|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-729 |
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: 988.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 7 IGELLSMLDSSTLGVRDDVTAIFKESLNSERGPMLVNTLVDYYLETNSQPVLHILTTLQEPHDKHLLDKINEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 87 LSILSLLGHVVRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 167 KKPGHVTEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENVETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 247 WKTLETHDVVIECAKISLDPTEASYEDGYSVShqlsacfpyrSADVTTSPYVDTQNSYGGSTSTPSSSSRLMLFSPPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 327 PQSLSSPSTRLLPEPLqvrchsaclhllylpaSLWSPSAVCGMTTPPTSPGNVPA-------DLSHPYSKAFGTTG--GK 397
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF----------------PLWSPSSVCGMTTPPTSPGMVPTtpselspSSSHLSSRGSSPPEaaGE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 398 GTPSG--TPATSPPPAPPCPQDDCVHGS--AAQASATAPRKEERADSSRPYLHRQ----SNDRGLEDPPGSKGSVTLRNL 469
Cdd:pfam04388 375 ATPETtpAKDSPYLKQPPPLSDSHVHRAlpASSQPSSPPRKDGRSQSSFPPLSKQaptnPNSRGLLEPPGDKSSVTLSEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 470 PDFLGDLA-SEEDSIEKDKEEAAISKELSEITTAEADPVVPRGGFDSPFYR--DSLSGSQRK--------THSAASGTQG 538
Cdd:pfam04388 455 PDFIKDLAlSSEDSVEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 539 SSVNPE-----PLHSSLDKHGPDTPKQAFTPIDPPSGSADVSPAGDRDRQTSLETSILTPSPCKIPPQRGVSFGSGQLPP 613
Cdd:pfam04388 535 PATTPEskpsaLAEDGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLP 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 614 YDHLFEVALPKTACHFVSKKTEELLKKVKGNPEEDCVPSTSPMEVLDRLIEQGAGAHSKELSRLSLPSKSVDWTHFGGSP 693
Cdd:pfam04388 615 YEHLFDLALPKTASLFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSA 694
|
730 740 750
....*....|....*....|....*....|....*.
gi 755497764 694 PSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRL 729
Cdd:pfam04388 695 PSDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
714-960 |
3.05e-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: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 714 YERFKRQQHALrNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQ 793
Cdd:TIGR02168 290 LYALANEISRL-EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 794 HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLV--------- 864
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqae 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 865 LGEVNELyLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHlLLEQKKYLEDVK 944
Cdd:TIGR02168 442 LEELEEE-LEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQ 515
|
250 260
....*....|....*....|..
gi 755497764 945 SQASG------QLLAAESRYEA 960
Cdd:TIGR02168 516 SGLSGilgvlsELISVDEGYEA 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
715-986 |
5.67e-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: 63.92 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNrrlLRKVIRAAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQARY-SQLQEQRDTMvTQLHSQIRQLQ 793
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREEL-EELQEELKEAEEELEELTAELQELeEKLEELRLEV-SELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 794 HdreEFYNQSQELQT----------KLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLS----NSESVQQQMEFLN 859
Cdd:TIGR02168 288 K---ELYALANEISRleqqkqilreRLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 860 RQLLVLGEVNELY---LEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKD-HLLLE 935
Cdd:TIGR02168 365 AELEELESRLEELeeqLETLRSKVAQLELQIA----SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQA 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755497764 936 QKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRL-EKDGRLR 986
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLD 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
766-979 |
1.06e-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: 60.32 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 766 KEQARYSQLQEqRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKL 845
Cdd:COG1579 4 EDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 846 SNSESvqqqmeflNRQllvlgevnelyLEQLQskhpdttKEVEMMKTAyRKELEKnrsHLLQQNQRLDASQRRVLELESL 925
Cdd:COG1579 83 GNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEELEEELAELEAE 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755497764 926 LAKKDHLLLEQKKYLEdvksQASGQLLAAESRYEAQR-KITRVLELEILDLYGRL 979
Cdd:COG1579 133 LAELEAELEEKKAELD----EELAELEAELEELEAEReELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
725-972 |
1.49e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 725 RNRRLLRKVIRaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL-QHDR--EEFYN 801
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 802 QSQELQTKLEDCRN-----MIAELRVELKKANNKVCHTELLLSQVSQKLS--------------NSES----VQQQMEFL 858
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISqlneqisqlkkeltNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 859 NRQLLVLGEVNELYLEQLQSkhpdttkeVEMMKTAYRKELEKNRshllQQNQRLDaSQRRVLELESLLAKKDHLLL---- 934
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQE----KLNQQKD-EQIKKLQQEKELLEKEIERLketi 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755497764 935 -EQKKYLEDVKSQASGQLLAAES---RYEAQRKITRVLELEI 972
Cdd:TIGR04523 436 iKNNSEIKDLTNQDSVKELIIKNldnTRESLETQLKVLSRSI 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
718-998 |
3.69e-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: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 718 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDRE 797
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 798 EFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEflnRQLLvlgEVNELYLEQLQ 877
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELE---ELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 878 SKhpdttkevemmkTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESR 957
Cdd:COG1196 394 AA------------AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755497764 958 YEAQRKITRVLELEILDLYGRLEKDGRLRKLEEDRAEAAEA 998
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
715-971 |
7.28e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQH 794
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 795 DREEFYNQSQELQTKLEDCRNMIAELRVELKKannkvchtelLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLE 874
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEE----------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 875 QLQskhpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA 954
Cdd:COG1196 359 ELA----EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250
....*....|....*..
gi 755497764 955 ESRYEAQRKITRVLELE 971
Cdd:COG1196 435 EEEEEEEEALEEAAEEE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
723-987 |
2.12e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 723 ALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQHDREEFYNQ 802
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 803 SQELQTKLEDCRNMIAELRVE---LKKANNKVCHT-ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQlqs 878
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqdLEQQRKQLEAQiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 879 khpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKK------DHLLLEQKKYLEDVKSQASGQLL 952
Cdd:COG4372 180 ---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklglALSALLDALELEEDKEELLEEVI 256
|
250 260 270
....*....|....*....|....*....|....*
gi 755497764 953 AAEsRYEAQRKITRVLELEILDLYGRLEKDGRLRK 987
Cdd:COG4372 257 LKE-IEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
735-971 |
8.48e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 735 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCR 814
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 815 NMIAELRVELKKANNKVCHTELLLS-----QVSQKLSNSESV------QQQMEFLnrqllvlgevnELYLEQLQSKHPDT 883
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVetieedRERVEEL-----------EAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 884 TKEVEMMKTAyrKELEKNRSHLLqqnQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAA-ESRYEAQR 962
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLE---ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAaEAEEEAEE 569
|
....*....
gi 755497764 963 KITRVLELE 971
Cdd:PRK02224 570 AREEVAELN 578
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
739-979 |
1.20e-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: 56.27 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 739 LEEHNAAMKDQLKLQEKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSqirQLQHDREEFYNQSQELQTKL----EDCR 814
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDI----INCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLdkseENAR 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 815 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFL-------NRQLLVLG-EVNELYLEqLQSkhpdTTKE 886
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaeNKQLNAYEiKVNKLELE-LAS----AKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 887 VEMMKTAYRKELEKNR---SHLLQQNQRLDASQRRVLELESLLAKK-DHLLLEQKKYLEDVKSQ-------ASGQLLAAE 955
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQydkiieeRDSELGLYK 731
|
250 260
....*....|....*....|....
gi 755497764 956 SRYEAQRKITRVLELEILDLYGRL 979
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
762-981 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 762 VSLQKEQARYSQLQEQRDtmvtQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQV 841
Cdd:COG4942 13 LAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 842 SQKLSNSE-SVQQQMEFLNRQLLVL---GEVNELYLEQLQSKHPDTTKEVEMMK--TAYRKE----LEKNRSHLLQQNQR 911
Cdd:COG4942 89 EKEIAELRaELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREqaeeLRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 912 LDASQRrvlELESLLAKkdhlLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 981
Cdd:COG4942 169 LEAERA---ELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
725-982 |
1.35e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 725 RNRRLLRKVIRAAALEEHNAAMkdqLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLH---SQIRQLQHDREEFYN 801
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEqleEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 802 QSQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQSKHP 881
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEE-------AEELQEEL---EELQKERQDLEQQ-----------RKQLEAQIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 882 DTTKEVEmMKTAYRKELEKNRSHLLQQNQRLDASQRRvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQ 961
Cdd:COG4372 140 ELQSEIA-EREEELKELEEQLESLQEELAALEQELQA-LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
250 260
....*....|....*....|.
gi 755497764 962 RKITRVLELEILDLYGRLEKD 982
Cdd:COG4372 218 EELLEAKDSLEAKLGLALSAL 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
754-963 |
1.56e-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: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 754 EKDIQMWKVSLQKEQARYSQLQEQRDTM---VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNK 830
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 831 VCHTELLLSQVSQkLSNSESVQqqmEFLNRQllvlgevneLYLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQ 910
Cdd:COG3883 95 LYRSGGSVSYLDV-LLGSESFS---DFLDRL---------SALSKIADADADLLEELK----ADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755497764 911 RLDASQRrvlELESLLAKKDHLLLEQKKYLEDVKSQASgQLLAAESRYEAQRK 963
Cdd:COG3883 158 ELEALKA---ELEAAKAELEAQQAEQEALLAQLSAEEA-AAEAQLAELEAELA 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
749-997 |
1.94e-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: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 749 QLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmvtqlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKAN 828
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAE-----------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 829 NKVchtELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQ 908
Cdd:COG1196 288 AEE---YELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 909 NQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKDGRLRKL 988
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
....*....
gi 755497764 989 EEDRAEAAE 997
Cdd:COG1196 444 LEEAAEEEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
695-914 |
2.46e-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: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 695 SDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIRAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 770
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 771 YSQLQEQRDTMVTQlhsqIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVEL----KKANNKVCHT-ELLLSQVSQKL 845
Cdd:TIGR02168 889 LALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTlEEAEALENKIE 964
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755497764 846 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKhpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDA 914
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEEL-----KERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
752-981 |
4.02e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 752 LQEKDIQMWKVSLQKEQA-RYSQLQEQRDTM--------VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRV 822
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAeRYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 823 ELKKANNKVCHTELLLSQVSQKLSNSES----VQQQMEFLNRQLLVLGEvnelYLEQLQSKHPDTTKEVEMMKTAYrKEL 898
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQqkqiLRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL-EEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 899 EKNrshLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ---ASGQLLAAESRYEA-QRKITRVLElEILD 974
Cdd:TIGR02168 350 KEE---LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERlEDRRERLQQ-EIEE 425
|
....*..
gi 755497764 975 LYGRLEK 981
Cdd:TIGR02168 426 LLKKLEE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
735-986 |
6.56e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 735 RAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE---EFYNQSQELQTKLE 811
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 812 DCRNMIAELRVELKKANNKV--CHTELL--------LSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHp 881
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVaeLNSKLAelkeriesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR- 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 882 DTTKEVEmmktayrKELEKNRSHLLQQN-QRLDASQRRVLE-LESLLAKKDHLL---------LEQKKYLEDVKSQASGQ 950
Cdd:PRK02224 634 ERKRELE-------AEFDEARIEEAREDkERAEEYLEQVEEkLDELREERDDLQaeigaveneLEELEELRERREALENR 706
|
250 260 270
....*....|....*....|....*....|....*.
gi 755497764 951 LLAAESRYEaqrkitRVLELEilDLYGRLEKDGRLR 986
Cdd:PRK02224 707 VEALEALYD------EAEELE--SMYGDLRAELRQR 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-981 |
1.24e-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: 53.15 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 690 GGS--PPSDELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKdQLKLQEKDIQMwkvsLQKE 767
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-KIGEIEKEIEQ----LEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 768 QARYSQLQEQrdtmvtqLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL-----LLSQVS 842
Cdd:TIGR02169 732 EEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeiqaELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 843 QKLSNSESVQQQME-FLNRQLLVLG----EVNEL--YLEQLQSKHPDTTKEVEMMKTAYRK-------------ELEKNR 902
Cdd:TIGR02169 805 EEVSRIEARLREIEqKLNRLTLEKEylekEIQELqeQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaalrDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 903 SHLLQQNQRLDAS----QRRVLELESLLAKKDHLLLEQKKYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEILDLY 976
Cdd:TIGR02169 885 GDLKKERDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
....*
gi 755497764 977 GRLEK 981
Cdd:TIGR02169 965 EEIRA 969
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
718-972 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 718 KRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQeqrdtmvtqlhsQIRQLQHDRE 797
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT------------QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 798 EFYNQSQELQTKLEDCRNMIAELRvELKKANNKVCHTELL------LSQVSQKLSNS-----------ESVQQQMEFLNR 860
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPLaahikaVTQIEQQAQRIhtelqskmrsrAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 861 QLLVLGEVNELyLEQLQSKHPDTTKEVEmMKTAYRKELEKN---RSHLLQQNQRLDASQRRvleLESLLAKKDHLLLEQK 937
Cdd:TIGR00618 336 QQSSIEEQRRL-LQTLHSQEIHIRDAHE-VATSIREISCQQhtlTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 755497764 938 KYLEDVKSQAS--GQLLAAESRYEAQRKITRVLELEI 972
Cdd:TIGR00618 411 TIDTRTSAFRDlqGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
729-969 |
1.93e-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: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 729 LLRKVIRAAALEEH-NAAMKDQLKL-QEKDIQMWKvsLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQ---- 802
Cdd:pfam05483 305 LQRSMSTQKALEEDlQIATKTICQLtEEKEAQMEE--LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkii 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 803 SQELQTK---LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQklsnSESVQQQMEFLNRQLLVLGEVNELYLEQLQSK 879
Cdd:pfam05483 383 TMELQKKsseLEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 880 HPDTT-------KEVEMMKTayrkELEKNRshlLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDV---KSQASG 949
Cdd:pfam05483 459 LTAIKtseehylKEVEDLKT----ELEKEK---LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEER 531
|
250 260
....*....|....*....|
gi 755497764 950 QLLAAESRYEAQRKITRVLE 969
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELE 551
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
715-982 |
2.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRrLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQ 791
Cdd:COG4372 41 DKLQEELEQLREE-LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 792 LQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSN------SESVQQQMEFLNRQLLVL 865
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 866 GEVNELYLEQLQSKHPdTTKEVEMMKTAYRKELEKNRSHLLQQNQRL-DASQRRVLELESLLAKKDHLLLEQKKYLEDVK 944
Cdd:COG4372 200 EELAEAEKLIESLPRE-LAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270
....*....|....*....|....*....|....*...
gi 755497764 945 SQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEKD 982
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
726-972 |
3.11e-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: 50.69 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 726 NRRLLR-KV--IRAAALEEHNAaMKDQLKLQEKDI-QMWKV----SLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDRE 797
Cdd:pfam13868 12 NSKLLAaKCnkERDAQIAEKKR-IKAEEKEEERRLdEMMEEererALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 798 EFYNQS-QELQTKLEDCRNMIAE-LRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLvlgevneLYLEQ 875
Cdd:pfam13868 91 EEYEEKlQEREQMDEIVERIQEEdQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-------EYLKE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 876 LQSKhpDTTKEVEMMKTAYRKELEKNRshLLQQNQRLDASQRrvlELESLLAKkdhLLLEQ------KKYLEDVKSQASG 949
Cdd:pfam13868 164 KAER--EEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKA---ERDELRAK---LYQEEqerkerQKEREEAEKKARQ 233
|
250 260
....*....|....*....|...
gi 755497764 950 QLLAAESRYEAQRKITRVLELEI 972
Cdd:pfam13868 234 RQELQQAREEQIELKERRLAEEA 256
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
726-877 |
3.59e-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: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 726 NRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYSQLQEQRDTMVTQL---HSQIRQLQHDREEFY 800
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755497764 801 NQ-SQELQTKLEDCRNMIAELRVELKKANNKvchtellLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 877
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQ-------LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
758-973 |
6.14e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 758 QMWKVSLQKEQARYSQLQEQRDTM-VTQLHSQIRQLQHDREEfYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL 836
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 837 LLSQVSQklsnsesvQQQMEFLNRQLLVLGEVnelyLEQLQSKHpDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQ 916
Cdd:COG4717 124 LLQLLPL--------YQELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755497764 917 RRVL-----ELESLLAKKDHLLLEQKKyLEDVKSQASGQLLAAESRYEAQRKITRVLELEIL 973
Cdd:COG4717 191 EEELqdlaeELEELQQRLAELEEELEE-AQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
782-981 |
7.64e-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: 50.44 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 782 VTQLHSQIRQLQHDREEFYNQSQELQTKLEDCR-------NMIAELRVELKKANNKVchtELLLSQVSQKLSNSESVQQQ 854
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRkeleelsRQISALRKDLARLEAEV---EQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 855 MEFLNRQL------LVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRV--------- 919
Cdd:TIGR02168 763 IEELEERLeeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaaterrled 842
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755497764 920 ---------LELESLLAKKDHL------LLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELEILDLYGRLEK 981
Cdd:TIGR02168 843 leeqieelsEDIESLAAEIEELeelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-975 |
8.90e-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: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 696 DELRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDiqmwkvsLQKEQArysQLQ 775
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-------AEAEIE---ELE 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 776 EQRDTMVTQLHSQIRQLQHDREEFYNQS---QELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQ 852
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNeeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI---EELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 853 QQMEFLNRQL---LVLGEVNELYLEQLQSKHPDTTKEVEMM---KTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLL 926
Cdd:TIGR02168 866 ELIEELESELealLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755497764 927 AKKDHLLLE--QKKYLEDVKSQAsgqllaaesryEAQRKITRvLELEILDL 975
Cdd:TIGR02168 946 SEEYSLTLEeaEALENKIEDDEE-----------EARRRLKR-LENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-987 |
1.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 728 RLLRKVIRaaaLEEHNAAMKDQLKLQeKDIQMWKVSLQKEQARYSQLQEQRDTM----------VTQLHSQIRQLqhdRE 797
Cdd:PRK03918 149 KVVRQILG---LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPEL---RE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 798 EFYNQSQELQtKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELY--LEQ 875
Cdd:PRK03918 222 ELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYikLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 876 LQSKHPDTTKEVEMMKTAYR---KELEKNRSHLLQQNQRLDASQRRVLELESLLA--KKDHLLLEQ----KKYLEDVKSQ 946
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEakakKEELERLKKR 380
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755497764 947 ASGQLLA-AESRYEAQRKITRVLELEILDLYGRLekdGRLRK 987
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEIEEEISKITARI---GELKK 419
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
740-944 |
1.87e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 740 EEHNAAMKDQLKLQEKDIQMWKvsLQKEQARYSQLQ------EQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDC 813
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 814 RNMIAELRVELKK-ANNKVCHTELLLSQVS-------QKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTK 885
Cdd:TIGR00618 738 EDALNQSLKELMHqARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDED 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755497764 886 EVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVK 944
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
749-986 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 749 QLKLQEKDIQMWKVSLQKE-QARYSQLQEQRDTMVTQlHSQIRQLQHDREEFynqSQELQTKLEDCRNMIAElrvelkka 827
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAElKQKENKLQENRKIIEAQ-RKAIQELQFENEKV---SLKLEEEIQENKDLIKE-------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 828 NNKVCHTELLLSQVSQKlsnSESVQQQMEFlNRQllvlgEVNELYLeqlqskhpDTTKEVEMMKTAYrKELEknrshLLQ 907
Cdd:pfam05483 150 NNATRHLCNLLKETCAR---SAEKTKKYEY-ERE-----ETRQVYM--------DLNNNIEKMILAF-EELR-----VQA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755497764 908 QNQRLDASqrrvLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLElEILDLYGRLEKDGRLR 986
Cdd:pfam05483 207 ENARLEMH----FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE-ESRDKANQLEEKTKLQ 280
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-906 |
3.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 691 GSPPSDELRTLRDQL----LLLHNQLLYERFKRQQHALRNRRllrkviraAALEEHNAAMKDQLKLQEKDIQMWKVSLQK 766
Cdd:COG4717 63 GRKPELNLKELKELEeelkEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 767 EQARySQLQEqrdtmvtqLHSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRVELKKANNKVchTELLLSQVSQKLS 846
Cdd:COG4717 135 EALE-AELAE--------LPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 847 NSESVQQQMEFLNRQLlvlgEVNELYLEQLQSKHPDTtkEVEMMKTAYRKELEKNRSHLL 906
Cdd:COG4717 200 ELEELQQRLAELEEEL----EEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLL 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
715-969 |
4.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNR-RLLRKVIRAAALEEHNAAMK----------DQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT 783
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 784 QL----HSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTEL----------------LLSQVSQ 843
Cdd:COG4717 185 QLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlkearlllliaaaLLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 844 KLSNSESVQQQMEFLnrqLLVLGEVNELYLEQLQSKHPDTTKEVEMMKTAYRKELEK----------------NRSHLLQ 907
Cdd:COG4717 265 GGSLLSLILTIAGVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellaalglppdlSPEELLE 341
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755497764 908 QNQRLDASQRRVLELESLL--AKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLE 969
Cdd:COG4717 342 LLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
714-967 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 714 YERF-KRQQHALRNRRLL-----RKViraAALEEhnaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDT------- 780
Cdd:COG4913 587 GTRHeKDDRRRIRSRYVLgfdnrAKL---AALEA-------ELAELEEELAEAEERLEALEAELDALQERREAlqrlaey 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 781 -----MVTQLHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQ 852
Cdd:COG4913 657 swdeiDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 853 QQMEFLNRQLLVLgEVNELYLEQLQSKHPDTtkevemMKTAYRKELEKNRSHLLQQNQRL------------------DA 914
Cdd:COG4913 737 EAAEDLARLELRA-LLEERFAAALGDAVERE------LRENLEERIDALRARLNRAEEELeramrafnrewpaetadlDA 809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 915 SQRRVLELESLLAK-KDHLLLEQKKYLEDVKSQASGQLLA------AESRYEAQRKITRV 967
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVAdllsklRRAIREIKERIDPL 869
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
724-972 |
2.06e-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: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 724 LRNRRLLRKVIRAAALEEHN-----------AAMKDQLKLQ-EKDIQMWKVS--------------------------LQ 765
Cdd:COG3206 90 LKSRPVLERVVDKLNLDEDPlgeeasreaaiERLRKNLTVEpVKGSNVIEISytspdpelaaavanalaeayleqnleLR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 766 KEQARYSQ--LQEQRDtmvtQLHSQIRQLQHDREEF---------YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHT 834
Cdd:COG3206 170 REEARKALefLEEQLP----ELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 835 ELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELyLEQLQSKHPDttkevemMKTAyRKELEKNRSHLLQQNQRLDA 914
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL-SARYTPNHPD-------VIAL-RAQIAALRAQLQQEAQRILA 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755497764 915 SQRRvlELESLLAKKDHLLLEQKKYLEDVKS--QASGQLLAAESRYEAQRKI-----TRVLELEI 972
Cdd:COG3206 317 SLEA--ELEALQAREASLQAQLAQLEARLAElpELEAELRRLEREVEVARELyesllQRLEEARL 379
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
736-831 |
2.57e-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: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 736 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSqlQEQRDTMVTQLHSQIRQLQHDREEFynqSQELQTKLedcRN 815
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|....*.
gi 755497764 816 MIAELRVELKKANNKV 831
Cdd:smart00935 92 ELQKILDKINKAIKEV 107
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
737-878 |
4.46e-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: 41.47 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 737 AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVtQLHSQ-IRQLQHDREEFynqsQELQTKledcrn 815
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYEREL-VLHAEdIKALQALREEL----NELKAE------ 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755497764 816 mIAELRVELKKANnkvchTELLLSQVS---QKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQS 878
Cdd:pfam07926 73 -IAELKAEAESAK-----AELEESEESweeQK----KELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
744-935 |
4.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 744 AAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQrdtmVTQLHSQIRQLQhdreefynQSQELQTKLedcrnmiaeLRVE 823
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLE--------QQQAAQERL---------LAAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 824 LKKANNKVCHT--ELLLS-QVSQKlsnSESVQQQMEFLNrqllvlgEVNELYLEQLQSkhpdTTKEVemmkTAYRKELEK 900
Cdd:PRK11637 130 LDAAFRQGEHTglQLILSgEESQR---GERILAYFGYLN-------QARQETIAELKQ----TREEL----AAQKAELEE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755497764 901 NRSH---LL----QQNQRLD----ASQRRVLELESLLAKKDHLLLE 935
Cdd:PRK11637 192 KQSQqktLLyeqqAQQQKLEqarnERKKTLTGLESSLQKDQQQLSE 237
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
767-945 |
5.14e-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: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 767 EQARYSQLQEQR---------------DTMVTQLHS-----QIRQLQHD-------REEFYNQSQ-ELQTKLEDCRNMIA 818
Cdd:pfam05622 242 EELRCAQLQQAElsqadallspssdpgDNLAAEIMPaeireKLIRLQHEnkmlrlgQEGSYRERLtELQQLLEDANRRKN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 819 ELRVELKKANNKVchTELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNE--LYLEQLQSKHPDTTKEVEmmktayrK 896
Cdd:pfam05622 322 ELETQNRLANQRI--LEL---------------QQQVEELQKALQEQGSKAEdsSLLKQKLEEHLEKLHEAQ-------S 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755497764 897 ELEKNRSHLLQQNQRLDAS-QRRVLELESLLAKKDH--LLLEQ--KKYLEDVKS 945
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNlAQKIDELQEALRKKDEdmKAMEEryKKYVEKAKS 431
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
738-963 |
5.43e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 738 ALEEHNAAMkdQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVT------QLHSQIRQLQHDREEFYNQSQELQTKLE 811
Cdd:pfam00038 22 FLEQQNKLL--ETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDFRQKYEDELNLRT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 812 DCRNMIAELRVELKKAN-NKVchtELllsqvsqklsnsesvQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEVEM- 889
Cdd:pfam00038 100 SAENDLVGLRKDLDEATlARV---DL---------------EAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 890 -------------MKTAYRKELEKNRSHL----------LQQ-----NQRLDASQRRVLEL----ESLLAKKDHlLLEQK 937
Cdd:pfam00038 162 aarkldltsalaeIRAQYEEIAAKNREEAeewyqskleeLQQaaarnGDALRSAKEEITELrrtiQSLEIELQS-LKKQK 240
|
250 260
....*....|....*....|....*.
gi 755497764 938 KYLEDvksqasgQLLAAESRYEAQRK 963
Cdd:pfam00038 241 ASLER-------QLAETEERYELQLA 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
715-923 |
5.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRRLLRkviRAAALEEHNAAMKDQLKLQEKDIQMWKvslqkEQARYSQLQEQRDTMVTQ---LHSQIRQ 791
Cdd:COG3206 159 EAYLEQNLELRREEARK---ALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQlseLESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 792 LQHDREEFYNQSQELQTKLEDCRNMIAELR--VELKKANNKVCHTELLLSQVSQKLS-NSESVQQqmefLNRQLlvlGEV 868
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARYTpNHPDVIA----LRAQI---AAL 303
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755497764 869 NELYLEQLQSKHPDTTKEVEMMKtAYRKELEKNRSHLLQQNQRLDASQRRVLELE 923
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQ-AREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
716-964 |
7.57e-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: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 716 RFKRQQHALRNRRLLRKVIRAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYSQLQ---EQRDtmvtqlhsqiRQL 792
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 793 QHDREEfynqSQELQTKLEDCRNMIAELRvelkkannkvchtelllsQVSQKLSNSESVQQQMEFLNRQLLvlgevnELY 872
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEEERK------------------RKKLELEKEKRDRKRAEEQRRKIL------EKE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 873 LEQLQSKHPDTTKEVEMMKtayrKELEKNRSHLLQQNQRLDASQRRVLELEsllakkdhllLEQKKYLEDVKSQAS---G 949
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKATeerS 566
|
250
....*....|....*
gi 755497764 950 QLLAAESRYEAQRKI 964
Cdd:pfam17380 567 RLEAMEREREMMRQI 581
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
720-825 |
8.67e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 720 QQHALRNRRLLRKViraAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYSQLQEQRDTMvtQLHSQ-----IRQLQH 794
Cdd:pfam13851 50 SEIQQENKRLTEPL---QKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 755497764 795 DREEFYNQS----QELQTKLEdCRNMIAELRVELK 825
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
773-942 |
1.08e-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: 41.68 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 773 QLQEQRDTMVTQLHSQIRQLQHDREE----FYNQSQELQTKLEDCRNMIAELRVELK--------KANNKVCHTELLLSQ 840
Cdd:pfam14988 15 EKQKKIEKLWNQYVQECEEIERRRQElasrYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklKESQEREIQDLEEEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 841 VSQKLSNSESVQQ-QMEFLNRQLLVLGEVNELYLEQL-QSKHPDTTKEVEMMKTAYRK--------------ELEKNRSH 904
Cdd:pfam14988 95 EKVRAETAEKDREaHLQFLKEKALLEKQLQELRILELgERATRELKRKAQALKLAAKQalsefcrsikrenrQLQKELLQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 755497764 905 LLQQNQRLDASQRRvleleslLAKKDHLLLEQKKYLED 942
Cdd:pfam14988 175 LIQETQALEAIKSK-------LENRKQRLKEEQWYLEA 205
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
715-974 |
1.29e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRRLLRKVIRA---------AALEEHNAAMKDQLKL-----------------QEKDIQMWkvslQKEQ 768
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAhnqqiiqyqQQIEQRQQQLLTALAGyaltlpqedeeaswlatRQQEAQSW----QQRQ 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 769 ARYSQLQEQ-------------RDTMVTQ------------------LHSQIRQLQHDREEFYNQSQELQTKLE------ 811
Cdd:PRK10246 682 NELTALQNRiqqltplletlpqSDDLPHSeetvaldnwrqvheqclsLHSQLQTLQQQDVLEAQRLQKAQAQFDtalqas 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 812 ---DCRNMIAEL-------RVELKKAN--NKVCHTELLLSQVSQKLSnsESVQQQMEFLNRQLLVlgEVNELYLEQL-QS 878
Cdd:PRK10246 762 vfdDQQAFLAALldeetltQLEQLKQNleNQRQQAQTLVTQTAQALA--QHQQHRPDGLDLTVTV--EQIQQELAQLaQQ 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 879 KHPDTTKEVEMmktayRKEL---EKNRSHLLQQNQRLDASQRRVLE---LESLLAKK--DHLL-LEQKKYLEDVKSQASG 949
Cdd:PRK10246 838 LRENTTRQGEI-----RQQLkqdADNRQQQQALMQQIAQATQQVEDwgyLNSLIGSKegDKFRkFAQGLTLDNLVWLANQ 912
|
330 340
....*....|....*....|....*
gi 755497764 950 QLLAAESRYEAQRKITRVLELEILD 974
Cdd:PRK10246 913 QLTRLHGRYLLQRKASEALELEVVD 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
719-975 |
1.40e-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: 43.12 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 719 RQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLqhdree 798
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI------ 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 799 fynqsQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLLVLGEV---NEL 871
Cdd:TIGR02168 785 -----EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaATERRLEDLEEQIEELSEDiesLAA 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 872 YLEQLQSKHPDTTKEVEmmktAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVksqasgQL 951
Cdd:TIGR02168 860 EIEELEELIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------EL 929
|
250 260
....*....|....*....|....
gi 755497764 952 LAAESRYEAQRKITRVLELEILDL 975
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
718-960 |
1.46e-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: 42.89 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 718 KRQQHALRnRRLLRKVIRAAALEEH-----NAAMKDQLKLQEKDIQMWK----VSLQKEQARYSQLQEQRDTMVTQLHSQ 788
Cdd:pfam10174 481 KEKVSALQ-PELTEKESSLIDLKEHasslaSSGLKKDSKLKSLEIAVEQkkeeCSKLENQLKKAHNAEEAVRTNPEINDR 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 789 IRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTE-LLLSQV---SQKLSNSESVQQQMEFLNRQLLV 864
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsLTLRQMkeqNKKVANIKHGQQEMKKKGAQLLE 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 865 LGEVNElylEQLQSKHPDTTKEvEMMKtayrkELEKNRSHLLQQNQRLDASQRRVLELESLLAKkdhLLLEQKKYLEDV- 943
Cdd:pfam10174 640 EARRRE---DNLADNSQQLQLE-ELMG-----ALEKTRQELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIl 707
|
250
....*....|....*....
gi 755497764 944 --KSQAsgqLLAAESRYEA 960
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, ... |
846-957 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 846 SNSESVQQQMEFLNRQLLVLGEVNE-LYLEQLQSKhpdttKEVEMMK------TAYRKELEKNRSHLLQQ----NQRLDA 914
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQElAILEAENSK-----AEVETLKaeieemAQNLRDLELDLVTLRSEkenlTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 755497764 915 SQRRVLELESLLAKKDHLL--LEQKKYLEDVKSQASGQLLAAESR 957
Cdd:pfam10473 92 KQERVSELESLNSSLENLLeeKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
718-986 |
1.81e-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: 41.83 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 718 KRQQHALRNRRLLRKVIRAAaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRdtmvtqlHSQIRQLQHDRE 797
Cdd:pfam13868 62 EKEEERKEERKRYRQELEEQ-IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK-------LEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 798 EFYNQSQEL------QTKLEDCRNM------------IAELRVELKKANnkvchtELLLSQVSQKLSNSESVQQQMEFLn 859
Cdd:pfam13868 134 EFNEEQAEWkelekeEEREEDERILeylkekaereeeREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDEL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 860 RQLLVLGEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 935
Cdd:pfam13868 207 RAKLYQEEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755497764 936 QKK-----YLEDVKSQasgqllaAESRyEAQRKITRVLELEILDLYGRLEKDGRLR 986
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 ... |
736-987 |
2.24e-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: 42.47 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 736 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQArysQLQEQRDTMvtqlhSQIRQ-LQHDREEFYNQSQELQTKLEDCR 814
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESENA---ELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 815 NMIAELRVELKKANNKVCHTELLLSQVSQKLSNSesvQQQMEFLNRQllvLGEVNELYLEQLQSKHPDTTKevemmktay 894
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDVSSLESQ---LQDTQELLQEETRQKLNLSTR--------- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 895 RKELEKNRSHLLQQNQRLDASQRRV-LELESLLAKkdhlLLEQKKYLEDVksqaSGQLLAAEsryEAQRKITRVLELEIL 973
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQ----LSDMKKKLEED----AGTLEALE---EGKKRLQRELEALTQ 559
|
250 260
....*....|....*....|.
gi 755497764 974 DL------YGRLEK-DGRLRK 987
Cdd:pfam01576 560 QLeekaaaYDKLEKtKNRLQQ 580
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
725-935 |
2.36e-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: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 725 RNRRLLRKVIRAAALEEHNA-AMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTmvtQLHSQIRQLQHDREefyNQS 803
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLpSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE---QNNRDIAGIKDKLA---KIR 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 804 QELQTKLEDCRNMI----AELRVELKKANNKVCHTELLLS--------QVSQKLSNSESVQQQmeflnrqllvlgEVNEL 871
Cdd:pfam12128 404 EARDRQLAVAEDDLqaleSELREQLEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQL------------ENFDE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755497764 872 YLEQLQSKHPDTTKEVEMMK---TAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLE 935
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQselRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
715-929 |
2.60e-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: 41.67 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRRLLRKVIRA--AALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 792
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 793 Q--------------HDREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchTELLLSQVSQKLSNSESVQQQMEFl 858
Cdd:COG4942 114 YrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAA- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755497764 859 nrqllvlgevnelyLEQLQSKHPDTTKEVEMMKTAYRKELEKnrshLLQQNQRLDASQRRVLELESLLAKK 929
Cdd:COG4942 190 --------------LEALKAERQKLLARLEKELAELAAELAE----LQQEAEELEALIARLEAEAAAAAER 242
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
718-935 |
2.87e-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: 40.75 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 718 KRQQHALRNRRLlRKVIRAAAleehnaamKDQLKLQEKDIQMWKVSLQKEQARYSQL-QEQRDTMVTQLHSQIRQLQHDR 796
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDAP--------AELRELRQELAALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 797 EEFYNQSQELQTKLEDCRNMIAELRVELKKANNKvchteLLLSQVSQK-LSNSESVQQQMEflnRQLLVLgEVNELYLEQ 875
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNR-----LNGPAPPGEpLSEAQRWALQAE---LAALKA-QIDMLEQEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755497764 876 LQSkhpdttkevEMMKTAYRKELEKNRSHLLQQNQRLDA-----SQRRVLELESLLAKKDHLLLE 935
Cdd:pfam12795 173 LSN---------NNRQDLLKARRDLLTLRIQRLEQQLQAlqellNEKRLQEAEQAVAQTEQLAEE 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
735-862 |
3.03e-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: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 735 RAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQE-----------QRDTMVTQLHSQ----IRQLQHDREEF 799
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADAdadlLEELKADKAEL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755497764 800 YNQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLsnsESVQQQMEFLNRQL 862
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAEL 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
801-982 |
3.04e-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: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 801 NQSQELQTKLEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 876
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 877 QSKHPDTTKEV-EMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLElesllakkDHLLLEQKKYLEDVKSQASgQLLAAE 955
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLA-ELAALR 166
|
170 180
....*....|....*....|....*..
gi 755497764 956 SRYEAQRKITRVLELEILDLYGRLEKD 982
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEAL 193
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
746-971 |
3.09e-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: 41.48 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 746 MKDQLKLQEkdiQMWKVSLQKEQ----ARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNM----I 817
Cdd:COG5185 346 EQGQESLTE---NLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 818 AELRVELKKANNKVCHTelllSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEqLQSKHPDTTKEVEMMKT---AY 894
Cdd:COG5185 423 EELQRQIEQATSSNEEV----SKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKEDLNEELTQIESrvsTL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755497764 895 RKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQASGQLLAAESRYEAQRKITRVLELE 971
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELT 574
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
747-946 |
3.65e-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: 41.54 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 747 KDQLKLQEKDIQMWKVSLQKEQARYSQLQEQ---RDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVE 823
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 824 LKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-----------LNRQLLVLGEV--NELYLEQLQSKHpdttKEVEMM 890
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdLEDELNKDDFElkKENLEKEIDEKN----KEIEEL 573
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755497764 891 KTAYrKELEKNRShllQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 946
Cdd:TIGR04523 574 KQTQ-KSLKKKQE---EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| PRK05563 |
PRK05563 |
DNA polymerase III subunits gamma and tau; Validated |
778-938 |
5.24e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235505 [Multi-domain] Cd Length: 559 Bit Score: 41.01 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 778 RDTMVTQLHSQ---IRQLQHDREEFYNQSQELQTK-LEDCRNMIAELRVELKKANNKVCHTELLLSQVSQKLSNS----- 848
Cdd:PRK05563 290 RDLLLVKTSPEleiLDESTENDELFKELSEKLDIErLYRMIDILNDAQQQIKWTNQPRIYLEVALVKLCEQAAASpeydt 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 849 --ESVQQQMEFLNRQLLVLGEVNELYLEQLQSKHPDTTKEV------------EMMKTAYRKELEKNRSH---LLQQNQR 911
Cdd:PRK05563 370 elEVLLQRVEQLEQELKQLKAQPVGVAPEQKEKKKEKKKNKkkkykvprgkiyKVLKEATRQDLELLKNVwgeILESLKA 449
|
170 180
....*....|....*....|....*...
gi 755497764 912 LDASQRRVL-ELESLLAKKDHLLLEQKK 938
Cdd:PRK05563 450 QRKSLRALLvNSEPVAASEDTVVLAFEY 477
|
|
| STAT5_CCD |
cd16855 |
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ... |
773-858 |
6.15e-03 |
|
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.
Pssm-ID: 341080 [Multi-domain] Cd Length: 194 Bit Score: 39.17 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 773 QLQEQRdtMVTQ-LHSQIRQLQHDREEF---YNQSQELQTKLEDCRNMIAELRVELK-KANNKVCHTELLLSQVSQKLSn 847
Cdd:cd16855 9 QLEELR--QRTQeTENDLRNLQQKQESFviqYQESQKIQAQLQQLQQQPQNERIELEqQLQQQKEQLEQLLNAKAQELL- 85
|
90
....*....|.
gi 755497764 848 sesvQQQMEFL 858
Cdd:cd16855 86 ----QLRMELA 92
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
714-831 |
7.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 714 YERFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQ-EKDIqmwkVSLQKEQARYSQLQEQRDTMVTQLHSQIRQL 792
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEdEEEL----RAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755497764 793 QH-----DREEFYNQSQELQTKLEDCRNMIAELRVELKKANNKV 831
Cdd:COG4717 419 EEllealDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
739-946 |
7.26e-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: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 739 LEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQEL-----QTKleDC 813
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneEKK--EL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 814 RNMIAELRVELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ-----LQSKHP 881
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQkslkkKQEEKQ 588
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755497764 882 DTTKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKKYLEDVKSQ 946
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
747-946 |
7.45e-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: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 747 KDQLKLQEKDIQmwkvSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRVELKK 826
Cdd:TIGR04523 116 KEQKNKLEVELN----KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 827 ANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGE-VNELY--LEQLQSKHPDTTKEVEMMK---TAYRKELEK 900
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDnIEKKQqeINEKTTEISNTQTQLNQLKdeqNKIKKQLSE 271
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755497764 901 NRSHLLQQNQRLDASQRRVLELESLLAKkdhllLEQKK---YLEDVKSQ 946
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKeqdWNKELKSE 315
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
716-975 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 716 RFKRQQHALRNRRLLRKVIRAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYSQLQEQRDTMVTQLHSQIRQLQHD 795
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 796 REE----------FYNQSQELQTKLEDcRNMIAELRVEL--KKANNKVCHTELL------------------LSQVSQKL 845
Cdd:TIGR00606 908 KEQdspletflekDQQEKEELISSKET-SNKKAQDKVNDikEKVKNIHGYMKDIenkiqdgkddylkqketeLNTVNAQL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 846 SNSESVQQQME---FLNRQLLVLGEVNELYL-EQL-QSKHPDTTKEVEMMKTAYRKELEKNR-SHLLQQNQRLDASQRRV 919
Cdd:TIGR00606 987 EECEKHQEKINedmRLMRQDIDTQKIQERWLqDNLtLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLI 1066
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755497764 920 LELESLLAKKDHLLLEQKKYLEdvKSQASGQLLAAESRYEAQRKITRVLELEILDL 975
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
731-920 |
7.94e-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: 40.71 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 731 RKVIRAAALEEHNAAMKDQLKLQEKDIqmwkvslqkEQaRYSQLQEQRdTMVTQLHSQIRQLQHDREEFYNQSQELQTKL 810
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAEL---------EQ-RLRQQQNAE-RLLEEFCQRIGQQLDAAEELEELLAELEAQL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 811 EDCRNMIAE-------LRVELKKANNKVchTEL----------------LLSQVSQKLSNSESVQQQMEFLnrqllvlge 867
Cdd:COG3096 567 EELEEQAAEaveqrseLRQQLEQLRARI--KELaarapawlaaqdalerLREQSGEALADSQEVTAAMQQL--------- 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755497764 868 vnelyLEQLqskhpdttkevemmktayrKELEKNRSHLLQQNQRLDASQRRVL 920
Cdd:COG3096 636 -----LERE-------------------REATVERDELAARKQALESQIERLS 664
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
715-988 |
9.49e-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: 39.52 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 715 ERFKRQQHALRNRRLLRKVIRAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYSQLQEQRdtmvtqlhsqiRQLQH 794
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAEW-----------KELEK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 795 DREEfynqsqELQTKLEDCRNMIAE---------LRVELKKannkvchtELLLSQVSQKLSNSESVQQQMEFLnRQLLVL 865
Cdd:pfam13868 148 EEER------EEDERILEYLKEKAEreeereaerEEIEEEK--------EREIARLRAQQEKAQDEKAERDEL-RAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497764 866 GEVN----ELYLEQLQSKHpdttKEVEMMKTAYRKELEKNRSHLLQQNQRLDASQRRVLELESLLAKKDHLLLEQKK--- 938
Cdd:pfam13868 213 EEQErkerQKEREEAEKKA----RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRmkr 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755497764 939 --YLEDVKSQAsgqllaaESRyEAQRKITRVLELEILDlygrlekdgRLRKL 988
Cdd:pfam13868 289 leHRRELEKQI-------EER-EEQRAAEREEELEEGE---------RLREE 323
|
|
| |
