|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-716 |
0e+00 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 995.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 327 PQSLSSPSTRLLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTAG-GKGTPSG--TPATSPP 396
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEAaGEATPETtpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 397 PAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNLPDFLGDLA-SEEDS 469
Cdd:pfam04388 389 KQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 470 IEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGSSVNPE-----PLH 534
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 535 SSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 614
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 615 HFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSPPSDELRTLRDQLLL 694
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 575771884 695 LHNQLLYERFKRQQHALRNRRL 716
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
701-947 |
3.69e-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: 64.69 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 701 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 780
Cdd:TIGR02168 290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 781 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 851
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 852 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 931
Cdd:TIGR02168 442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
|
250 260
....*....|....*....|..
gi 575771884 932 SQASG------QLLAAESRYEA 947
Cdd:TIGR02168 516 SGLSGilgvlsELISVDEGYEA 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-973 |
7.51e-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: 63.54 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQEQRDTMvTQLHSQIRQLQ 780
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 781 HdreEFYNQSQELQT----------KLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLN 846
Cdd:TIGR02168 288 K---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 847 RQLLVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLE 922
Cdd:TIGR02168 365 AELEELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 575771884 923 QKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRLR 973
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLD 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
753-966 |
1.21e-09 |
|
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: 59.94 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 753 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 832
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 833 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 912
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 575771884 913 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 966
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
712-959 |
2.67e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 712 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL-QHDR--EEFYN 788
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 789 QSQELQTKLEDCRN-----MIAELRVELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 845
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 846 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 921
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 575771884 922 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 959
Cdd:TIGR04523 436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
705-985 |
4.43e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 705 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDRE 784
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 785 EFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 864
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 865 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 944
Cdd:COG1196 394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 575771884 945 YEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEA 985
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-958 |
8.88e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQH 781
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 782 DREEFYNQSQELQTKLEDCRNMIAELRVELKKannkvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 861
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 862 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 941
Cdd:COG1196 359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250
....*....|....*..
gi 575771884 942 ESRYEAQRKITRVLELE 958
Cdd:COG1196 435 EEEEEEEEALEEAAEEE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
710-974 |
3.94e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 710 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQHDREEFYNQ 789
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 790 SQELQTKLEDCRNMIAELRVE---LKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 865
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 866 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKK------DHLLLEQKKYLEDVKSQASGQLL 939
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVI 256
|
250 260 270
....*....|....*....|....*....|....*
gi 575771884 940 AAEsRYEAQRKITRVLELEILDLYGRLEKDGRLRK 974
Cdd:COG4372 257 LKE-IEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
722-958 |
9.99e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 722 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 801
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 802 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 870
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 871 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 949
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569
|
....*....
gi 575771884 950 KITRVLELE 958
Cdd:PRK02224 570 AREEVAELN 578
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
726-966 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 726 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 801
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 802 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 873
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 874 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 942
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
|
250 260
....*....|....*....|....
gi 575771884 943 SRYEAQRKITRVLELEILDLYGRL 966
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
749-968 |
1.71e-07 |
|
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: 54.77 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 749 VSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQV 828
Cdd:COG4942 13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 829 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRKE----LEKNRSHLLQQNQR 898
Cdd:COG4942 89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREqaeeLRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 899 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 968
Cdd:COG4942 169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
736-984 |
1.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 736 QLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKAN 815
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 816 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 895
Cdd:COG1196 288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 896 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKL 975
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
....*....
gi 575771884 976 EEDRAEAAE 984
Cdd:COG1196 444 LEEAAEEEA 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
712-969 |
2.69e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 712 RNRRLLRKVIRAAALEEHNAAMkdqLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLH---SQIRQLQHDREEFYN 788
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 789 QSQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQSKHP 868
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE-------AEELQEEL---EELQKERQDLEQQ-----------RKQLEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 869 DTTKEVEmMKTAYRKELEKNRSHLLQQNQRLDASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQ 948
Cdd:COG4372 140 ELQSEIA-EREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
250 260
....*....|....*....|.
gi 575771884 949 RKITRVLELEILDLYGRLEKD 969
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSAL 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
741-950 |
2.85e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 741 EKDIQMWKVSLQKEQARYSQLQEQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNK 817
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 818 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 897
Cdd:COG3883 95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 575771884 898 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 950
Cdd:COG3883 158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
682-901 |
2.87e-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: 55.06 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 682 SDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIRAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 757
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 758 YSQLQEQRDTMVTQlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVEL----KKANNKVCHT-ELLLSQVSQKL 832
Cdd:TIGR02168 889 LALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIE 964
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771884 833 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKhpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDA 901
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL-----KERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
739-968 |
5.02e-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: 54.29 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 739 LQEKDIQMWKVSLQKEQA-RYSQLQEQRDTM--------VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRV 809
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAeRYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 810 ELKKANNKVCHTELLLSQVSQKLSNSES----VQQQMEFLNRQLLVLgevnELYLEQLQSKHPDTTKEVEMMKTAYrKEL 885
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQqkqiLRERLANLERQLEEL----EAQLEELESKLDELAEELAELEEKL-EEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 886 EKNrshLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ---ASGQLLAAESRYEA-QRKITRVLElEILD 961
Cdd:TIGR02168 350 KEE---LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERlEDRRERLQQ-EIEE 425
|
....*..
gi 575771884 962 LYGRLEK 968
Cdd:TIGR02168 426 LLKKLEE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
722-973 |
7.67e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 722 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 798
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 799 DCRNMIAELRVELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 868
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 869 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 937
Cdd:PRK02224 634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
|
250 260 270
....*....|....*....|....*....|....*.
gi 575771884 938 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLR 973
Cdd:PRK02224 707 VEALEALYD------EAEELE--SMYGDLRAELRQR 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
677-968 |
1.52e-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: 52.76 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 677 GGS--PPSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKdQLKLQEKDIQMwkvsLQKE 754
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQ----LEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 755 QARYSQLQEQrdtmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL-----LLSQVS 829
Cdd:TIGR02169 732 EEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 830 QKLSNSESVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPDTTKEVEMMKTAYRK-------------ELEKNR 889
Cdd:TIGR02169 805 EEVSRIEARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaalrDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 890 SHLLQQNQRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEILDLY 963
Cdd:TIGR02169 885 GDLKKERDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
....*
gi 575771884 964 GRLEK 968
Cdd:TIGR02169 965 EEIRA 969
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
705-959 |
1.62e-06 |
|
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: 52.66 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 705 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQeqrdtmvtqlhsQIRQLQHDRE 784
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 785 EFYNQSQELQTKLEDCRNMIAELRvELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 847
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 848 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 924
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 575771884 925 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 959
Cdd:TIGR00618 411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
716-956 |
2.39e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 716 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQ---- 789
Cdd:pfam05483 305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 790 SQELQTK---LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 866
Cdd:pfam05483 383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 867 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 936
Cdd:pfam05483 459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
|
250 260
....*....|....*....|
gi 575771884 937 QLLAAESRYEAQRKITRVLE 956
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELE 551
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
713-864 |
3.96e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 713 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQEQRDTMVTQL---HSQIRQLQHDREEFY 787
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771884 788 NQ-SQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 864
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
702-969 |
4.97e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNRrLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQ 778
Cdd:COG4372 41 DKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 779 LQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLVL 852
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 853 GEVNELYLEQLQSKHPdTTKEVEMMKTAYRKELEKNRSHLLQQNQRL-DASQRRVLELESLLAKKDHLLLEQKKYLEDVK 931
Cdd:COG4372 200 EELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270
....*....|....*....|....*....|....*...
gi 575771884 932 SQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 969
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
713-959 |
4.98e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 713 NRRLLR-KV--IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE 784
Cdd:pfam13868 12 NSKLLAaKCnkERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 785 EFYNQS-QELQTKLEDCRNMIAE-LRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQ 862
Cdd:pfam13868 91 EEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EYLKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 863 LQSKhpDTTKEVEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASG 936
Cdd:pfam13868 164 KAER--EEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQ 233
|
250 260
....*....|....*....|...
gi 575771884 937 QLLAAESRYEAQRKITRVLELEI 959
Cdd:pfam13868 234 RQELQQAREEQIELKERRLAEEA 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
745-960 |
6.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 745 QMWKVSLQKEQARYSQLQEQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL 823
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 824 LLSQVSQklsnsesvQQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 903
Cdd:COG4717 124 LLQLLPL--------YQELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771884 904 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 960
Cdd:COG4717 191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
769-968 |
1.09e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 769 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR-------NMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQ 841
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 842 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 906
Cdd:TIGR02168 763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771884 907 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 968
Cdd:TIGR02168 843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
683-962 |
1.17e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 683 DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 762
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 763 EQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQ 839
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 840 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 913
Cdd:TIGR02168 866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 575771884 914 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 962
Cdd:TIGR02168 946 SEEYSLTLEeaEALENKIEDDEE-----------EARRRLKR-LENKIKEL 984
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
727-931 |
1.94e-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: 49.20 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 727 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------EQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 800
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 801 RNMIAELRVELKK-ANNKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 872
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771884 873 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 931
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
715-974 |
2.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 715 RLLRKVIRaaaLEEHNAAMKDQLKLQeKDIQMWKVSLQKEQARYSQLQEQRDTM----------VTQLHSQIRQLqhdRE 784
Cdd:PRK03918 149 KVVRQILG---LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPEL---RE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 785 EFYNQSQELQtKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQ 862
Cdd:PRK03918 222 ELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 863 LQSKHPDTTKEVEMMKTAYR---KELEKNRSHLLQQNQRLDASQRRVLELESLLA--KKDHLLLEQ----KKYLEDVKSQ 933
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEakakKEELERLKKR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 575771884 934 ASGQLLA-AESRYEAQRKITRVLELEILDLYGRLekdGRLRK 974
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEIEEEISKITARI---GELKK 419
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
678-893 |
4.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 678 GSPPSDELRTLRDQL----LLLHNQLLYERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQK 753
Cdd:COG4717 63 GRKPELNLKELKELEeelkEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 754 EQARySQLQEqrdtmvtqLHSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRVELKKANNKVchTELLLSQVSQKLS 833
Cdd:COG4717 135 EALE-AELAE--------LPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 834 NSESVQQQMEFLNRQLlvlgEVNELYLEQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 893
Cdd:COG4717 200 ELEELQQRLAELEEEL----EEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
736-973 |
4.13e-05 |
|
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: 47.79 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 736 QLKLQEKDIQMWKVSLQKE-QARYSQLQEQRDTMVTQlHSQIRQLQHDREEFynqSQELQTKLEDCRNMIAElrvelkka 814
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAElKQKENKLQENRKIIEAQ-RKAIQELQFENEKV---SLKLEEEIQENKDLIKE-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 815 NNKVCHTELLLSQVSQKlsnSESVQQQMEFlNRQllvlgEVNELYLeqlqskhpDTTKEVEMMKTAYrKELEknrshLLQ 894
Cdd:pfam05483 150 NNATRHLCNLLKETCAR---SAEKTKKYEY-ERE-----ETRQVYM--------DLNNNIEKMILAF-EELR-----VQA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771884 895 QNQRLDASqrrvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLElEILDLYGRLEKDGRLR 973
Cdd:pfam05483 207 ENARLEMH----FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQ 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
702-956 |
5.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT 770
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 771 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL----------------LLSQVSQ 830
Cdd:COG4717 185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 831 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 894
Cdd:COG4717 265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771884 895 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 956
Cdd:COG4717 342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
701-954 |
1.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 701 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDT------- 767
Cdd:COG4913 587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 768 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQ 839
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 840 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 901
Cdd:COG4913 737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 902 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 954
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
711-959 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 711 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVS--------------------------LQ 752
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISytspdpelaaavanalaeayleqnleLR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 753 KEQARYSQ--LQEQRDtmvtQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHT 821
Cdd:COG3206 170 REEARKALefLEEQLP----ELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 822 ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDA 901
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILA 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771884 902 SQRRvlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 959
Cdd:COG3206 317 SLEA--ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
723-818 |
3.02e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 42.19 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 723 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 802
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 575771884 803 MIAELRVELKKANNKV 818
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
724-865 |
5.89e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.09 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 724 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrn 802
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771884 803 mIAELRVELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 865
Cdd:pfam07926 73 -IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
725-950 |
6.22e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 725 ALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYSQLQEQRDTMVT------QLHSQIRQLQHDREEFYNQSQELQTKL 797
Cdd:pfam00038 22 FLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 798 EDCRNMIAELRVELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEM 876
Cdd:pfam00038 99 TSAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 877 --------------MKTAYRKELEKNRSHL----------LQQ-----NQRLDASQRRVLEL----ESLLAKKDHlLLEQ 923
Cdd:pfam00038 161 daarkldltsalaeIRAQYEEIAAKNREEAeewyqskleeLQQaaarnGDALRSAKEEITELrrtiQSLEIELQS-LKKQ 239
|
250 260
....*....|....*....|....*..
gi 575771884 924 KKYLEDvksqasgQLLAAESRYEAQRK 950
Cdd:pfam00038 240 KASLER-------QLAETEERYELQLA 259
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
731-922 |
6.26e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 731 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRVE 810
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 811 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 887
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 575771884 888 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 922
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
754-932 |
6.62e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 754 EQARYSQLQEQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRNMIA 805
Cdd:pfam05622 242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 806 ELRVELKKANNKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 883
Cdd:pfam05622 322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 575771884 884 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 932
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
702-910 |
6.74e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNRRLLRkviRAAALEEHNAAMKDQLKLQEKDIQMWKvslqkEQARYSQLQEQRDTMVTQ---LHSQIRQ 778
Cdd:COG3206 159 EAYLEQNLELRREEARK---ALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQlseLESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 779 LQHDREEFYNQSQELQTKLEDCRNMIAELR--VELKKANNKVCHTELLLSQVSQKLS-NSESVQQqmefLNRQLlvlGEV 855
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYTpNHPDVIA----LRAQI---AAL 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 575771884 856 NELYLEQLQSKHPDTTKEVEMMKtAYRKELEKNRSHLLQQNQRLDASQRRVLELE 910
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQ-AREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
703-951 |
9.98e-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: 43.19 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 703 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQ---EQRDtmvtqlhsqiRQL 779
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 780 QHDREEfynqSQELQTKLEDCRNMIAELRvelkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 859
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 860 LEQLQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---G 936
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerS 566
|
250
....*....|....*
gi 575771884 937 QLLAAESRYEAQRKI 951
Cdd:pfam17380 567 RLEAMEREREMMRQI 581
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
707-812 |
1.03e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 707 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQEQRDTMvtQLHSQ-----IRQLQH 781
Cdd:pfam13851 50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 575771884 782 DREEFYNQS----QELQTKLEdCRNMIAELRVELK 812
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
760-929 |
1.31e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 41.29 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 760 QLQEQRDTMVTQLHSQIRQLQHDREE----FYNQSQELQTKLEDCRNMIAELRVELK--------KANNKVCHTELLLSQ 827
Cdd:pfam14988 15 EKQKKIEKLWNQYVQECEEIERRRQElasrYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklKESQEREIQDLEEEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 828 VSQKLSNSESVQQ-QMEFLNRQLLVLGEVNELYLEQL-QSKHPDTTKEVEMMKTAYRK--------------ELEKNRSH 891
Cdd:pfam14988 95 EKVRAETAEKDREaHLQFLKEKALLEKQLQELRILELgERATRELKRKAQALKLAAKQalsefcrsikrenrQLQKELLQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 575771884 892 LLQQNQRLDASQRRvleleslLAKKDHLLLEQKKYLED 929
Cdd:pfam14988 175 LIQETQALEAIKSK-------LENRKQRLKEEQWYLEA 205
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
702-961 |
1.43e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 755
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 756 ARYSQLQEQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 798
Cdd:PRK10246 682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 799 ---DCRNMIAEL-------RVELKKAN--NKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 865
Cdd:PRK10246 762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 866 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKK--DHLL-LEQKKYLEDVKSQASG 936
Cdd:PRK10246 838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKegDKFRkFAQGLTLDNLVWLANQ 912
|
330 340
....*....|....*....|....*
gi 575771884 937 QLLAAESRYEAQRKITRVLELEILD 961
Cdd:PRK10246 913 QLTRLHGRYLLQRKASEALELEVVD 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-962 |
1.64e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 706 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLqhdree 785
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------ 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 786 fynqsQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEV---NEL 858
Cdd:TIGR02168 785 -----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDiesLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 859 YLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQL 938
Cdd:TIGR02168 860 EIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------EL 929
|
250 260
....*....|....*....|....
gi 575771884 939 LAAESRYEAQRKITRVLELEILDL 962
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
705-947 |
1.70e-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: 42.50 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 705 KRQQHALRnRRLLRKVIRAAALEEH-----NAAMKDQLKLQEKDIQMWK----VSLQKEQARYSQLQEQRDTMVTQLHSQ 775
Cdd:pfam10174 481 KEKVSALQ-PELTEKESSLIDLKEHasslaSSGLKKDSKLKSLEIAVEQkkeeCSKLENQLKKAHNAEEAVRTNPEINDR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 776 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLV 851
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 852 LGEVNElylEQLQSKHPDTTKEvEMMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV- 930
Cdd:pfam10174 640 EARRRE---DNLADNSQQLQLE-ELMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIl 707
|
250
....*....|....*....
gi 575771884 931 --KSQAsgqLLAAESRYEA 947
Cdd:pfam10174 708 emKQEA---LLAAISEKDA 723
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
833-944 |
1.96e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.97 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 833 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 901
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 575771884 902 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 944
Cdd:pfam10473 92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
712-922 |
2.67e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 712 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtQLHSQIRQLQHDREefyNQS 790
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLA---KIR 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 791 QELQTKLEDCRNMI----AELRVELKKANNKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNEL 858
Cdd:pfam12128 404 EARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771884 859 YLEQLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 922
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
705-973 |
2.84e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 705 KRQQHALRNRRLLRKVIRAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRdtmvtqlHSQIRQLQHDRE 784
Cdd:pfam13868 62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 785 EFYNQSQEL------QTKLEDCRNM------------IAELRVELKKANnkvchtELLLSQVSQKLSNSESVQQQMEFLn 846
Cdd:pfam13868 134 EFNEEQAEWkelekeEEREEDERILeylkekaereeeREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDEL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 847 RQLLVLGEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 922
Cdd:pfam13868 207 RAKLYQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771884 923 QKK-----YLEDVKSQasgqllaAESRyEAQRKITRVLELEILDLYGRLEKDGRLR 973
Cdd:pfam13868 283 KRRmkrleHRRELEKQ-------IEER-EEQRAAEREEELEEGERLREEEAERRER 330
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
723-974 |
3.30e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 723 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQArysQLQEQRDTMvtqlhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 801
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESENA---ELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 802 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQSKHPDTTKevemmktay 881
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 882 RKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYLEDVksqaSGQLLAAEsryEAQRKITRVLELEIL 960
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKLEED----AGTLEALE---EGKKRLQRELEALTQ 559
|
250 260
....*....|....*....|.
gi 575771884 961 DL------YGRLEK-DGRLRK 974
Cdd:pfam01576 560 QLeekaaaYDKLEKtKNRLQQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
702-916 |
3.36e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 702 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 779
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 780 Q--------------HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFl 845
Cdd:COG4942 114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575771884 846 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 916
Cdd:COG4942 190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
788-969 |
3.45e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 788 NQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 863
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 864 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLElesllakkDHLLLEQKKYLEDVKSQASgQLLAAE 942
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLA-ELAALR 166
|
170 180
....*....|....*....|....*..
gi 575771884 943 SRYEAQRKITRVLELEILDLYGRLEKD 969
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
705-922 |
4.21e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 705 KRQQHALRNRRLlRKVIRAAAleehnaamKDQLKLQEKDIQMWKVSLQKEQARYSQL-QEQRDTMVTQLHSQIRQLQHDR 783
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDAP--------AELRELRQELAALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 784 EEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNELYLEQ 862
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDMLEQEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771884 863 LQSkhpdttkevEMMKTAYRKELEKNRSHLLQQNQRLDA-----SQRRVLELESLLAKKDHLLLE 922
Cdd:pfam12795 173 LSN---------NNRQDLLKARRDLLTLRIQRLEQQLQAlqellNEKRLQEAEQAVAQTEQLAEE 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
722-849 |
4.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 722 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQE-----------QRDTMVTQLHSQ----IRQLQHDREEF 786
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771884 787 YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 849
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
734-933 |
4.85e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 734 KDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVE 810
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 811 LKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-----------LNRQLLVLGEV--NELYLEQLQSKHpdttKEVEMM 877
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdLEDELNKDDFElkKENLEKEIDEKN----KEIEEL 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771884 878 KTAYrKELEKNRShllQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 933
Cdd:TIGR04523 574 KQTQ-KSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
733-958 |
4.88e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 733 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNM----I 804
Cdd:COG5185 346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 805 AELRVELKKANNKVchtelllsQVSQKLSN---SESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEMMKT-- 879
Cdd:COG5185 423 EELQRQIEQATSSN--------EEVSKLLNeliSELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESrv 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 880 -AYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 958
Cdd:COG5185 495 sTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
765-925 |
5.17e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 765 RDTMVTQLHSQ---IRQLQHDREEFYNQSQELQTK-LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNS----- 835
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDIErLYRMIDILNDAQQQIKWTNQPRIYLEVALVKLCEQAAASpeydt 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 836 --ESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEV------------EMMKTAYRKELEKNRSH---LLQQNQR 898
Cdd:PRK05563 370 elEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKkkkykvprgkiyKVLKEATRQDLELLKNVwgeILESLKA 449
|
170 180
....*....|....*....|....*...
gi 575771884 899 LDASQRRVL-ELESLLAKKDHLLLEQKK 925
Cdd:PRK05563 450 QRKSLRALLvNSEPVAASEDTVVLAFEY 477
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
760-845 |
6.19e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 39.17 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 760 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 834
Cdd:cd16855 9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 575771884 835 sesvQQQMEFL 845
Cdd:cd16855 86 ----QLRMELA 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
701-818 |
7.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 701 YERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQ-EKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 779
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdEEEL----RAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 575771884 780 QH-----DREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKV 818
Cdd:COG4717 419 EEllealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
718-907 |
9.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 718 RKVIRAAALEEHNAAMKDQLKLQEKDIqmwkvslqkEQaRYSQLQEQRdTMVTQLHSQIRQLQHDREEFYNQSQELQTKL 797
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAEL---------EQ-RLRQQQNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 798 EDCRNMIAE-------LRVELKKANNKVchTEL----------------LLSQVSQKLSNSESVQQQMEFLnrqllvlge 854
Cdd:COG3096 567 EELEEQAAEaveqrseLRQQLEQLRARI--KELaarapawlaaqdalerLREQSGEALADSQEVTAAMQQL--------- 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 575771884 855 vnelyLEQLqskhpdttkevemmktayrKELEKNRSHLLQQNQRLDASQRRVL 907
Cdd:COG3096 636 -----LERE-------------------REATVERDELAARKQALESQIERLS 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
726-933 |
9.49e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 726 LEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQEL-----QTKleDC 800
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneEKK--EL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 801 RNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ-----LQSKHP 868
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQkslkkKQEEKQ 588
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771884 869 DTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 933
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
703-962 |
9.52e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 703 RFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHD 782
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 783 REE----------FYNQSQELQTKLEDcRNMIAELRVEL--KKANNKVCHTELL------------------LSQVSQKL 832
Cdd:TIGR00606 908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 833 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QSKHPDTTKEVEMMKTAYRKELEKNR-SHLLQQNQRLDASQRRV 906
Cdd:TIGR00606 987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLI 1066
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771884 907 LELESLLAKKDHLLLEQKKYLEdvKSQASGQLLAAESRYEAQRKITRVLELEILDL 962
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
734-933 |
9.90e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 734 KDQLKLQEKDIQmwkvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKK 813
Cdd:TIGR04523 116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771884 814 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQSKHPDTTKEVEMMK---TAYRKELEK 887
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKdeqNKIKKQLSE 271
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 575771884 888 NRSHLLQQNQRLDASQRRVLELESLLAKkdhllLEQKK---YLEDVKSQ 933
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKeqdWNKELKSE 315
|
|
| |
