|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-710 |
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: 979.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 327 PQSLSSPSTRLLPEPLqaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GKGTPSG--TPATSPP 395
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 396 PAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNLPDFLGDLA-SEEDS 468
Cdd:pfam04388 389 KQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 469 IEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQGSSVNPE-----PLH 533
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 534 SSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPPYDHLFEVALPKTAC 613
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 614 HFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFG-----DELRTLRDQLLL 688
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGgsapsDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 575771787 689 LHNQLLYERFKRQQHALRNRRL 710
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
695-941 |
4.34e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 695 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 774
Cdd:TIGR02168 290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 775 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 845
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 846 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 925
Cdd:TIGR02168 442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
|
250 260
....*....|....*....|..
gi 575771787 926 SQASG------QLLAAESRYEA 941
Cdd:TIGR02168 516 SGLSGilgvlsELISVDEGYEA 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-967 |
9.07e-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: 63.15 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQEQRDTMvTQLHSQIRQLQ 774
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 775 HDREEFYN-------QSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLNRQL 843
Cdd:TIGR02168 288 KELYALANeisrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 844 LVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLEQKK 919
Cdd:TIGR02168 368 EELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELE 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 575771787 920 YLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRLR 967
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLD 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
747-960 |
1.52e-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: 59.55 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 747 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 826
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 827 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 906
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 575771787 907 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 960
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
706-953 |
4.03e-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: 60.80 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 706 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL-QHDR--EEFYN 782
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 783 QSQELQTKLEDCRN-----MIAELRVELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 839
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 840 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 915
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 575771787 916 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 953
Cdd:TIGR04523 436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
699-979 |
5.17e-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: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 699 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDRE 778
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 779 EFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 858
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 859 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 938
Cdd:COG1196 394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 575771787 939 YEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEA 979
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
696-952 |
9.76e-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: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQH 775
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 776 DREEFYNQSQELQTKLEDCRNMIAELRVELKKannkvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 855
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 856 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 935
Cdd:COG1196 359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250
....*....|....*..
gi 575771787 936 ESRYEAQRKITRVLELE 952
Cdd:COG1196 435 EEEEEEEEALEEAAEEE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
704-968 |
5.71e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 704 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQHDREEFYNQ 783
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 784 SQELQTKLEDCRNMIAELRVE---LKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 859
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 860 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKK------DHLLLEQKKYLEDVKSQASGQLL 933
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVI 256
|
250 260 270
....*....|....*....|....*....|....*
gi 575771787 934 AAEsRYEAQRKITRVLELEILDLYGRLEKDGRLRK 968
Cdd:COG4372 257 LKE-IEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
716-952 |
1.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 716 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 795
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 796 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 864
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 865 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 943
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569
|
....*....
gi 575771787 944 KITRVLELE 952
Cdd:PRK02224 570 AREEVAELN 578
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
720-960 |
1.84e-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: 55.50 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 720 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 795
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 796 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 867
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 868 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 936
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
|
250 260
....*....|....*....|....
gi 575771787 937 SRYEAQRKITRVLELEILDLYGRL 960
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
743-962 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 743 VSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQV 822
Cdd:COG4942 13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 823 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRKE----LEKNRSHLLQQNQR 892
Cdd:COG4942 89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREqaeeLRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 893 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 962
Cdd:COG4942 169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
730-978 |
2.20e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 730 QLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKAN 809
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 810 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 889
Cdd:COG1196 288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 890 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKL 969
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
....*....
gi 575771787 970 EEDRAEAAE 978
Cdd:COG1196 444 LEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
642-895 |
2.78e-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: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 642 MEVLDRLIEQGAGAHSKELSRLSlpsksvdwtHFGDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIRAAAL 720
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALD---------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDI 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 721 EEHNAAMKDQLKLQEK---DIQMWKVSLQKEQARYSQLQEQRDTMVTQlhsqIRQLQHDREEFYNQSQELQTKLEDCRNM 797
Cdd:TIGR02168 855 ESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 798 IAELRVEL----KKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKhpdttKEVEMMK 872
Cdd:TIGR02168 931 LEGLEVRIdnlqERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL-----KERYDFL 1005
|
250 260
....*....|....*....|...
gi 575771787 873 TAYRKELEKNRSHLLQQNQRLDA 895
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
735-944 |
2.83e-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: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 735 EKDIQMWKVSLQKEQARYSQLQEQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNK 811
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 812 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 891
Cdd:COG3883 95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 575771787 892 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 944
Cdd:COG3883 158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
706-963 |
3.97e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 706 RNRRLLRKVIRAAALEEHNAAMkdqLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLH---SQIRQLQHDREEFYN 782
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 783 QSQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQSKHP 862
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE-------AEELQEEL---EELQKERQDLEQQ-----------RKQLEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 863 DTTKEVEmMKTAYRKELEKNRSHLLQQNQRLDASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQ 942
Cdd:COG4372 140 ELQSEIA-EREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
250 260
....*....|....*....|.
gi 575771787 943 RKITRVLELEILDLYGRLEKD 963
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSAL 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
716-967 |
9.04e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 716 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 792
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 793 DCRNMIAELRVELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 862
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 863 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 931
Cdd:PRK02224 634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
|
250 260 270
....*....|....*....|....*....|....*.
gi 575771787 932 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLR 967
Cdd:PRK02224 707 VEALEALYD------EAEELE--SMYGDLRAELRQR 734
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
699-953 |
2.01e-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: 52.28 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 699 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQeqrdtmvtqlhsQIRQLQHDRE 778
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 779 EFYNQSQELQTKLEDCRNMIAELRvELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 841
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 842 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 918
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 575771787 919 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 953
Cdd:TIGR00618 411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
710-950 |
2.94e-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: 51.65 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 710 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQ---- 783
Cdd:pfam05483 305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 784 SQELQTK---LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 860
Cdd:pfam05483 383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 861 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 930
Cdd:pfam05483 459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
|
250 260
....*....|....*....|
gi 575771787 931 QLLAAESRYEAQRKITRVLE 950
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELE 551
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
707-858 |
4.25e-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: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 707 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQEQRDTMVTQL---HSQIRQLQHDREEFY 781
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771787 782 NQ-SQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 858
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
696-963 |
6.36e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNRrLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQ 772
Cdd:COG4372 41 DKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 773 LQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLVL 846
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 847 GEVNELYLEQLQSKHPdTTKEVEMMKTAYRKELEKNRSHLLQQNQRL-DASQRRVLELESLLAKKDHLLLEQKKYLEDVK 925
Cdd:COG4372 200 EELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270
....*....|....*....|....*....|....*...
gi 575771787 926 SQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 963
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
676-962 |
6.53e-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: 50.45 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 676 GDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKdQLKLQEKDIQMwkvsLQKEQARYSQL 755
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQ----LEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 756 QEQrdtmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL-----LLSQVSQKLSNSE 830
Cdd:TIGR02169 739 LEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 831 SVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPDTTKEVEMMKTAYRK-------------ELEKNRSHLLQQN 890
Cdd:TIGR02169 812 ARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaalrDLESRLGDLKKER 891
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771787 891 QRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEILDLYGRLEK 962
Cdd:TIGR02169 892 DELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
715-953 |
8.24e-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: 49.15 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 715 IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQS-QELQ 788
Cdd:pfam13868 23 ERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKlQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 789 TKLEDCRNMIAE-LRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQLQSKhpDTTKE 867
Cdd:pfam13868 102 QMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EYLKEKAER--EEERE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 868 VEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASGQLLAAESRYEA 941
Cdd:pfam13868 173 AEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQRQELQQAREEQ 244
|
250
....*....|..
gi 575771787 942 QRKITRVLELEI 953
Cdd:pfam13868 245 IELKERRLAEEA 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-954 |
8.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 739 QMWKVSLQKEQARYSQLQEQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL 817
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 818 LLSQVSQklsnsesvQQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 897
Cdd:COG4717 124 LLQLLPL--------YQELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771787 898 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 954
Cdd:COG4717 191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-962 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 763 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR-------NMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQ 835
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 836 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 900
Cdd:TIGR02168 763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771787 901 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 962
Cdd:TIGR02168 843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-956 |
1.28e-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: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 677 DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 756
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 757 EQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQ 833
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 834 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 907
Cdd:TIGR02168 866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 575771787 908 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 956
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 ... |
721-925 |
2.40e-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: 48.81 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 721 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------EQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 794
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 795 RNMIAELRVELKK-ANNKVCHTELLLSQVSQKL-------SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 866
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNEEVtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771787 867 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 925
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
709-968 |
2.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 709 RLLRKVIRaaaLEEHNAAMKDQLKLQeKDIQMWKVSLQKEQARYSQLQEQRDTM----------VTQLHSQIRQLqhdRE 778
Cdd:PRK03918 149 KVVRQILG---LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPEL---RE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 779 EFYNQSQELQtKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQ 856
Cdd:PRK03918 222 ELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 857 LQSKHPDTTKEVEMMKTAYR---KELEKNRSHLLQQNQRLDASQRRVLELESLLA--KKDHLLLEQ----KKYLEDVKSQ 927
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEakakKEELERLKKR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 575771787 928 ASGQLLA-AESRYEAQRKITRVLELEILDLYGRLekdGRLRK 968
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEIEEEISKITARI---GELKK 419
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
730-967 |
5.07e-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: 47.41 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 730 QLKLQEKDIQMWKVSLQKE-QARYSQLQEQRDTMVTQlHSQIRQLQHDREEFynqSQELQTKLEDCRNMIAElrvelkka 808
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAElKQKENKLQENRKIIEAQ-RKAIQELQFENEKV---SLKLEEEIQENKDLIKE-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 809 NNKVCHTELLLSQVSQKlsnSESVQQQMEFlNRQllvlgEVNELYLeqlqskhpDTTKEVEMMKTAYrKELEknrshLLQ 888
Cdd:pfam05483 150 NNATRHLCNLLKETCAR---SAEKTKKYEY-ERE-----ETRQVYM--------DLNNNIEKMILAF-EELR-----VQA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771787 889 QNQRLDASqrrvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLElEILDLYGRLEKDGRLR 967
Cdd:pfam05483 207 ENARLEMH----FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQ 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
695-887 |
5.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 695 YERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARySQLQEqrdtmvtqLHSQIRQLQ 774
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAE--------LPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 775 HDREEFynqsQELQTKLEDCRNMIAELRVELKKANNKVchTELLLSQVSQKLSNSESVQQQMEFLNRQLlvlgEVNELYL 854
Cdd:COG4717 153 ERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEEL----EEAQEEL 222
|
170 180 190
....*....|....*....|....*....|...
gi 575771787 855 EQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 887
Cdd:COG4717 223 EELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
696-950 |
6.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT 764
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 765 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL----------------LLSQVSQ 824
Cdd:COG4717 185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 825 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 888
Cdd:COG4717 265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771787 889 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 950
Cdd:COG4717 342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
695-948 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 695 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDT------- 761
Cdd:COG4913 587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 762 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQ 833
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 834 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 895
Cdd:COG4913 737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 896 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 948
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
705-953 |
3.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 705 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVS--------------------------LQ 746
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISytspdpelaaavanalaeayleqnleLR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 747 KEQARYSQ--LQEQRDtmvtQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHT 815
Cdd:COG3206 170 REEARKALefLEEQLP----ELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 816 ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDA 895
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILA 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771787 896 SQRRvlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 953
Cdd:COG3206 317 SLEA--ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
717-812 |
3.37e-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: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 717 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 796
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 575771787 797 MIAELRVELKKANNKV 812
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
725-916 |
6.49e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 725 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRVE 804
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 805 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 881
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 575771787 882 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 916
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
696-904 |
7.05e-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: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNRRLLRkviRAAALEEHNAAMKDQLKLQEKDIQMWKvslqkEQARYSQLQEQRDTMVTQ---LHSQIRQ 772
Cdd:COG3206 159 EAYLEQNLELRREEARK---ALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQlseLESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 773 LQHDREEFYNQSQELQTKLEDCRNMIAELR--VELKKANNKVCHTELLLSQVSQKLS-NSESVQQqmefLNRQLlvlGEV 849
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYTpNHPDVIA----LRAQI---AAL 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 575771787 850 NELYLEQLQSKHPDTTKEVEMMKtAYRKELEKNRSHLLQQNQRLDASQRRVLELE 904
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQ-AREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
718-859 |
7.09e-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: 40.70 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 718 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrn 796
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771787 797 mIAELRVELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 859
Cdd:pfam07926 73 -IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
719-944 |
8.05e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 719 ALEEHNAAMkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT------QLHSQIRQLQHDREEFYNQSQELQTKLE 792
Cdd:pfam00038 22 FLEQQNKLL--ETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDFRQKYEDELNLRT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 793 DCRNMIAELRVELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEM- 870
Cdd:pfam00038 100 SAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 871 -------------MKTAYRKELEKNRSHL----------LQQ-----NQRLDASQRRVLEL----ESLLAKKDHlLLEQK 918
Cdd:pfam00038 162 aarkldltsalaeIRAQYEEIAAKNREEAeewyqskleeLQQaaarnGDALRSAKEEITELrrtiQSLEIELQS-LKKQK 240
|
250 260
....*....|....*....|....*.
gi 575771787 919 KYLEDvksqasgQLLAAESRYEAQRK 944
Cdd:pfam00038 241 ASLER-------QLAETEERYELQLA 259
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
748-926 |
8.36e-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: 43.52 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 748 EQARYSQLQEQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRNMIA 799
Cdd:pfam05622 242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 800 ELRVELKKANNKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 877
Cdd:pfam05622 322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 575771787 878 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 926
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
697-945 |
1.02e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 697 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQ---EQRDtmvtqlhsqiRQL 773
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 774 QHDREEfynqSQELQTKLEDCRNMIAELRvelkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 853
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 854 LEQLQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---G 930
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerS 566
|
250
....*....|....*
gi 575771787 931 QLLAAESRYEAQRKI 945
Cdd:pfam17380 567 RLEAMEREREMMRQI 581
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
701-806 |
1.28e-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: 41.43 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 701 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQEQRDTMvtQLHSQ-----IRQLQH 775
Cdd:pfam13851 50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 575771787 776 DREEFYNQS----QELQTKLEdCRNMIAELRVELK 806
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
754-923 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 754 QLQEQRDTMVTQLHSQIRQLQHDREE----FYNQSQELQTKLEDCRNMIAELRVELK--------KANNKVCHTELLLSQ 821
Cdd:pfam14988 15 EKQKKIEKLWNQYVQECEEIERRRQElasrYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklKESQEREIQDLEEEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 822 VSQKLSNSESVQQ-QMEFLNRQLLVLGEVNELYLEQL-QSKHPDTTKEVEMMKTAYRK--------------ELEKNRSH 885
Cdd:pfam14988 95 EKVRAETAEKDREaHLQFLKEKALLEKQLQELRILELgERATRELKRKAQALKLAAKQalsefcrsikrenrQLQKELLQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 575771787 886 LLQQNQRLDASQRRvleleslLAKKDHLLLEQKKYLED 923
Cdd:pfam14988 175 LIQETQALEAIKSK-------LENRKQRLKEEQWYLEA 205
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
696-955 |
1.73e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 749
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 750 ARYSQLQEQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 792
Cdd:PRK10246 682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 793 ---DCRNMIAEL-------RVELKKAN--NKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 859
Cdd:PRK10246 762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 860 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKKD---HLLLEQKKYLEDVKSQASG 930
Cdd:PRK10246 838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKEgdkFRKFAQGLTLDNLVWLANQ 912
|
330 340
....*....|....*....|....*
gi 575771787 931 QLLAAESRYEAQRKITRVLELEILD 955
Cdd:PRK10246 913 QLTRLHGRYLLQRKASEALELEVVD 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-956 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 700 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLqhdree 779
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------ 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 780 fynqsQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEV---NEL 852
Cdd:TIGR02168 785 -----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDiesLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 853 YLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQL 932
Cdd:TIGR02168 860 EIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------EL 929
|
250 260
....*....|....*....|....
gi 575771787 933 LAAESRYEAQRKITRVLELEILDL 956
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
699-941 |
2.11e-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: 42.12 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 699 KRQQHALRnRRLLRKVIRAAALEEH-----NAAMKDQLKLQEKDIQMWK----VSLQKEQARYSQLQEQRDTMVTQLHSQ 769
Cdd:pfam10174 481 KEKVSALQ-PELTEKESSLIDLKEHasslaSSGLKKDSKLKSLEIAVEQkkeeCSKLENQLKKAHNAEEAVRTNPEINDR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 770 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLV 845
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 846 LGEVNElylEQLQSKHPDTTKEvEMMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV- 924
Cdd:pfam10174 640 EARRRE---DNLADNSQQLQLE-ELMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIl 707
|
250
....*....|....*....
gi 575771787 925 --KSQAsgqLLAAESRYEA 941
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, ... |
827-938 |
2.38e-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: 39.59 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 827 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 895
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 575771787 896 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 938
Cdd:pfam10473 92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
706-916 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 706 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtQLHSQIRQLQHDREefyNQS 784
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLA---KIR 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 785 QELQTKLEDCRNMI----AELRVELKKANNKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNEL 852
Cdd:pfam12128 404 EARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771787 853 YLEQLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 916
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
696-910 |
3.65e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 696 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 773
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 774 Q--------------HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFl 839
Cdd:COG4942 114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575771787 840 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 910
Cdd:COG4942 190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
782-963 |
3.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 782 NQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 857
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 858 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLElesllakkDHLLLEQKKYLEDVKSQASgQLLAAE 936
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLA-ELAALR 166
|
170 180
....*....|....*....|....*..
gi 575771787 937 SRYEAQRKITRVLELEILDLYGRLEKD 963
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
717-968 |
3.98e-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: 41.31 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 717 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQArysQLQEQRDTMvtqlhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 795
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESENA---ELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 796 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQSKHPDTTKevemmktay 875
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 876 RKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYLEDVksqaSGQLLAAEsryEAQRKITRVLELEIL 954
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKLEED----AGTLEALE---EGKKRLQRELEALTQ 559
|
250 260
....*....|....*....|.
gi 575771787 955 DL------YGRLEK-DGRLRK 968
Cdd:pfam01576 560 QLeekaaaYDKLEKtKNRLQQ 580
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-843 |
4.27e-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: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 716 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQE-----------QRDTMVTQLHSQ----IRQLQHDREEF 780
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771787 781 YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 843
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
699-967 |
4.37e-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: 40.67 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 699 KRQQHALRNRRLLRKVIRAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRdtmvtqlHSQIRQLQHDRE 778
Cdd:pfam13868 62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 779 EFYNQSQEL------QTKLEDCRNM------------IAELRVELKKANnkvchtELLLSQVSQKLSNSESVQQQMEFLn 840
Cdd:pfam13868 134 EFNEEQAEWkelekeEEREEDERILeylkekaereeeREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDEL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 841 RQLLVLGEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDhLLLE 916
Cdd:pfam13868 207 RAKLYQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE-QEEA 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 575771787 917 QKKYLEDVKSQASGQLLAAESryEAQRKITRVLELEILDLYGRLEKDGRLR 967
Cdd:pfam13868 282 EKRRMKRLEHRRELEKQIEER--EEQRAAEREEELEEGERLREEEAERRER 330
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
699-916 |
4.54e-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: 39.98 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 699 KRQQHALRNRRLlRKVIRAAAleehnaamKDQLKLQEKDIQMWKVSLQKEQARYSQL-QEQRDTMVTQLHSQIRQLQHDR 777
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDAP--------AELRELRQELAALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 778 EEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNELYLEQ 856
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDMLEQEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771787 857 LQSkhpdttkevEMMKTAYRKELEKNRSHLLQQNQRLDA-----SQRRVLELESLLAKKDHLLLE 916
Cdd:pfam12795 173 LSN---------NNRQDLLKARRDLLTLRIQRLEQQLQAlqellNEKRLQEAEQAVAQTEQLAEE 228
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
759-919 |
5.14e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 759 RDTMVTQLHSQ---IRQLQHDREEFYNQSQELQTK-LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNS----- 829
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDIErLYRMIDILNDAQQQIKWTNQPRIYLEVALVKLCEQAAASpeydt 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 830 --ESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEV------------EMMKTAYRKELEKNRSH---LLQQNQR 892
Cdd:PRK05563 370 elEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKkkkykvprgkiyKVLKEATRQDLELLKNVwgeILESLKA 449
|
170 180
....*....|....*....|....*...
gi 575771787 893 LDASQRRVL-ELESLLAKKDHLLLEQKK 919
Cdd:PRK05563 450 QRKSLRALLvNSEPVAASEDTVVLAFEY 477
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
727-952 |
5.75e-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: 40.71 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 727 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNM----I 798
Cdd:COG5185 346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 799 AELRVELKKANNKVCHTelllSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEqLQSKHPDTTKEVEMMKT---AY 875
Cdd:COG5185 423 EELQRQIEQATSSNEEV----SKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKEDLNEELTQIESrvsTL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771787 876 RKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 952
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
728-927 |
6.32e-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: 40.77 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 728 KDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVE 804
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 805 LKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-----------LNRQLLVLGEV--NELYLEQLQSKHpdttKEVEMM 871
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdLEDELNKDDFElkKENLEKEIDEKN----KEIEEL 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771787 872 KTAYrKELEKNRShllQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 927
Cdd:TIGR04523 574 KQTQ-KSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
754-839 |
7.33e-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: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 754 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 828
Cdd:cd16855 9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 575771787 829 sesvQQQMEFL 839
Cdd:cd16855 86 ----QLRMELA 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
695-812 |
8.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771787 695 YERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQ-EKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 773
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdEEEL----RAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 575771787 774 QH-----DREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKV 812
Cdd:COG4717 419 EEllealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| |
