKSN 280
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-------QRLKCCSLEKQLHSVrfsERRVEELQDRINDLEK 353
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAAT---ERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 354 ERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERDQNEKLVQENRDlqlqclq 433
Cdd:TIGR02168 853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELRE------- 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145976944 434 qkqRLHELQSRLKFFNQESDINADDLSEAL-LLIKAQKEQKNGDLSFLEKVDSKInKDLDRSMKEL 498
Cdd:TIGR02168 923 ---KLAQLELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRL-KRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-423 |
6.36e-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: 73.55 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 101 RLGRDVEmeemIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAgsqecpgkglrf 180
Cdd:TIGR02168 672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALR------------ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 181 QNVDEAETVQPTLTKYSNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-- 255
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLskeLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAel 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 256 TDQRSNIRDNVETIK-LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSV 334
Cdd:TIGR02168 813 TLLNEEAANLRERLEsLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 335 RFserRVEELQDRINDLEKERELLKENYDKLynsafsAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTER 414
Cdd:TIGR02168 893 RS---ELEELSEELRELESKRSELRRELEEL------REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
....*....
gi 145976944 415 DQNEKLVQE 423
Cdd:TIGR02168 964 EDDEEEARR 972
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
792-891 |
6.18e-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: 6.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 792 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
|
90 100
....*....|....*....|
gi 145976944 872 QENIYMGKVNVPLISLAHDK 891
Cdd:cd00030 74 SKDDFLGEVEIPLSELLDSG 93
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-600 |
2.04e-10 |
|
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: 65.43 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 114 QLQEKVHELERQNEVLKNRLISAKQQLQVQghrQTSYSRVQARVNtgrrrasasagsqecpgkglrfQNVDEAETVQPTL 193
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEK---TTEISNTQTQLN----------------------QLKDEQNKIKKQL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 194 TKySNSLLEEARGEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLKRKENEIELSLLQLRE-----QQATDQRSNIR 263
Cdd:TIGR04523 270 SE-KQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 264 D-----NVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDAL---MANGDELNKQlKEQRLKCCSLEKQLHSVR 335
Cdd:TIGR04523 349 KeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQ-KDEQIKKLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 336 FSERRVE--ELQDRINDLEKERELLKENYDKLYNsaFSAAHEEQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKte 413
Cdd:TIGR04523 428 IERLKETiiKNNSEIKDLTNQDSVKELIIKNLDN--TRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELKKLN-- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 414 rDQNEKLVQENRDLQLQCLQQKQRLHELQSR-----LKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVdskiN 488
Cdd:TIGR04523 503 -EEKKELEEKVKDLTKKISSLKEKIEKLESEkkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----Q 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 489 KDLDRSMKELQathaETVQELEKTRNMLIMQHKInkdYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRAARIQKLEAQ 568
Cdd:TIGR04523 578 KSLKKKQEEKQ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQ 649
|
490 500 510
....*....|....*....|....*....|....
gi 145976944 569 LKDIAYGTKQYkfKPEIMPD--DSVDEFDETIHL 600
Cdd:TIGR04523 650 IKETIKEIRNK--WPEIIKKikESKTKIDDIIEL 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-486 |
4.51e-10 |
|
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: 64.31 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 106 VEMEEMIEQLQEKVHELERQnevlknrlisaKQQLQVQGHRQTSYSRVQARVNTGRRRASAsagsqecpgkgLRFQN-VD 184
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERYKELKAELRELELALLV-----------LRLEElRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 185 EAETVQPTLTKYsNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSN 261
Cdd:TIGR02168 240 ELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 262 IRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSER-- 339
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAsl 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 340 --RVEELQDRINDLEKERELLKENYDKLYNSAFSAaheeqwKLKEQQMkvQIAQLETALKSDLTDKTEVLDKLKTERDQN 417
Cdd:TIGR02168 399 nnEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ELKELQA--ELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145976944 418 EKLVQENRDLQLQCLQQKQRLHELQSRLKffnqesdiNADDLSEALLLIKAQKEQKNGD---LSFLEKVDSK 486
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQE--------NLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEG 534
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-558 |
6.63e-10 |
|
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: 63.98 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921 321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 123 ERQNEVLKNRliSAKQQLQVQGHRQTSYSRvqaRVNTGRRRASASAGSQECPGKGLR----FQNVDEAETVQPTLTkysn 198
Cdd:pfam15921 397 KEQNKRLWDR--DTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLT---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----------LQLREQQ----ATDQRSNIR 263
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdLKLQELQhlknEGDHLRNVQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 264 DNVETIKLhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLeKQLHSVRfsERRVEE 343
Cdd:pfam15921 548 TECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF-KILKDKK--DAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 344 LQDRINDLEKERELL--------------KENYDKLYNSAFSAAHE------------EQWKLKEQQMKVQIAQLETALK 397
Cdd:pfam15921 623 LEARVSDLELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNElnslsedyevlkRNFRNKSEEMETTTNKLKMQLK 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 398 SDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFnQESDINADDLSEALllikaqKEQKNGDL 477
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL-EEAMTNANKEKHFL------KEEKNKLS 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 478 SFLEKVDSKINKdldrSMKELQATHAETVQELEKTRNMLIMQHKINKDYQmEVETVTQKMEnlQQDYELKVEqyvHLLDI 557
Cdd:pfam15921 776 QELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---HTLDV 845
|
.
gi 145976944 558 R 558
Cdd:pfam15921 846 K 846
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-572 |
1.55e-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: 59.36 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLvndkkRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921 73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEM-----QMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 116 QEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNtgrrraSASAGSQECPGKGLRFQnvDEAETVQ-PTLT 194
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR------SILVDFEEASGKKIYEH--DSMSTMHfRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEEL----EHLAEILKTQLKRK------ENEIELSLLQLREQQATDQRSNIRD 264
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEALksesQNKIELLLQQHQDRieqlisEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 265 NVETIklhKQLVEKSNA-----LSVIEGKFIQLQEKQRTL-RISHDALmangDELNKQ--LKEQRLKCCSLEKQLHSvRF 336
Cdd:pfam15921 300 QLEII---QEQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQlvLANSELTEARTERDQFS-QE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 337 SERRVEELQDRINDL---EKERELLKENYDKLYN----SAFSAAHEEQwKLKEQQMKVQ-IAQLETALKSDLTDKTE-VL 407
Cdd:pfam15921 372 SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQrLEALLKAMKSECQGQMErQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 408 DKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRlKFFNQESDINADDLSEALLLIKAQKEQKNGDLsflekvdSKI 487
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKERAIEATNAEI-------TKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 488 NKDLDRSMKELQ-----ATHAETVQ-ELEKTRNMLIMQHKINKDYQMEVETVTQ-----------------KMENLQQDY 544
Cdd:pfam15921 523 RSRVDLKLQELQhlkneGDHLRNVQtECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvekaQLEKEINDR 602
|
570 580
....*....|....*....|....*...
gi 145976944 545 ELKVEQYVHLLDIRAARIQKLEAQLKDI 572
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-423 |
2.26e-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: 57.85 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 197 SNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLR--EQQATDQRSNIRDNVETI-KLHK 273
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRalEQELAALEAELAELEKEIaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 274 QLVEKSNALSviegkfIQLQEKQRTLRISHDALMANGDELNKQLKEQRlkccsLEKQLHSVRfsERRVEELQDRINDLEK 353
Cdd:COG4942 98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYLAPAR--REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 354 ERELLKENYDKLynSAFSAAHEEQwKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQE 423
Cdd:COG4942 165 LRAELEAERAEL--EALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-568 |
2.29e-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: 58.49 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 195 KYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEI---ELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKnklEVELNKLEKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 272 HKQLVEKSNalsviegKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDL 351
Cdd:TIGR04523 151 EKELEKLNN-------KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 352 EKERELLKENYDKLyNSAFSAAhEEQWKLKEQQMKvQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQenrdlqlqc 431
Cdd:TIGR04523 224 KKQNNQLKDNIEKK-QQEINEK-TTEISNTQTQLN-QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN--------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 432 lqqkqrlhELQSRLKFFNQESDINAD-DLSEALLLIKAQKEQKNGDLSFLEKVDSKIN---KDLDRSMKELQATHAETVQ 507
Cdd:TIGR04523 292 --------QLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNeqiSQLKKELTNSESENSEKQR 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145976944 508 ELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIraaRIQKLEAQ 568
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ-NQEKLNQQKDE---QIKKLQQE 420
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-480 |
5.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQEcpgKGLRF 180
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE---QDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 181 QNVDEAETVQptltkysnsLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKrkenEIELSLLQLREQQATDQRS 260
Cdd:COG1196 307 LEERRRELEE---------RLEELEEELAELEEELEELEEELEELEEELEEAEEELE----EAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 261 NIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccslEKQLHsvrfsERR 340
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE----EEEEE-----EAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 341 VEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLdKLKTERDQNEKL 420
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLA 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 421 VQENRDLQLQCLQQKQRLHELQSRLKffnqesDINADDLSEALLLIKAQKEQKNGDLSFL 480
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
792-887 |
8.83e-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: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 792 LHVTVKCCTGLQSRASYLQPHAYVVYKFFDFPDHD--TAIVPSSNDPQFDDHMCFPVPmnmdldrYLKSESLSFYVFDDS 869
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
|
90
....*....|....*...
gi 145976944 870 DTQENIYMGKVNVPLISL 887
Cdd:smart00239 75 RFGRDDFIGQVTIPLSDL 92
|
|
| C2 |
pfam00168 |
C2 domain; |
792-899 |
1.41e-07 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 792 LHVTVKCCTGLQSRASYLQPHAYV-VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDldrylksESLSFYVFDDSD 870
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 145976944 871 TQENIYMGKVNVPLISLAHDKCISGIFEL 899
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
223-588 |
1.50e-07 |
|
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: 55.88 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 223 EELEHLAEILKTQLKRKENEIELSLLQLREQQAT---------DQRSNIRDNVETIKLH----KQLVEKSNAL-SVIEGK 288
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 289 FIQLQEKQRTLRISHDALMANGDELNK--QLKEQRLKCCSLEKQLHSVrfserRVEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQltEEKEAQMEELNKAKAAHSF-----VVTEFEATTCSLE---ELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 367 NSafsaahEEQWKLKEQQMKVQIAQLETALKsdLTDKTEV-LDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHE----L 441
Cdd:pfam05483 374 KN------EDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKKILAEDEKLLDEKKQFEKIAEELKGKEQEliflL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 442 QSRLK-FFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKD-LDRSMKELQATHAETVQELEKTRNMLIMQ 519
Cdd:pfam05483 446 QAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145976944 520 HKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIAYGTKQYKFKPEIMPD 588
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-358 |
1.75e-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: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 126 NEVLKNRLISAKQQLQVQghrQTSYSRVQARVntgrrrASASAGSQECPGKglrfqnVDEAETVQPTLTKYSNSL---LE 202
Cdd:TIGR02168 318 LEELEAQLEELESKLDEL---AEELAELEEKL------EELKEELESLEAE------LEELEAELEELESRLEELeeqLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 203 EARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDqrsnirdnvetikLHKQLVEKSNAL 282
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE-------------LQAELEELEEEL 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145976944 283 SVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQlhsvrfsERRVEELQDRINDLEKERELL 358
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL-------QENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-412 |
2.17e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 101 RLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQvqgHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrf 180
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEE-------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 181 QNVDEAETVQPTLTKYSNSLlEEARGEIRNLENVIQSQRGQIEELEhlaeilktqlkRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEI-ENVKSELKELEARIEELEEDLHKLE-----------EALNDLEARLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 261 nirdnvetiKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVrfsERR 340
Cdd:TIGR02169 802 ---------KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEE 869
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145976944 341 VEELQDRINDLEKERELLKENYDKLynsafsAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKT 412
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDEL------EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-445 |
1.91e-06 |
|
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: 52.38 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIRNLENVIQSQRGQIE-----------ELEHLAEILKTQLKRKENEIELSLLQLREQQA--TDQRSNIRDNVE 267
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEklteeiselekRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGelEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 268 TIK-----LHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRfseRRVE 342
Cdd:TIGR02169 312 EKEreledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR---DELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 343 ELQDRINDLEKERELLKENYDKLynsafsaaHEEQWKLKEQ--QMKVQIAQLE---TALKSDLTDKTEVLDKLKTERDQN 417
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRL--------QEELQRLSEElaDLNAAIAGIEakiNELEEEKEDKALEIKKQEWKLEQL 460
|
250 260 270
....*....|....*....|....*....|..
gi 145976944 418 ----EKLVQENRDLQLQCLQQKQRLHELQSRL 445
Cdd:TIGR02169 461 aadlSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-573 |
2.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEksn 280
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 281 alsviegkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccSLEKQLHSVRFSERRVEELQDRINDLEKERELLKE 360
Cdd:COG4717 160 ----------ELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 361 NYDKLYNSAFSAAHEEQWKLKEQQMKV--QIAQLETALKSDLTDKTEVLDKLKT-----------ERDQNEKLVQENRDL 427
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 428 QLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQkngdLSFLEKVDSKInkDLDRSMKELQATHAETVQ 507
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145976944 508 ELEKTRNMLIMQHKINKDYQMEVETVTQKMENLqqDYELKVEQYVHLLDIRAARIQKLEAQLKDIA 573
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-426 |
3.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSysrvqARVNTGRRRASASAGSQEcpgkglRFQNVDEA 186
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEAR------REELEDRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 187 ETVQPTltkysnslLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQatDQRSNIRDNV 266
Cdd:PRK02224 324 EELRDR--------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR--EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 267 ETikLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKE-QRL----KC--C--SLEKQLHSVRFS 337
Cdd:PRK02224 394 EE--LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaEALleagKCpeCgqPVEGSPHVETIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 338 ERR--VEELQDRINDLEKERELLKENYDKLynSAFSAAHEEQWKLKEQQMKVQ--IAQLETALKSD---LTDKTEVLDKL 410
Cdd:PRK02224 472 EDRerVEELEAELEDLEEEVEEVEERLERA--EDLVEAEDRIERLEERREDLEelIAERRETIEEKrerAEELRERAAEL 549
|
330
....*....|....*.
gi 145976944 411 KTERDQNEKLVQENRD 426
Cdd:PRK02224 550 EAEAEEKREAAAEAEE 565
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
148-426 |
4.20e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 148 TSYSRVQARVNTGRRRASASAGSQecpgkglRFQNVDEAETVqptltkySNSLLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNE-------QQTNSKDGEQL-------SDFQLEDLVGMIQNAEkNILLLNQARLQALE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 227 HLAEIL--KTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHD 304
Cdd:PLN02939 157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 305 ALMANGDELNKQLKEqrlkccslekqlhsvrfserrVEELQDRINDLEKERELLKENYDKLyNSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939 237 LLKDDIQFLKAELIE---------------------VAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145976944 385 MKVQIAQLETalksdLTDkteVLDKLKTERDQNEKLVQENRD 426
Cdd:PLN02939 295 YDCWWEKVEN-----LQD---LLDRATNQVEKAALVLDQNQD 328
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-361 |
7.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQqatdQRSNIRDNVETIKlhKQLVEKSN 280
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQ----IRGNGGDRLEQLE--REIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 281 ALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFS-ERRVEELQDRINDLEKERELLK 359
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
..
gi 145976944 360 EN 361
Cdd:COG4913 433 RR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-570 |
1.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 219 RGQIEELehlAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVEtiKLHKQlveKSNALsviegKFIQLQEKQRT 298
Cdd:COG1196 158 RAIIEEA---AGISKYKERKEEAERKLEATEENLERLEDILGELERQLE--PLERQ---AEKAE-----RYRELKEELKE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 299 LRISH-----DALMANGDELNKQLKEQRLKCCSLEKQLHSVrfsERRVEELQDRindLEKERELLKENYDKLYNSAFSAA 373
Cdd:COG1196 225 LEAELlllklRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLE---LEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 374 HEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESD 453
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 454 INADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRsMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETV 533
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
330 340 350
....*....|....*....|....*....|....*..
gi 145976944 534 TQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLK 570
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-572 |
3.10e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 368 SAFSAAHEEQWKLKEQ--QMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRL 445
Cdd:COG4942 13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 446 KFFNQESDINADDLSEalLLIKAQKEQKNGDLSFLEKVDS--------KINKDLDRSMKELQATHAETVQELEKTRNMLI 517
Cdd:COG4942 93 AELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 145976944 518 MQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI 572
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-426 |
3.17e-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: 48.53 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169 176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 124 RQNEVLKnRLISAKQQlqvqghrqtSYSRVQARVNTGRRRASASAGsqecpgkglrfqnvDEAETVQPTLtkysnsllEE 203
Cdd:TIGR02169 251 EELEKLT-EEISELEK---------RLEEIEQLLEELNKKIKDLGE--------------EEQLRVKEKI--------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQA-----TDQRSNIRDNVETIKLHKQLVEK 278
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 279 SNALSVIEGKfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRF----SERRVEELQDRINDLEKE 354
Cdd:TIGR02169 379 EFAETRDELK--DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkineLEEEKEDKALEIKKQEWK 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145976944 355 RELLKENYDKlynsafsaAHEEQWKLKEQQMKVQiaqletalkSDLTDKTEVLDKLKTERDQNEKLVQENRD 426
Cdd:TIGR02169 457 LEQLAADLSK--------YEQELYDLKEEYDRVE---------KELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-516 |
3.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 48 EELEDRFLRLH------DENILLKQHARKQEDKIKRMATKLIRLvndkkrYERVGGGPKRLGRDVEMEEMIEQLQEKVHE 121
Cdd:PRK03918 276 EELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRL------EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 122 LERQNEVLKNRLisakqqlqvqghrqTSYSRVQARVNTGRRRASASAGsqECPGKGLRfqNVDEAETVQPTLTKYsnslL 201
Cdd:PRK03918 350 LEKRLEELEERH--------------ELYEEAKAKKEELERLKKRLTG--LTPEKLEK--ELEELEKAKEEIEEE----I 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 202 EEARGEIRNLENVIQSQRGQIEEL----------------EHLAEILKT---QLKRKENEIELSLLQLRE--QQATDQRS 260
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEEytaELKRIEKELKEIEEKERKlrKELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 261 NIRDNVETIKLHK---QLVEKSNALSVIEGKfiQLQEKQRTLRishdalmangdELNKQLKEQRLKCCSLEKQLHSVRFS 337
Cdd:PRK03918 488 VLKKESELIKLKElaeQLKELEEKLKKYNLE--ELEKKAEEYE-----------KLKEKLIKLKGEIKSLKKELEKLEEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 338 ERRVEELQDRINDLEKERELLKenyDKLYNSAFSAAHEEQWKLKE-QQMKVQIAQLETAlKSDLTDKTEVLDKLKTERDQ 416
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKElEPFYNEYLELKDA-EKELEREEKELKKLEEELDK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 417 NEKLVQEnrdlqlQCLQQKQRLHELQSRLKFFNQESDINADD----LSEALLLIKAQKEQkngdlsfLEKVDSKINKDLD 492
Cdd:PRK03918 631 AFEELAE------TEKRLEELRKELEELEKKYSEEEYEELREeyleLSRELAGLRAELEE-------LEKRREEIKKTLE 697
|
490 500
....*....|....*....|....
gi 145976944 493 RsMKELQATHAETVQELEKTRNML 516
Cdd:PRK03918 698 K-LKEELEEREKAKKELEKLEKAL 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-410 |
5.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 112 IEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGsqecpgkglrfqnVDEAETVQP 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-------------IAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 192 TLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllqlREQQATDQRSNIRDNVETIKL 271
Cdd:COG4913 679 RLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD------ELQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 272 hkqlveksnalsviEGKFIQLQEKQRTLRIShDALMANGDELNKQLKEQRLKccsLEKQLHsvRFSERRVEELQDRINDL 351
Cdd:COG4913 752 --------------EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAETADLDADL 811
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 352 EKERELLKEnYDKLYNSAFsAAHEEQWK-LKEQQMKVQIAQLETALKSDLTDKTEVLDKL 410
Cdd:COG4913 812 ESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-513 |
6.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 193 LTKYSNS------LLEEARGEIRNLENVIQSQrGQIEELEHLAEILKTQLKRKENEIELSLLQLREqqatdQRSNIRDNV 266
Cdd:PRK03918 157 LDDYENAyknlgeVIKEIKRRIERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELRE-----ELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 267 ETIKLHKQLVEKSN-ALSVIEGKFIQLQEKQRtlrishdalmangdELNKQLKEQRLKCCSLEKQlhsvrfsERRVEELQ 345
Cdd:PRK03918 231 KELEELKEEIEELEkELESLEGSKRKLEEKIR--------------ELEERIEELKKEIEELEEK-------VKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 346 DRINDLEKERELLKENYDKLYNSafsaahEEQWKLKEQQMKVQIAQLEtalksDLTDKTEVLDKLKTERDQNEKLVQENR 425
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREI------EKRLSRLEEEINGIEERIK-----ELEEKEERLEELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 426 DLQLQCLQQKQRLHELQsRLKffNQESDINADDLSEALLLIKAQKEQKNGDlsfLEKVDSKINKdLDRSMKELQathaET 505
Cdd:PRK03918 359 ERHELYEEAKAKKEELE-RLK--KRLTGLTPEKLEKELEELEKAKEEIEEE---ISKITARIGE-LKKEIKELK----KA 427
|
....*...
gi 145976944 506 VQELEKTR 513
Cdd:PRK03918 428 IEELKKAK 435
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
207-323 |
7.49e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLKRKENEIELSLLQLRE--QQATDQRSNIRDNVETIK-----LHKQLVE 277
Cdd:COG1340 141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 145976944 278 KSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLK 323
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-569 |
9.28e-05 |
|
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: 46.89 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 15 KDTGLNLFGVGGLQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQ--EDKIKRMA------------- 79
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvlEKELKHLRealqqtqqshayl 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 80 TKLIRLVNDKKRYERVGGgpKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISaKQQLQVQGHRQTSYSRVQARVNt 159
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHTELQSKMR- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 160 grRRASASAGSQecpgkGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQrgQIEELEHLAEI--LKTQLK 237
Cdd:TIGR00618 322 --SRAKLLMKRA-----AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLqqQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 238 RKENEIELSLLQLREQQATDQRSNIRDNVETIKL---HKQLVEKSNALSVIEgKFIQLQEKQRTLRISHDALMANGDELN 314
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaKKQQELQQRYAELCA-AAITCTAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 315 KQLKEQRLKCCSLEKQLHSVRfsERRVEELQD---------------------------RINDLEKERELLKENYDKLYN 367
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVV--LARLLELQEepcplcgscihpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYH 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 368 SAfSAAHEEQWKLKEQQMKVQiaQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENrDLQLQCLQQKQRLHELQSRLKF 447
Cdd:TIGR00618 550 QL-TSERKQRASLKEQMQEIQ--QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 448 FNQESDINADDLSEALLLIKAQKEQKNGDLSFlEKVDSKInkdldRSMKELQATHAETVQELEKTrnmliMQHKInkdyq 527
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREHA-----LSIRVLPKELLASRQLALQK-----MQSEK----- 689
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 145976944 528 mevETVTQKMENLQQDYELKVEQYVHLLDIR----------AARIQKLEAQL 569
Cdd:TIGR00618 690 ---EQLTYWKEMLAQCQTLLRELETHIEEYDrefneienasSSLGSDLAARE 738
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
34-360 |
1.03e-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: 46.66 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 34 RTVKTRQAVSRVSREELEdRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGggpkrLGRDVEMEEMie 113
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQE-RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA-----MERERELERI-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 114 QLQEKVHELER-QNEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAEtvQPT 192
Cdd:pfam17380 354 RQEERKRELERiRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--QEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 193 LTKYSNSLLEEARGeiRNLENVIQSQrgqiEELEHLAEILKTQ-LKRKENEIELSLLQLREQQATDQRSNIRDNvETIKL 271
Cdd:pfam17380 432 ARQREVRRLEEERA--REMERVRLEE----QERQQQVERLRQQeEERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 272 HKQLVEKSNALSVIEGkfiQLQEKQRTLRISHDALMANGDELNKQLKEQRLKccsLEKQLhsvrfseRRVEELQDRINDL 351
Cdd:pfam17380 505 KQAMIEEERKRKLLEK---EMEERQKAIYEEERRREAEEERRKQQEMEERRR---IQEQM-------RKATEERSRLEAM 571
|
....*....
gi 145976944 352 EKERELLKE 360
Cdd:pfam17380 572 EREREMMRQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-474 |
1.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQL 140
Cdd:COG4717 46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 141 QVQGHRQTsYSRVQARVNTGRRRAsASAGSQECPGKGLRFQ---NVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQS 217
Cdd:COG4717 126 QLLPLYQE-LEALEAELAELPERL-EELEERLEELRELEEEleeLEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 218 QRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQrsnIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQR 297
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 298 T-----------LRISHDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSE--------------RRVEELQDRINDLE 352
Cdd:COG4717 281 LvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 353 KEREL--LKENYDKLYNSAFSAAHEE-----QWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTE--RDQNEKLVQE 423
Cdd:COG4717 361 EELQLeeLEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEE 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 145976944 424 NRDLQLQCLQQKQRLHELQSRLKffNQESDinaDDLSEALLLIKAQKEQKN 474
Cdd:COG4717 441 LEELEEELEELREELAELEAELE--QLEED---GELAELLQELEELKAELR 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-370 |
1.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELERQ 125
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAaNLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 126 NEVLKNRLISAKQQLQVQGHRQTSYSRVQARVNTGRRRASASAGSQEcpgkglrfQNVDEAEtvqptltkysnSLLEEAR 205
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE--------EALALLR-----------SELEELS 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 206 GEIRNLENVIQSQRGQIEELEHLAEilktQLKRKENEIELSLLQLREQQATDQrsniRDNVETIKLHKQLVEKSnaLSVI 285
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEY----SLTLEEAEALENKIEDD--EEEA 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 286 EGKFIQLQEKQRTL-RISHDALmangDELnKQLKEqRLKccSLEKQLHSVrfsERRVEELQDRINDLEKE-RELLKENYD 363
Cdd:TIGR02168 971 RRRLKRLENKIKELgPVNLAAI----EEY-EELKE-RYD--FLTAQKEDL---TEAKETLEEAIEEIDREaRERFKDTFD 1039
|
....*..
gi 145976944 364 KLyNSAF 370
Cdd:TIGR02168 1040 QV-NENF 1045
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-360 |
1.70e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQR--SNIRDNVETIKLHKQL 275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 276 VEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLKEqrlkccsLEKQLhsvrfsERRVEELQDRINDLEKER 355
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
|
....*
gi 145976944 356 ELLKE 360
Cdd:COG1579 166 EELAA 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
209-564 |
2.17e-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: 45.94 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 209 RNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQAtdQRSNIRDNVEtiKLHKQLVEKSNALSVIEGK 288
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 289 FIQLQEKQRTLrishdalmanGDELN--KQLKEQRLKCCSLEKQLHSVRfsERRVEELQDRINDLEKERELLKENYDKLY 366
Cdd:pfam01576 287 RNKAEKQRRDL----------GEELEalKTELEDTLDTTAAQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKH 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 367 NSAFSAAHEEQwklkeQQMKVQIAQLETALKSDLTDKTEVLDKLKTerdqnekLVQENRDLQLQCLQQKQRLHELQSRLk 446
Cdd:pfam01576 355 TQALEELTEQL-----EQAKRNKANLEKAKQALESENAELQAELRT-------LQQAKQDSEHKRKKLEGQLQELQARL- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 447 ffnQESDINADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQAThaetvQEL--EKTRNMLIMQHKINk 524
Cdd:pfam01576 422 ---SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQKLNLSTRLR- 492
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 145976944 525 dyQMEVETvTQKMENLQQDYELK--VEQYVHLLDIRAARIQK 564
Cdd:pfam01576 493 --QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
235-611 |
3.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 235 QLKRKENEIELSLLQLREQ---QATDQRSNIRDNVETI-KLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANG 310
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKtgiLIAALSEQLRKALFELdKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 311 DELNKQLKEQRLKCCSLEKQLHSVrfsERRVEELQDRINDLEKERELLKEnydklynsafsaaheeqwklKEQQMKVQIA 390
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESL---QEEAEELQEELEELQKERQDLEQ--------------------QRKQLEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 391 QLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQK 470
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 471 EQKNGDLSfLEKVDSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQ 550
Cdd:COG4372 220 LLEAKDSL-EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLL 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145976944 551 YVHLLDIRAARIQKLEAQLKdiaYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHI 611
Cdd:COG4372 299 ALLLNLAALSLIGALEDALL---AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVL 356
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-365 |
3.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNVETIKL 271
Cdd:COG3206 191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 272 HKQLVEKSNALSVIEGKF-------IQLQEKQRTLRISHDALMANG-DELNKQLKEQRLKCCSLEKQLHSVRFSERRVEE 343
Cdd:COG3206 269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
|
170 180
....*....|....*....|..
gi 145976944 344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206 349 LEAELRRLEREVEVARELYESL 370
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
324-582 |
4.39e-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: 43.98 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 324 CCSLEKQLHSVRFSERRVEELQDRINDLEKERELLKENYDKLynsafsaahEEQWKLKEQQMKVQIAQLEtALKSDLTDK 403
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---------LKQLAALERRIAALARRIR-ALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 404 TEVLDKLKTERDQNEKLVQENRDlQLQCLQQKQRLHELQSRLKFFnqesdINADDLSEALLLIKAqkeqkngdLSFLEKV 483
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKE-ELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQY--------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 484 DSKINKDLDRSMKELQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRA---A 560
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEeleA 227
|
250 260
....*....|....*....|..
gi 145976944 561 RIQKLEAQLKDIAYGTKQYKFK 582
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-543 |
5.72e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELERQNEVLKNrlisAKQQLQVQG 144
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK----AEEAKKADE 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 145 HRQTSYSRVQARvnTGRRRASASAGSQECPGKGLRFQNVDEAETVQPTLTKYSNSLLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:PTZ00121 1449 AKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 225 LEHLAEILKTQLKRKENEIELS--LLQLREQQATDQRSNIRDNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRIS 302
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 303 HDALMANGDELNKQLKEQRLKCCSLEKQLHSVRFSE----RRVEELQ--DRINDLEKERELLKENYDKLYNSAFSAAHEE 376
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 377 QWKLKEQQMKvqiaQLETALKSDLTDKTEVLDKLKTErdQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESD-IN 455
Cdd:PTZ00121 1687 EKKAAEALKK----EAEEAKKAEELKKKEAEEKKKAE--ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkIA 1760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 456 ADDLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQaTHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQ 535
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF-DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
....*...
gi 145976944 536 KMENLQQD 543
Cdd:PTZ00121 1840 NMQLEEAD 1847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
66-594 |
6.02e-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: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 66 QHARKQEDKIKRMATKLiRLVNDKKRYERVGggpKRLgrdVEMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGH 145
Cdd:COG4913 265 AAARERLAELEYLRAAL-RLWFAQRRLELLE---AEL---EELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 146 RQ-TSYSRVQARVNTGRRRASASAGSQECPGKGLRFQNVDEAETvqptltkysnslLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:COG4913 338 DRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE------------FAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 225 LEHLAEILKTQLKRKENEIELSLLQLREqqatdQRSNIRDNVETIKlhKQLVEksnALSVIE------GKFIQLQEKQ-- 296
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLER-----RKSNIPARLLALR--DALAE---ALGLDEaelpfvGELIEVRPEEer 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 297 ---------RTLRIS---------------------------------HDALMANGDE-----------------LNKQL 317
Cdd:COG4913 476 wrgaiervlGGFALTllvppehyaaalrwvnrlhlrgrlvyervrtglPDPERPRLDPdslagkldfkphpfrawLEAEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 318 KEQR-LKCCSLEKQLHSVRFS---------------------------------------ERRVEELQDRINDLEKEREL 357
Cdd:COG4913 556 GRRFdYVCVDSPEELRRHPRAitragqvkgngtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 358 LKENYDKL--YNSAFSAAHEEQWKLKE-QQMKVQIAQLETALKsDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQ 434
Cdd:COG4913 636 LEAELDALqeRREALQRLAEYSWDEIDvASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 435 KQrlhELQSRLKFFNQESDINADDLSEALLLIKAQK----EQKNGDLSfLEKVDSKINKDLDRSMKELQATHAETVQELE 510
Cdd:COG4913 715 IG---RLEKELEQAEEELDELQDRLEAAEDLARLELrallEERFAAAL-GDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 511 KTRnmlimqHKINKDYQMEVETVT----------QKMENLQQD----YELK------------VEQYVHLLD--IRAA-- 560
Cdd:COG4913 791 RAM------RAFNREWPAETADLDadleslpeylALLDRLEEDglpeYEERfkellnensiefVADLLSKLRraIREIke 864
|
650 660 670
....*....|....*....|....*....|....*
gi 145976944 561 RIQKLEAQLKDIAYGT-KQYKFKPEIMPDDSVDEF 594
Cdd:COG4913 865 RIDPLNDSLKRIPFGPgRYLRLEARPRPDPEVREF 899
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-539 |
7.84e-04 |
|
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: 43.88 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 108 MEEMIEQLQEKVHE------LERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQARvntgrrraSASAGSQECPGKGLRFQ 181
Cdd:TIGR00606 617 KEEQLSSYEDKLFDvcgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ--------LTDENQSCCPVCQRVFQ 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 182 NVDEAETVQPTLtkysNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQR-- 259
Cdd:TIGR00606 689 TEAELQEFISDL----QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlk 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 260 SNIRDN---VETIKLHKQLVEKSNA-LSVIEGKFIQLQEKQRtlRISHDALMANGDELNKQLKEQRLKccsLEKQLHSVR 335
Cdd:TIGR00606 765 NDIEEQetlLGTIMPEEESAKVCLTdVTIMERFQMELKDVER--KIAQQAAKLQGSDLDRTVQQVNQE---KQEKQHELD 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 336 FSERRVEELQDRINDLEKERELLKENYDKL--------YNSAFSAAHEEQW--KLKE--------QQMKVQIAQLETALK 397
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELkseklqigTNLQRRQQFEEQLveLSTEvqslireiKDAKEQDSPLETFLE 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 398 SDLTDKTEVLDKLKTERDQNEKLVQENRDLQLQCLQQkqrlhelqsRLKFFNQESDINADDlseallliKAQKEQK---- 473
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGY---------MKDIENKIQDGKDDY--------LKQKETElntv 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 474 NGDLSFLEKVDSKINKDLDRSMKELQATHA---------------ETVQELEKTRNMLIMQhkINKDYQMEVETVTQKME 538
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDIDTQKIqerwlqdnltlrkreNELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLE 1060
|
.
gi 145976944 539 N 539
Cdd:TIGR00606 1061 E 1061
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
107-363 |
1.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQA---RVNTgrRRASASAGSQECPGKGLRFQNV 183
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDleeLIAE--RRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 184 D-EAETVQPTLTKySNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTqLKRKENEIElSLLQLREQQAT--DQRs 260
Cdd:PRK02224 550 EaEAEEKREAAAE-AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIE-RLREKREALAElnDER- 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 261 niRDNVETIK-LHKQLVEKSNALSVIEGKfiqlQEKQRTlrishDALMANGDELNKQLKEQRlkcCSLEKQLHSVRFSER 339
Cdd:PRK02224 626 --RERLAEKReRKRELEAEFDEARIEEAR----EDKERA-----EEYLEQVEEKLDELREER---DDLQAEIGAVENELE 691
|
250 260
....*....|....*....|....
gi 145976944 340 RVEELQDRINDLEKERELLKENYD 363
Cdd:PRK02224 692 ELEELRERREALENRVEALEALYD 715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-416 |
1.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 221 QIEELEHLAEILKTQLKRKENEIElsllqlreqQATDQRSNIRDNVETIKlhKQLVEKSNALSVIEGKFIQLQEKQRTLR 300
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELA---------ALEARLEAAKTELEDLE--KEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 301 ishdalmaNGDELNkqlkeqrlkccSLEKQLHSVrfsERRVEELQDRINDLEKERELLKENYDKLynsafsaahEEQWKL 380
Cdd:COG1579 87 --------NNKEYE-----------ALQKEIESL---KRRISDLEDEILELMERIEELEEELAEL---------EAELAE 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 145976944 381 KEQQMKVQIAQLETALKsdltDKTEVLDKLKTERDQ 416
Cdd:COG1579 136 LEAELEEKKAELDEELA----ELEAELEELEAEREE 167
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
207-407 |
1.65e-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: 41.04 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 207 EIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIelsllqlreQQATDQRSNIrdnvetiklhKQLVEKSNalsvie 286
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKENRLLKRLQKRQEKAL---------GKYEGTESEL----------PQLIARHN------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 287 gkfiqlqEKQRTLRISHDALMANGDELNKQLKE------------QRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKE 354
Cdd:pfam15619 67 -------EEVRVLRERLRRLQEKERDLERKLKEkeaellrlrdqlKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEK 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 145976944 355 RELLkENYDKLYNSAFSAA-HEEQWKLKEQQMKVQIAQLE-TALKSDLTDKTEVL 407
Cdd:pfam15619 140 IQDL-ERKLELENKSFRRQlAAEKKKHKEAQEEVKILQEEiERLQQKLKEKEREL 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
338-531 |
1.97e-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: 42.19 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 338 ERRVEELQDRINDLEKERELLKENYDKLYNSAFSAahEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQN 417
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRD--REQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 418 EKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQ-------ESDINADDLSEALLLIK---AQKEQKNGDLSFLEKVDSKI 487
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKeeeAERKQLQAKLQQTEEELRSL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 145976944 488 NKDLdRSMKELQATHAETVQELEKTRNMLimQHKINKDYQMEVE 531
Cdd:pfam07888 191 SKEF-QELRNSLAQRDTQVLQLQDTITTL--TQKLTTAHRKEAE 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-585 |
2.49e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 200 LLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSL-----LQLREQQATDQRSNIRDNVETI--KLH 272
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMstqkaLEEDLQIATKTICQLTEEKEAQmeELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 273 KQLVEKSNALSVIEGKFIQLQEkqrTLRISHDALMANGDELNKQLKEQRLKCCSLEKQlhsVRFSERRVEELQDRINDLE 352
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEM---TKFKNNKEVELEELKKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 353 KERELLKEN--YDKLYNSAFSAAHEEQWKLKEQQ-----MKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENR 425
Cdd:pfam05483 416 EDEKLLDEKkqFEKIAEELKGKEQELIFLLQAREkeihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 426 DLQLQCLQQKQRLHELQSRLKffNQESDINADdlseallliKAQKEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAET 505
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELK--KHQEDIINC---------KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 506 VQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDI-AYGTKQYKFKPE 584
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLnAYEIKVNKLELE 644
|
.
gi 145976944 585 I 585
Cdd:pfam05483 645 L 645
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-573 |
2.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 341 VEELQDRINDLEKERELLKEnYDKLynsafsaaheeQWKLKEQQMKVQIAQLEtALKSDLTDKTEVLDKLKTERDQNEKL 420
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YREL-----------KEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 421 VQENRDLQLqclqqkqrlhelQSRLKFFNQESDINAddLSEALLLIKAQKEQKNGDLSFLEKVDSKINKDLDR---SMKE 497
Cdd:COG1196 262 LAELEAELE------------ELRLELEELELELEE--AQAEEYELLAELARLEQDIARLEERRRELEERLEEleeELAE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145976944 498 LQATHAETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYELKVEQYVHLLDIRAARIQKLEAQLKDIA 573
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
|
| C2B_RasGAP |
cd08675 |
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ... |
792-899 |
2.73e-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: 39.28 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 792 LHVTVKCCTGLQ----------SRASYLQPHAYVVYKffdfpdhdTAIVPSSNDPQFDDHMCFPVPMNMDLDRY---LKS 858
Cdd:cd08675 1 LSVRVLECRDLAlksngtcdpfARVTLNYSSKTDTKR--------TKVKKKTNNPRFDEAFYFELTIGFSYEKKsfkVEE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 145976944 859 ESLSFY-----VFDDSDTQENIYMGKVNVPLISLAHDKCISGIFEL 899
Cdd:cd08675 73 EDLEKSelrveLWHASMVSGDDFLGEVRIPLQGLQQAGSHQAWYFL 118
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
107-376 |
2.74e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 107 EMEEMIEQLQE--KVH--ELERQNEVLKNRLISAKQqlqvqghrqtsySRVQARVNTGRRRASASAGSQECPGKgLRFQN 182
Cdd:PRK05771 17 YKDEVLEALHElgVVHieDLKEELSNERLRKLRSLL------------TKLSEALDKLRSYLPKLNPLREEKKK-VSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 183 VDEAEtvqptltKYSNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKtqlKRKENEIELSLLQlreqqatdQRSNI 262
Cdd:PRK05771 84 LEELI-------KDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE---PWGNFDLDLSLLL--------GFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 263 RdnVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRtlrishDALMA-----NGDELNKQLKEQRLKccslEKQLHSVRFS 337
Cdd:PRK05771 146 S--VFVGTVPEDKLEELKLESDVENVEYISTDKGY------VYVVVvvlkeLSDEVEEELKKLGFE----RLELEEEGTP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 145976944 338 ERRVEELQDRINDLEKERELLKE---NYDKLYNSAFSAAHEE 376
Cdd:PRK05771 214 SELIREIKEELEEIEKERESLLEelkELAKKYLEELLALYEY 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-569 |
3.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELERQN 126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 127 EVLKNRLISAKQQLQVQGHRQtSYSRVQARVNTGRRRASASAGS-----QECPGKGLRFQNV-DEAETVQPTLT--KYSN 198
Cdd:PRK03918 283 KELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGieeriKELEEKEERLEELkKKLKELEKRLEelEERH 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 199 SLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLKRKEnEIELSLLQLREQQAT--DQRSNIRDNVETIKLHK--- 273
Cdd:PRK03918 362 ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIEELKKAKgkc 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 274 -------------QLVEKSNA-LSVIEGKFIQLQEKQRTLRishdalmANGDELNKQLKEQR--LKCCSLEKQLHSV--R 335
Cdd:PRK03918 439 pvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELAEQLKELeeK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 336 FSERRVEELQDRindlEKERELLKENYDKLyNSAFSAAHEEQWKLKEqqMKVQIAQLETALKSDLTDKTEVLDKLKTE-- 413
Cdd:PRK03918 512 LKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAELLKELEELgf 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 414 --RDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDiNADDLSEALLLIKAQKEQKNGDLSFLEKV-DSKINKD 490
Cdd:PRK03918 585 esVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-ELDKAFEELAETEKRLEELRKELEELEKKySEEEYEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 491 LDRSMKELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVETVTQKMENLQQDYElKVEQYVHLLDIRA- 559
Cdd:PRK03918 664 LREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVKKYKALLKERAl 742
|
570
....*....|
gi 145976944 560 ARIQKLEAQL 569
Cdd:PRK03918 743 SKVGEIASEI 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-514 |
3.84e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 312 ELNKQLKEQRLKCCSLEKQLHSVR--FSERRVEELQDRINDLEKERELLKENYDKLyNSAFSAAHEEQWKLKEQQMKVQI 389
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERL-EARLDALREELDELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 390 AQLEtALKSDLTDKTEVLDKLKTERDQneklvqenrdlqlqclqqkqrlheLQSRLKFFNQESDINADDLSEALLLIKAQ 469
Cdd:COG4913 338 DRLE-QLEREIERLERELEERERRRAR------------------------LEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 145976944 470 KEQKNGDLSFLEKVDSKINKDLDRSMKELQATHAEtVQELEKTRN 514
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAE-IASLERRKS 436
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
107-426 |
3.97e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 107 EMEEMIEQLQEKVHELERQNEVL--KNRLISAKQQLQ-----VQGHRQTSYSRVQAR---VNTGRRRASASAGSQECPGK 176
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILaeDEKLLDEKKQFEkiaeeLKGKEQELIFLLQARekeIHDLEIQLTAIKTSEEHYLK 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 177 GLRFQNVD-EAETVQPT-LTKYSNSLLEEARG----------EIRNLENVI-----QSQR--GQIEELEHLA-------E 230
Cdd:pfam05483 472 EVEDLKTElEKEKLKNIeLTAHCDKLLLENKEltqeasdmtlELKKHQEDIinckkQEERmlKQIENLEEKEmnlrdelE 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 231 ILKTQLKRKENEIELSLlqlrEQQATDQRSNIRDNVETIKLHKQLVEKSNAL-SVIEGKFIQLQEKQRtlriSHDALMAN 309
Cdd:pfam05483 552 SVREEFIQKGDEVKCKL----DKSEENARSIEYEVLKKEKQMKILENKCNNLkKQIENKNKNIEELHQ----ENKALKKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 310 GDELNKQLKEQRLKCCSLEKQLHSVRfserrvEELQDRINDLEKERELLKENYDKLYNS--------------------- 368
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAK------QKFEEIIDNYQKEIEDKKISEEKLLEEvekakaiadeavklqkeidkr 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 369 ---------AFSAAHEEQW--------------KLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENR 425
Cdd:pfam05483 698 cqhkiaemvALMEKHKHQYdkiieerdselglyKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
.
gi 145976944 426 D 426
Cdd:pfam05483 778 E 778
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-364 |
4.23e-03 |
|
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: 41.35 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LKRKENEIElsllQLREQQATDQRSNiRDNVETI-KLH 272
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRER-LEELESLkKEN 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 273 KQLVEKSNALSVI----EGKFIQLQEKQRTLRISHDALMANGDELNKQLKEQRLKCCSLEKQL---HSVRFSERRVEELQ 345
Cdd:pfam10174 478 KDLKEKVSALQPEltekESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIN 557
|
170
....*....|....*....
gi 145976944 346 DRINDLEKERELLKENYDK 364
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGK 576
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-446 |
5.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 27 LQETSTARTVKTRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDV 106
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE---------EEE 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 107 EMEEMIEQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYsrvQARVNTGRRRASASAGSQECPGKGLRFQNVDEA 186
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY---EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 187 ETVQPTLtkysnsllEEARGEIRNLENViqsqrgqiEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDnv 266
Cdd:COG1196 537 EAALEAA--------LAAALQNIVVEDD--------EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG-- 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 267 etiklhkQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKQLkEQRLKCCSLEKQLHSVRFSERRVEELQD 346
Cdd:COG1196 599 -------AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL-AGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 347 RINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQNEKLVQENRD 426
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
410 420
....*....|....*....|
gi 145976944 427 LQLQCLQQKQRLHELQSRLK 446
Cdd:COG1196 751 EALEELPEPPDLEELERELE 770
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
199-578 |
6.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 199 SLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIELSLLQLREQQATDQRSNIRDNvETIKLHKQLVEK 278
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-MKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 279 SNALSVIEGKFIQLQE-KQRTLRISHDALMANGDELN------KQLKEQRLKCCSLEKQLHSVRFSERRVEELQ------ 345
Cdd:PRK01156 262 ESDLSMELEKNNYYKElEERHMKIINDPVYKNRNYINdyfkykNDIENKKQILSNIDAEINKYHAIIKKLSVLQkdyndy 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 346 ----DRINDLEKERELLKENYDKlYNSAFSAAheEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTERDQ-NEKL 420
Cdd:PRK01156 342 ikkkSRYDDLNNQILELEGYEMD-YNSYLKSI--ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEiNVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 421 VQENRDL---QLQCLQQKQRLHELQSRLKFFNQES--DINADDLSEALL--LIKAQKEQKNG---DLSFLEKVDSKINKD 490
Cdd:PRK01156 419 QDISSKVsslNQRIRALRENLDELSRNMEMLNGQSvcPVCGTTLGEEKSnhIINHYNEKKSRleeKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 491 LDRSMKELQATHAETVQELEKTRNML---------------IMQHKINKDYQMEVETVTQKMENLQQDYE--LKVEQYVH 553
Cdd:PRK01156 499 IVDLKKRKEYLESEEINKSINEYNKIesaradledikikinELKDKHDKYEEIKNRYKSLKLEDLDSKRTswLNALAVIS 578
|
410 420
....*....|....*....|....*..
gi 145976944 554 LLDIRAARIQKLE--AQLKDIAYGTKQ 578
Cdd:PRK01156 579 LIDIETNRSRSNEikKQLNDLESRLQE 605
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
315-517 |
6.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 315 KQLKEQRLKCCSLEKQLHSVRFSERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLEt 394
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 395 alksDLTDKTEVLDKLKTERDQNEKLVQENRDlqlqclqqkqrlhELQSRLKFFNQESDINADDLSEALLLIKAQKEQKN 474
Cdd:COG4717 150 ----ELEERLEELRELEEELEELEAELAELQE-------------ELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 145976944 475 GDLSFLEKVDSKINKDLDRSMKELQATHAEtvQELEKTRNMLI 517
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLL 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-405 |
6.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQQATDQRsNIRDNVETIKLH-KQLVEKS 279
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID----KLQAEIAEAEA-EIEERREELGERaRALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 280 NALSVIE--------GKFIqlqekQRTLRIShdALMANGDELNKQLKEQRLKccsLEKQLHSVRFSERRVEELQDRINDL 351
Cdd:COG3883 100 GSVSYLDvllgsesfSDFL-----DRLSALS--KIADADADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 145976944 352 EKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTE 405
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-513 |
7.04e-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: 40.93 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 48 EELEDRFLRLHDEnilLKQHARKQEDKIKRMA--TKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQ--------- 116
Cdd:pfam01576 299 EELEALKTELEDT---LDTTAAQQELRSKREQevTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEqakrnkanl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 117 EKV-HELERQNEVLKNRLISAKQQLQVQGHR----QTSYSRVQARVNTGRRRA---------------SASAGSQECPGK 176
Cdd:pfam01576 376 EKAkQALESENAELQAELRTLQQAKQDSEHKrkklEGQLQELQARLSESERQRaelaeklsklqseleSVSSLLNEAEGK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 177 GLRFQNvdEAETVQPTLTKYSNSLLEEAR------GEIRNLENVIQSQRGQIEELEHLAEILKTQL----------KRKE 240
Cdd:pfam01576 456 NIKLSK--DVSSLESQLQDTQELLQEETRqklnlsTRLRQLEDERNSLQEQLEEEEEAKRNVERQLstlqaqlsdmKKKL 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 241 NEIELSLLQLREQQATDQRsnirdnvETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRISHDALMANGDELNKqlKEQ 320
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLQR-------ELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK--KQK 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 321 RLKCCSLEKQLHSVRFSERR--------------------VEELQDRINDLEKERELLKENYDKLYNS---AFSAAHE-E 376
Cdd:pfam01576 605 KFDQMLAEEKAISARYAEERdraeaeareketralslaraLEEALEAKEELERTNKQLRAEMEDLVSSkddVGKNVHElE 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 377 QWK-LKEQQ---MKVQIAQLETALKSdltdkTEVLdKLKTERDQNEKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQES 452
Cdd:pfam01576 685 RSKrALEQQveeMKTQLEELEDELQA-----TEDA-KLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAEL 758
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145976944 453 DINADDLSEALllikAQKEQKNGDLSFLEKVDSKINKDLD---RSMKELQATHAETVQELEKTR 513
Cdd:pfam01576 759 EDERKQRAQAV----AAKKKLELDLKELEAQIDAANKGREeavKQLKKLQAQMKDLQRELEEAR 818
|
|
| C2B_RasA3 |
cd04010 |
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ... |
792-887 |
7.69e-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: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 792 LHVTVKCCTGLQSRASYLQPHAYV--VYKFFDFPDHDTAIVPSSNDPQFDDHMCFPVPMNMDLDRYLK---SESLSFY-- 864
Cdd:cd04010 2 LSVRVIECSDLALKNGTCDPYASVtlIYSNKKQDTKRTKVKKKTNNPQFDEAFYFDVTIDSSPEKKQFempEEDAEKLel 81
|
90 100
....*....|....*....|....*.
gi 145976944 865 ---VFDDSDTQENIYMGKVNVPLISL 887
Cdd:cd04010 82 rvdLWHASMGGGDVFLGEVRIPLRGL 107
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-354 |
8.13e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 35 TVKTRQAVSRVSREELEDRFLRLHDENiLLKQHARKQEDKIKRMAT------KLIRLVNDKKRYerVGGGPKrLGRDVEM 108
Cdd:PRK04863 760 VVKIADRQWRYSRFPEVPLFGRAAREK-RIEQLRAEREELAERYATlsfdvqKLQRLHQAFSRF--IGSHLA-VAFEADP 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 109 EEMIEQLQEKVHELER-------QNEVLKNRLISAKQQLQvQGHRQTSYSRVQARVNTGRRRASASAGSQECPGKGL--- 178
Cdd:PRK04863 836 EAELRQLNRRRVELERaladhesQEQQQRSQLEQAKEGLS-ALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRfvq 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 179 RFQN-VDEAETVQPTLT-------------KYSNSLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQ 235
Cdd:PRK04863 915 QHGNaLAQLEPIVSVLQsdpeqfeqlkqdyQQAQQTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQR 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 236 LKRKENEIELSLLQLREQQATDQRSNirdnvetiKLHKQLVeksnalSVIEGKFIQLQEKQR-----TLRISHDA---LM 307
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYN--------QVLASLK------SSYDAKRQMLQELKQelqdlGVPADSGAeerAR 1059
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 145976944 308 ANGDELNKQLKEQRLKCCSLEKQLhsvRFSERRVEELQDRINDLEKE 354
Cdd:PRK04863 1060 ARRDELHARLSANRSRRNQLEKQL---TFCEAEMDNLTKKLRKLERD 1103
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
304-424 |
8.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 304 DALMANGDELNKQLKEQRLKCCSLEKQLhsvrfsERRVEELQDRINDLEKERELLKENYDKLYNSAFSAAHEE------- 376
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEALLKEA------EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEadeiike 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145976944 377 -QWKLKEQQMKVQIAQLETALKSdLTDKTEVLDKLKTERDQNEKLVQEN 424
Cdd:PRK00409 593 lRQLQKGGYASVKAHELIEARKR-LNKANEKKEKKKKKQKEKQEELKVG 640
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
113-513 |
9.13e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 113 EQLQEKVHELERQNEVLKNRLISAKQQLQVQGHRQTSYSRVQA---RVNTGRRRASA-------------SAGSQECP-- 174
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEApdwEQSIGKVISPEllhrtdldpevwdGSVGGELNly 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 175 GKGLRFQNVDEAETVQPTltkysnsllEEARGEIRNLENVIQSQRGQIEELEHlaeilktqlkrkeneiELSLLqlreqq 254
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASE---------EELRERLDKAEEALQSAREKQAAAEE----------------QLVQA------ 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 255 atdqrsnirdNVETIKLHKQLVEKSNALSVIEGKFIQLQEKQRTLRishdalmangDELNKQLKEQRlkccslekqlhsv 334
Cdd:pfam12128 631 ----------NGELEKASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERK------------- 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 335 RFSERRVEELQDRINDLEKERELLKENYDKLYNSAfSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDKLKTER 414
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA-RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 415 DQN-----------EKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEALLLIKAQKEQKNGDLSFLEKV 483
Cdd:pfam12128 757 KRDlaslgvdpdviAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIAD 836
|
410 420 430
....*....|....*....|....*....|
gi 145976944 484 DSKINKDLDRSMKELQATHAETVQELEKTR 513
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
109-569 |
9.57e-03 |
|
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: 40.19 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 109 EEMIEQLQEKVHELERQN-------EVLKNRLiSAKQQlqvqghrqtSYSRVQARVNTGRRRasasagsqecpgkglrfq 181
Cdd:pfam10174 302 ESELLALQTKLETLTNQNsdckqhiEVLKESL-TAKEQ---------RAAILQTEVDALRLR------------------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 182 nVDEAETVQPTLTKYSNSLLEEA---RGEIRNLENVIQSQRGQIEELEHLAEILKTQLKRKENEIElsllQLREQ-QATD 257
Cdd:pfam10174 354 -LEEKESFLNKKTKQLQDLTEEKstlAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLA----GLKERvKSLQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 258 QRSNIRDNVETiKLHKQLVEKSNalsVIEgkfiQLQE-KQRTLRISHDALmangDELNKQLKEQRLKCCSLEKQLHSvrf 336
Cdd:pfam10174 429 TDSSNTDTALT-TLEEALSEKER---IIE----RLKEqREREDRERLEEL----ESLKKENKDLKEKVSALQPELTE--- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 337 SERRVEELQDRINDLeKERELLKENYDKLYNSAFSAAHEEQWKLKEQQMKVQIAQLETALKSDLTDKTEVLDK-LKTERD 415
Cdd:pfam10174 494 KESSLIDLKEHASSL-ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQeVARYKE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 416 QN-------EKLVQENRDLQLQCLQQKQRLHELQSRLKFFNQESDINADDLSEalllikAQKEQKNGDLSFLEKVdSKIN 488
Cdd:pfam10174 573 ESgkaqaevERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKH------GQQEMKKKGAQLLEEA-RRRE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976944 489 KDLDRSMKELQAthAETVQELEKTRNmlimqhkinkdyqmEVETVTQKMENLQQDYElkvEQYVHLLDIRAARIQKLEAQ 568
Cdd:pfam10174 646 DNLADNSQQLQL--EELMGALEKTRQ--------------ELDATKARLSSTQQSLA---EKDGHLTNLRAERRKQLEEI 706
|
.
gi 145976944 569 L 569
Cdd:pfam10174 707 L 707
|
|
| |
