|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-724 |
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: 974.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 327 PQSLSSPSTRLLPEPLqvrchsaclhllylpaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GK 397
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF----------------PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 398 GTPSG--TPATSPPPAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNL 469
Cdd:pfam04388 375 ATPETtpAKDSPYLKQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 470 PDFLGDLA-SEEDSIEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQG 538
Cdd:pfam04388 455 PDFIKDLAlSSEDSVEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 539 SSVNPE-----PLHSSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPP 613
Cdd:pfam04388 535 PATTPEskpsaLAEDGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLP 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 614 YDHLFEVALPKTACHFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFG--- 690
Cdd:pfam04388 615 YEHLFDLALPKTASLFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGgsa 694
|
730 740 750
....*....|....*....|....*....|....*.
gi 568914075 691 --DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRL 724
Cdd:pfam04388 695 psDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
709-955 |
3.42e-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: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 709 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 788
Cdd:TIGR02168 290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 789 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 859
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 860 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 939
Cdd:TIGR02168 442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
|
250 260
....*....|....*....|..
gi 568914075 940 SQASG------QLLAAESRYEA 955
Cdd:TIGR02168 516 SGLSGilgvlsELISVDEGYEA 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
710-981 |
6.67e-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: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQEQRDTMvTQLHSQIRQLQ 788
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 789 HdreEFYNQSQELQT----------KLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLN 854
Cdd:TIGR02168 288 K---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 855 RQLLVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLE 930
Cdd:TIGR02168 365 AELEELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568914075 931 QKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRLR 981
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLD 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
761-974 |
1.35e-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: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 761 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 840
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 841 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 920
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568914075 921 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 974
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
720-967 |
2.10e-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: 61.96 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 720 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL-QHDR--EEFYN 796
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 797 QSQELQTKLEDCRN-----MIAELRVELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 853
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 854 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 929
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568914075 930 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 967
Cdd:TIGR04523 436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
713-993 |
4.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 713 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDRE 792
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 793 EFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 872
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 873 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 952
Cdd:COG1196 394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568914075 953 YEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEA 993
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
710-966 |
8.73e-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: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQH 789
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 790 DREEFYNQSQELQTKLEDCRNMIAELRVELKKannkvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 869
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 870 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 949
Cdd:COG1196 359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250
....*....|....*..
gi 568914075 950 ESRYEAQRKITRVLELE 966
Cdd:COG1196 435 EEEEEEEEALEEAAEEE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
718-982 |
3.13e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 718 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQHDREEFYNQ 797
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 798 SQELQTKLEDCRNMIAELRVE---LKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 873
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 874 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKK------DHLLLEQKKYLEDVKSQASGQLL 947
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVI 256
|
250 260 270
....*....|....*....|....*....|....*
gi 568914075 948 AAEsRYEAQRKITRVLELEILDLYGRLEKDGRLRK 982
Cdd:COG4372 257 LKE-IEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
730-966 |
9.66e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 730 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 809
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 810 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 878
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 879 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 957
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569
|
....*....
gi 568914075 958 KITRVLELE 966
Cdd:PRK02224 570 AREEVAELN 578
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
734-974 |
1.42e-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: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 734 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 809
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 810 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 881
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 882 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 950
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
|
250 260
....*....|....*....|....
gi 568914075 951 SRYEAQRKITRVLELEILDLYGRL 974
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
757-976 |
1.47e-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: 55.16 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 757 VSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQV 836
Cdd:COG4942 13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 837 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRK----ELEKNRSHLLQQNQR 906
Cdd:COG4942 89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARReqaeELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 907 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 976
Cdd:COG4942 169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
749-958 |
1.73e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 749 EKDIQMWKVSLQKEQARYSQLQEQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNK 825
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 826 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 905
Cdd:COG3883 95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568914075 906 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 958
Cdd:COG3883 158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
744-992 |
1.96e-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: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 744 QLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKAN 823
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 824 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 903
Cdd:COG1196 288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 904 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKL 983
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
....*....
gi 568914075 984 EEDRAEAAE 992
Cdd:COG1196 444 LEEAAEEEA 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
720-977 |
2.03e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 720 RNRRLLRKVIRAAALEEHNAAMkdqLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLH---SQIRQLQHDREEFYN 796
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 797 QSQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQSKHP 876
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE-------AEELQEEL---EELQKERQDLEQQ-----------RKQLEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 877 DTTKEVEmMKTAYRKELEKNRSHLLQQNQRLDASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQ 956
Cdd:COG4372 140 ELQSEIA-EREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
250 260
....*....|....*....|.
gi 568914075 957 RKITRVLELEILDLYGRLEKD 977
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSAL 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
656-909 |
2.27e-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: 55.45 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 656 MEVLDRLIEQGAGAHSKELSRLSlpsksvdwtHFGDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIRAAAL 734
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALD---------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDI 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 735 EEHNAAMKDQLKLQEK---DIQMWKVSLQKEQARYSQLQEQRDTMVTQlhsqIRQLQHDREEFYNQSQELQTKLEDCRNM 811
Cdd:TIGR02168 855 ESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 812 IAELRVEL----KKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKhpdttKEVEMMK 886
Cdd:TIGR02168 931 LEGLEVRIdnlqERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL-----KERYDFL 1005
|
250 260
....*....|....*....|...
gi 568914075 887 TAYRKELEKNRSHLLQQNQRLDA 909
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
730-981 |
7.17e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 730 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 806
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 807 DCRNMIAELRVELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 876
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 877 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 945
Cdd:PRK02224 634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
|
250 260 270
....*....|....*....|....*....|....*.
gi 568914075 946 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLR 981
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 ... |
713-967 |
1.65e-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: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 713 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQeqrdtmvtqlhsQIRQLQHDRE 792
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 793 EFYNQSQELQTKLEDCRNMIAELRvELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 855
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 856 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 932
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 568914075 933 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 967
Cdd:TIGR00618 411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
724-964 |
2.23e-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: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 724 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQ---- 797
Cdd:pfam05483 305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 798 SQELQTK---LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 874
Cdd:pfam05483 383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 875 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 944
Cdd:pfam05483 459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
|
250 260
....*....|....*....|
gi 568914075 945 QLLAAESRYEAQRKITRVLE 964
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELE 551
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
721-872 |
3.76e-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: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 721 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQEQRDTMVTQL---HSQIRQLQHDREEFY 795
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568914075 796 NQ-SQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 872
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
710-977 |
3.99e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNRrLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQ 786
Cdd:COG4372 41 DKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 787 LQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLVL 860
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 861 GEVNELYLEQLQSKHPdTTKEVEMMKTAYRKELEKNRSHLLQQNQRL-DASQRRVLELESLLAKKDHLLLEQKKYLEDVK 939
Cdd:COG4372 200 EELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270
....*....|....*....|....*....|....*...
gi 568914075 940 SQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 977
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
733-976 |
4.89e-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: 51.22 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 733 ALEEHNAAMKD---QLKLQEKDIQMwkvsLQKEQARYSQLQEQrdtmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 809
Cdd:TIGR02169 703 RLDELSQELSDasrKIGEIEKEIEQ----LEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 810 NMIAELRVELKKANNKVCHTEL-----LLSQVSQKLSNSESVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPD 877
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIpeiqaELSKLEEEVSRIEARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 878 TTKEVEMMKTAYRK-------------ELEKNRSHLLQQNQRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKS 940
Cdd:TIGR02169 852 IEKEIENLNGKKEEleeeleeleaalrDLESRLGDLKKERDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270
....*....|....*....|....*....|....*...
gi 568914075 941 QAS--GQLLAAESRYEAQRKITRVLELEILDLYGRLEK 976
Cdd:TIGR02169 932 ELSeiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
721-967 |
5.34e-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: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 721 NRRLLR-KV--IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE 792
Cdd:pfam13868 12 NSKLLAaKCnkERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 793 EFYNQS-QELQTKLEDCRNMIAE-LRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQ 870
Cdd:pfam13868 91 EEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EYLKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 871 LQSKhpDTTKEVEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASG 944
Cdd:pfam13868 164 KAER--EEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQ 233
|
250 260
....*....|....*....|...
gi 568914075 945 QLLAAESRYEAQRKITRVLELEI 967
Cdd:pfam13868 234 RQELQQAREEQIELKERRLAEEA 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
753-968 |
7.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 753 QMWKVSLQKEQARYSQLQEQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRNMIAELRVELKKANNKvchtel 831
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREE------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 832 lLSQVSQKLSNSESVqQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 911
Cdd:COG4717 118 -LEKLEKLLQLLPLY-QELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914075 912 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 968
Cdd:COG4717 191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
777-976 |
9.80e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 777 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR-------NMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQ 849
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 850 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 914
Cdd:TIGR02168 763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914075 915 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 976
Cdd:TIGR02168 843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
691-970 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 691 DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 770
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 771 EQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQ 847
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 848 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 921
Cdd:TIGR02168 866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568914075 922 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 970
Cdd:TIGR02168 946 SEEYSLTLEeaEALENKIEDDEE-----------EARRRLKR-LENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
723-982 |
2.00e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 723 RLLRKVIRaaaLEEHNAAMKDQLKLQeKDIQMWKVSLQKEQARYSQLQEQRDTM----------VTQLHSQIRQLqhdRE 792
Cdd:PRK03918 149 KVVRQILG---LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPEL---RE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 793 EFYNQSQELQtKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQ 870
Cdd:PRK03918 222 ELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 871 LQSKHPDTTKEVEMMKTAYR---KELEKNRSHLLQQNQRLDASQRRVLELESLLA--KKDHLLLEQ----KKYLEDVKSQ 941
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEakakKEELERLKKR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568914075 942 ASGQLLA-AESRYEAQRKITRVLELEILDLYGRLekdGRLRK 982
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEIEEEISKITARI---GELKK 419
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
735-939 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 735 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------EQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 808
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 809 RNMIAELRVELKK-ANNKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 880
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568914075 881 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 939
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
744-981 |
3.79e-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: 48.18 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 744 QLKLQEKDIQMWKVSLQKE-QARYSQLQEQRDTMVTQlHSQIRQLQHDREEFynqSQELQTKLEDCRNMIAElrvelkka 822
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAElKQKENKLQENRKIIEAQ-RKAIQELQFENEKV---SLKLEEEIQENKDLIKE-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 823 NNKVCHTELLLSQVSQKlsnSESVQQQMEFlNRQllvlgEVNELYLeqlqskhpDTTKEVEMMKTAYrKELEknrshLLQ 902
Cdd:pfam05483 150 NNATRHLCNLLKETCAR---SAEKTKKYEY-ERE-----ETRQVYM--------DLNNNIEKMILAF-EELR-----VQA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914075 903 QNQRLDASqrrvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLElEILDLYGRLEKDGRLR 981
Cdd:pfam05483 207 ENARLEMH----FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQ 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
709-901 |
4.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 709 YERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARySQLQEqrdtmvtqLHSQIRQLQ 788
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAE--------LPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 789 HDREEFynqsQELQTKLEDCRNMIAELRVELKKANNKVchTELLLSQVSQKLSNSESVQQQMEFLNRQLlvlgEVNELYL 868
Cdd:COG4717 153 ERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEEL----EEAQEEL 222
|
170 180 190
....*....|....*....|....*....|...
gi 568914075 869 EQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 901
Cdd:COG4717 223 EELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-964 |
6.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT 778
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 779 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL----------------LLSQVSQ 838
Cdd:COG4717 185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 839 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 902
Cdd:COG4717 265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914075 903 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 964
Cdd:COG4717 342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
709-962 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 709 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDT------- 775
Cdd:COG4913 587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 776 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQ 847
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 848 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 909
Cdd:COG4913 737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 910 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 962
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
719-967 |
2.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 719 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVS--------------------------LQ 760
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISytspdpelaaavanalaeayleqnleLR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 761 KEQARYSQ--LQEQRDtmvtQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHT 829
Cdd:COG3206 170 REEARKALefLEEQLP----ELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 830 ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDA 909
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILA 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914075 910 SQRRvlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 967
Cdd:COG3206 317 SLEA--ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
731-826 |
2.61e-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: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 731 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 810
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 568914075 811 MIAELRVELKKANNKV 826
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
739-930 |
5.08e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 739 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRVE 818
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 819 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 895
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568914075 896 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 930
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
732-873 |
5.70e-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: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 732 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrn 810
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914075 811 mIAELRVELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 873
Cdd:pfam07926 73 -IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
710-918 |
6.14e-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: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNRRLLRkviRAAALEEHNAAMKDQLKLQEKDIQMWKvslqkEQARYSQLQEQRDTMVTQ---LHSQIRQ 786
Cdd:COG3206 159 EAYLEQNLELRREEARK---ALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQlseLESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 787 LQHDREEFYNQSQELQTKLEDCRNMIAELR--VELKKANNKVCHTELLLSQVSQKLS-NSESVQQqmefLNRQLlvlGEV 863
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYTpNHPDVIA----LRAQI---AAL 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568914075 864 NELYLEQLQSKHPDTTKEVEMMKtAYRKELEKNRSHLLQQNQRLDASQRRVLELE 918
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQ-AREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
733-958 |
6.38e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 733 ALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYSQLQEQRDTMVT------QLHSQIRQLQHDREEFYNQSQELQTKL 805
Cdd:pfam00038 22 FLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 806 EDCRNMIAELRVELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEM 884
Cdd:pfam00038 99 TSAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 885 --------------MKTAYRKELEKNRSHL----------LQQ-----NQRLDASQRRVLEL----ESLLAKKDHlLLEQ 931
Cdd:pfam00038 161 daarkldltsalaeIRAQYEEIAAKNREEAeewyqskleeLQQaaarnGDALRSAKEEITELrrtiQSLEIELQS-LKKQ 239
|
250 260
....*....|....*....|....*..
gi 568914075 932 KKYLEDvksqasgQLLAAESRYEAQRK 958
Cdd:pfam00038 240 KASLER-------QLAETEERYELQLA 259
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
762-940 |
6.56e-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: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 762 EQARYSQLQEQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRNMIA 813
Cdd:pfam05622 242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 814 ELRVELKKANNKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 891
Cdd:pfam05622 322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568914075 892 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 940
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
711-959 |
8.42e-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: 43.57 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 711 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQ---EQRDtmvtqlhsqiRQL 787
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 788 QHDREEfynqSQELQTKLEDCRNMIAELRvelkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 867
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 868 LEQLQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---G 944
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerS 566
|
250
....*....|....*
gi 568914075 945 QLLAAESRYEAQRKI 959
Cdd:pfam17380 567 RLEAMEREREMMRQI 581
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
715-820 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 715 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQEQRDTMvtQLHSQ-----IRQLQH 789
Cdd:pfam13851 50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 568914075 790 DREEFYNQS----QELQTKLEdCRNMIAELRVELK 820
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
768-937 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 768 QLQEQRDTMVTQLHSQIRQLQHDREE----FYNQSQELQTKLEDCRNMIAELRVELK--------KANNKVCHTELLLSQ 835
Cdd:pfam14988 15 EKQKKIEKLWNQYVQECEEIERRRQElasrYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklKESQEREIQDLEEEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 836 VSQKLSNSESVQQ-QMEFLNRQLLVLGEVNELYLEQL-QSKHPDTTKEVEMMKTAYRK--------------ELEKNRSH 899
Cdd:pfam14988 95 EKVRAETAEKDREaHLQFLKEKALLEKQLQELRILELgERATRELKRKAQALKLAAKQalsefcrsikrenrQLQKELLQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 568914075 900 LLQQNQRLDASQRRvleleslLAKKDHLLLEQKKYLED 937
Cdd:pfam14988 175 LIQETQALEAIKSK-------LENRKQRLKEEQWYLEA 205
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
710-969 |
1.42e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 763
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 764 ARYSQLQEQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 806
Cdd:PRK10246 682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 807 ---DCRNMIAEL-------RVELKKAN--NKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 873
Cdd:PRK10246 762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 874 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKK--DHLL-LEQKKYLEDVKSQASG 944
Cdd:PRK10246 838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKegDKFRkFAQGLTLDNLVWLANQ 912
|
330 340
....*....|....*....|....*
gi 568914075 945 QLLAAESRYEAQRKITRVLELEILD 969
Cdd:PRK10246 913 QLTRLHGRYLLQRKASEALELEVVD 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
714-970 |
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 568914075 714 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLqhdree 793
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------ 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 794 fynqsQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEV---NEL 866
Cdd:TIGR02168 785 -----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDiesLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 867 YLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQL 946
Cdd:TIGR02168 860 EIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------EL 929
|
250 260
....*....|....*....|....
gi 568914075 947 LAAESRYEAQRKITRVLELEILDL 970
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
713-955 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 713 KRQQHALRnRRLLRKVIRAAALEEH-----NAAMKDQLKLQEKDIQMWK----VSLQKEQARYSQLQEQRDTMVTQLHSQ 783
Cdd:pfam10174 481 KEKVSALQ-PELTEKESSLIDLKEHasslaSSGLKKDSKLKSLEIAVEQkkeeCSKLENQLKKAHNAEEAVRTNPEINDR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 784 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLV 859
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 860 LGEVNElylEQLQSKHPDTTKEvEMMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV- 938
Cdd:pfam10174 640 EARRRE---DNLADNSQQLQLE-ELMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIl 707
|
250
....*....|....*....
gi 568914075 939 --KSQAsgqLLAAESRYEA 955
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, ... |
841-952 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 841 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 909
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568914075 910 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 952
Cdd:pfam10473 92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
720-930 |
2.58e-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: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 720 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtQLHSQIRQLQHDREefyNQS 798
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLA---KIR 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 799 QELQTKLEDCRNMI----AELRVELKKANNKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNEL 866
Cdd:pfam12128 404 EARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914075 867 YLEQLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 930
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
713-981 |
2.86e-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: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 713 KRQQHALRNRRLLRKVIRAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRdtmvtqlHSQIRQLQHDRE 792
Cdd:pfam13868 62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 793 EFYNQSQEL------QTKLEDCRNM------------IAELRVELKKANnkvchtELLLSQVSQKLSNSESVQQQMEFLn 854
Cdd:pfam13868 134 EFNEEQAEWkelekeEEREEDERILeylkekaereeeREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDEL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 855 RQLLVLGEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 930
Cdd:pfam13868 207 RAKLYQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568914075 931 QKK-----YLEDVKSQasgqllaAESRyEAQRKITRVLELEILDLYGRLEKDGRLR 981
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 ... |
731-982 |
2.88e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 731 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQArysQLQEQRDTMvtqlhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 809
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESENA---ELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 810 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQSKHPDTTKevemmktay 889
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 890 RKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYLEDVksqaSGQLLAAEsryEAQRKITRVLELEIL 968
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKLEED----AGTLEALE---EGKKRLQRELEALTQ 559
|
250 260
....*....|....*....|.
gi 568914075 969 DL------YGRLEK-DGRLRK 982
Cdd:pfam01576 560 QLeekaaaYDKLEKtKNRLQQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
710-924 |
2.95e-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: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 710 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 787
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 788 Q--------------HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFl 853
Cdd:COG4942 114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568914075 854 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 924
Cdd:COG4942 190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
730-857 |
3.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 730 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQE-----------QRDTMVTQLHSQ----IRQLQHDREEF 794
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568914075 795 YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 857
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-977 |
3.25e-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: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 796 NQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 871
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 872 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLElesllakkDHLLLEQKKYLEDVKSQASgQLLAAE 950
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLA-ELAALR 166
|
170 180
....*....|....*....|....*..
gi 568914075 951 SRYEAQRKITRVLELEILDLYGRLEKD 977
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
713-930 |
3.54e-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: 40.36 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 713 KRQQHALRNRRLlRKVIRAAAleehnaamKDQLKLQEKDIQMWKVSLQKEQARYSQL-QEQRDTMVTQLHSQIRQLQHDR 791
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDAP--------AELRELRQELAALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 792 EEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNELYLEQ 870
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDMLEQEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914075 871 LQSkhpdttkevEMMKTAYRKELEKNRSHLLQQNQRLDA-----SQRRVLELESLLAKKDHLLLE 930
Cdd:pfam12795 173 LSN---------NNRQDLLKARRDLLTLRIQRLEQQLQAlqellNEKRLQEAEQAVAQTEQLAEE 228
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
741-966 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 741 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNM----I 812
Cdd:COG5185 346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 813 AELRVELKKANNKVCHTelllSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEqLQSKHPDTTKEVEMMKT---AY 889
Cdd:COG5185 423 EELQRQIEQATSSNEEV----SKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKEDLNEELTQIESrvsTL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914075 890 RKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 966
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
742-941 |
4.16e-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: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 742 KDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVE 818
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 819 LKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-----------LNRQLLVLGEV--NELYLEQLQSKHpdttKEVEMM 885
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdLEDELNKDDFElkKENLEKEIDEKN----KEIEEL 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568914075 886 KTAYrKELEKNRShllQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 941
Cdd:TIGR04523 574 KQTQ-KSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
773-933 |
5.21e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 773 RDTMVTQLHSQ---IRQLQHDREEFYNQSQELQTK-LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNS----- 843
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDIErLYRMIDILNDAQQQIKWTNQPRIYLEVALVKLCEQAAASpeydt 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 844 --ESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEV------------EMMKTAYRKELEKNRSH---LLQQNQR 906
Cdd:PRK05563 370 elEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKkkkykvprgkiyKVLKEATRQDLELLKNVwgeILESLKA 449
|
170 180
....*....|....*....|....*...
gi 568914075 907 LDASQRRVL-ELESLLAKKDHLLLEQKK 933
Cdd:PRK05563 450 QRKSLRALLvNSEPVAASEDTVVLAFEY 477
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
768-853 |
7.23e-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: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 768 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 842
Cdd:cd16855 9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 568914075 843 sesvQQQMEFL 853
Cdd:cd16855 86 ----QLRMELA 92
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
734-941 |
8.00e-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: 40.39 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 734 LEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQEL-----QTKleDC 808
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneEKK--EL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 809 RNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ-----LQSKHP 876
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQkslkkKQEEKQ 588
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914075 877 DTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 941
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
709-826 |
8.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 709 YERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQ-EKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 787
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdEEEL----RAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568914075 788 QH-----DREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKV 826
Cdd:COG4717 419 EEllealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
742-941 |
8.56e-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: 40.39 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 742 KDQLKLQEKDIQmwkvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKK 821
Cdd:TIGR04523 116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 822 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQSKHPDTTKEVEMMK---TAYRKELEK 895
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKdeqNKIKKQLSE 271
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568914075 896 NRSHLLQQNQRLDASQRRVLELESLLAKkdhllLEQKK---YLEDVKSQ 941
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKeqdWNKELKSE 315
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
711-970 |
8.60e-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: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 711 RFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHD 790
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 791 REE----------FYNQSQELQTKLEDcRNMIAELRVEL--KKANNKVCHTELL------------------LSQVSQKL 840
Cdd:TIGR00606 908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 841 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QSKHPDTTKEVEMMKTAYRKELEKNR-SHLLQQNQRLDASQRRV 914
Cdd:TIGR00606 987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLI 1066
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568914075 915 LELESLLAKKDHLLLEQKKYLEdvKSQASGQLLAAESRYEAQRKITRVLELEILDL 970
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
726-915 |
9.51e-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: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 726 RKVIRAAALEEHNAAMKDQLKLQEKDIqmwkvslqkEQaRYSQLQEQRdTMVTQLHSQIRQLQHDREEFYNQSQELQTKL 805
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAEL---------EQ-RLRQQQNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914075 806 EDCRNMIAE-------LRVELKKANNKVchTEL----------------LLSQVSQKLSNSESVQQQMEFLnrqllvlge 862
Cdd:COG3096 567 EELEEQAAEaveqrseLRQQLEQLRARI--KELaarapawlaaqdalerLREQSGEALADSQEVTAAMQQL--------- 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568914075 863 vnelyLEQLqskhpdttkevemmktayrKELEKNRSHLLQQNQRLDASQRRVL 915
Cdd:COG3096 636 -----LERE-------------------REATVERDELAARKQALESQIERLS 664
|
|
| |
