|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-667 |
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: 909.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 7 VGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHD----------------- 69
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDkhlfdklneclkkaatr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 70 ----------------------------------KMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 115
Cdd:pfam04388 81 lqaltllghvvrrqptwlhkianhpllksllkclKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 116 KKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 195
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 196 WKRLETHDVVIECAKISLDPTEASYEDGYSVShqisarfphrSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQL 275
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 276 PQTLSSPSTRLITEPPqaTLWSPSMVCGMTTPPTSPGNVP-------PDLSHPYSKVFGTTG--GKGTPLG--TPATSPP 344
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPttpselsPSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 345 PAPLCHSDDYVHISLP--QATVTPPRKEERMDSARPCLHRQHHL-LNDRGSEEPPGSKGSVTLSDLPGFLGDLA-SEEDS 420
Cdd:pfam04388 389 KQPPPLSDSHVHRALPasSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 421 IEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYR--DSLPGSQRK--------THSAASSSQGASVNPE-----PLH 485
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 486 SSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAH 565
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 566 HFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLL 645
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 2240436685 646 LHNQLLYERFKRQQHALRNRRL 667
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
653-890 |
1.73e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQ 729
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELeleLEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 730 LQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELyLEQLQNKHSDTTK 809
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELEEAEEELEE-AEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 810 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRIT 889
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
.
gi 2240436685 890 Q 890
Cdd:COG1196 449 E 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
634-895 |
1.81e-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: 65.46 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 634 DEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIqmwKVSLQKEQARYNQLQ 713
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 714 EQRDT---MVTKLHSQIRQLqhdREEFynqsQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNrqllvlG 790
Cdd:TIGR02168 796 EELKAlreALDELRAELTLL---NEEA----ANLRERLESLERRIAATERRLEDLEEQI---EELSEDIESLA------A 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 791 EVNELylEQLQNKHSDTTKEVEMMKAAYRKELEKNRShvlqqtqRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLq 870
Cdd:TIGR02168 860 EIEEL--EELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLAQLEL- 929
|
250 260
....*....|....*....|....*.
gi 2240436685 871 argQLQAAESRY-EAQKRITQVFELE 895
Cdd:TIGR02168 930 ---RLEGLEVRIdNLQERLSEEYSLT 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
653-905 |
2.64e-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: 65.08 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRN----------------RRLLRKVIKAAA--LEEHNAAMKD-QLKLQEKDIQMWKVS--LQKEQARYNQ 711
Cdd:TIGR02168 213 ERYKELKAELRElelallvlrleelreeLEELQEELKEAEeeLEELTAELQElEEKLEELRLEVSELEeeIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 712 LQEQRDTMVTK----------LHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 781
Cdd:TIGR02168 293 LANEISRLEQQkqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 782 LNRQLlvlgevnELYLEQLQNKHSDTTKEVemmkAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD-HLLLEQ 860
Cdd:TIGR02168 373 RLEEL-------EEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2240436685 861 KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 905
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
702-895 |
5.85e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 702 LQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEF 781
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL---EQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 782 LNRQLLVLGEVNELY---LEQLQNKHSDTTKEVEMMKAAyRKELEKNRSHVLQQTQRLDTS----QKRILELESHLAKKD 854
Cdd:COG4372 85 LNEQLQAAQAELAQAqeeLESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLESLQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436685 855 HLLLEQKKYLEDVKLQ-ARGQLQAAESryEAQKRITQVFELE 895
Cdd:COG4372 164 EELAALEQELQALSEAeAEQALDELLK--EANRNAEKEEELA 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
656-905 |
9.32e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 656 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDRE 735
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 736 EFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLvlgEVNELYLEQLQNKHSDTTKEVEMMK 815
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALL---EAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 816 AA--YRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFE 893
Cdd:COG1196 394 AAaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250
....*....|..
gi 2240436685 894 LEILDLYGRLEK 905
Cdd:COG1196 474 LLEAALAELLEE 485
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
682-903 |
1.10e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.94 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 682 AAMKDQLKLqekdiqmwkVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 758
Cdd:COG1579 1 AMPEDLRAL---------LDLQELDSELDRLEHRLKELpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 759 RIELKKANNKLSNSESvqqqmeflNRQllvlgevnelyLEQLQnkhsdttKEVEMMKAAyRKELEKnrsHVLQQTQRLDT 838
Cdd:COG1579 72 EARIKKYEEQLGNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436685 839 SQKRILELESHLAKKDHLLLEQKKYLEdvklQARGQLQAAESRYEAQ-KRITQVFELEILDLYGRL 903
Cdd:COG1579 122 LEEELAELEAELAELEAELEEKKAELD----EELAELEAELEELEAErEELAAKIPPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-893 |
1.15e-09 |
|
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: 62.77 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 652 YERFKRQQHAlrNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHS------ 725
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeele 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 726 ----QIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESvqqQMEFLNRQLLVLGEVNElylEQLQ 801
Cdd:TIGR02168 355 sleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEIE---ELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 802 NKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLakkdhllleqkkyledvkLQARGQLQAAESR 881
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL------------------DAAERELAQLQAR 490
|
250
....*....|..
gi 2240436685 882 YEAQKRITQVFE 893
Cdd:TIGR02168 491 LDSLERLQENLE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-861 |
5.13e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 663 RNRRLLRKVIKaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQL-QHDR--EEFYN 739
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 740 QSQELQTKLEDCRN-----MIAELRIELKKANNKLSNSES----VQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTTKE 810
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNqisqNNKIISQLNEQISQL----KKELTNSESENSEKQRE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 811 VEMMKAAYRKELEKNRSHvLQQTQRLdTSQKRILELESHLAKKDHLLLEQK 861
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSY-KQEIKNL-ESQINDLESKIQNQEKLNQQKDEQ 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
673-894 |
1.21e-08 |
|
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: 59.30 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 673 KAAALEEHNAamkdQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCR 752
Cdd:TIGR02168 675 RRREIEELEE----KIEELEEKIA----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 753 NMIAELRIELKKANNKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQ 832
Cdd:TIGR02168 747 ERIAQLSKELTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436685 833 TQRLDTSQKRILELESHLAKkdhlLLEQKKYLEDVKLQARGQL-QAAESRYEAQKRITQVFEL 894
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIeELEELIEELESELEALLNE 881
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
628-895 |
1.21e-08 |
|
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: 59.31 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 628 GGS--PPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKvikaAALEEHNAAMKD---QLKLQEKDIQMwkvsL 702
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDasrKIGEIEKEIEQ----L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 703 QKEQARYNQLQEQrdtmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNS--ESVQQQME 780
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 781 FLNRQLlvlgEVNELYLEQLQNKHSDTTKEVEMM------KAAYRKELEKNRSHVlqqTQRLDTSQKRILELESHLAKKD 854
Cdd:TIGR02169 802 KLEEEV----SRIEARLREIEQKLNRLTLEKEYLekeiqeLQEQRIDLKEQIKSI---EKEIENLNGKKEELEEELEELE 874
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2240436685 855 HLLLEQKKYLEDVK---LQARGQLQAAESRYEAQKriTQVFELE 895
Cdd:TIGR02169 875 AALRDLESRLGDLKkerDELEAQLRELERKIEELE--AQIEKKR 916
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
682-905 |
6.26e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 682 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIE 761
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 762 LKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAaYRKELEKNRSHVLQQTQRLDTSQK 841
Cdd:COG4942 92 IAELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2240436685 842 RILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 905
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
692-890 |
9.89e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 692 EKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKK---- 764
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 765 ------ANNKLS---NSESVQqqmEFLNRQllvlgevneLYLEQLQNKHSDTTKEVemmKAAyRKELEKNRSHVLQQTQR 835
Cdd:COG3883 95 lyrsggSVSYLDvllGSESFS---DFLDRL---------SALSKIADADADLLEEL---KAD-KAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2240436685 836 LDTSQKrilELESHLAKKDHLLLEQKKYLEDVKLQaRGQLQAAESRYEAQKRITQ 890
Cdd:COG3883 159 LEALKA---ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
686-858 |
1.34e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 686 DQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLH---SQIRQLQHDRE--EFYNQSQELQTKLEDCRNMIAELRI 760
Cdd:COG4717 71 KELKELEEELK----EAEEKEEEYAELQEELEELEEELEeleAELEELREELEklEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 761 ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKH----SDTTKEVEMM---KAAYRKELEKNRSHVLQQT 833
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELqqrLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*..
gi 2240436685 834 QRLD--TSQKRILELESHLAKKDHLLL 858
Cdd:COG4717 227 EELEqlENELEAAALEERLKEARLLLL 253
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
664-885 |
5.56e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.62 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 664 NRRLLRKVIKAAALEEHNAAMkdQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVT------KLHSQIRQLQHDREEF 737
Cdd:pfam00038 10 NDRLASYIDKVRFLEQQNKLL--ETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAEDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 738 YNQSQELQTKLEDCRNMIAELRIELKKANnkLSNSEsVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEM---- 813
Cdd:pfam00038 88 RQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVD-LEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMdaar 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 814 ----------MKAAY-------RKELEKN---RSHVLQQ-----TQRLDTSQKRILE-------LESHLAKkdhlLLEQK 861
Cdd:pfam00038 165 kldltsalaeIRAQYeeiaaknREEAEEWyqsKLEELQQaaarnGDALRSAKEEITElrrtiqsLEIELQS----LKKQK 240
|
250 260
....*....|....*....|....
gi 2240436685 862 KYLEDvklqargQLQAAESRYEAQ 885
Cdd:pfam00038 241 ASLER-------QLAETEERYELQ 257
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
673-802 |
1.32e-06 |
|
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: 48.79 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 673 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQ-IRQLQHDREEFynqsQELQTKledc 751
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVL-HAEdIKALQALREEL----NELKAE---- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436685 752 rnmIAELRIELKKANNKLSNSES--------VQQQMEFLNRQLLVLGEVNELYLEQLQN 802
Cdd:pfam07926 73 ---IAELKAEAESAKAELEESEEsweeqkkeLEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-870 |
1.75e-06 |
|
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: 52.33 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 677 LEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIA 756
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIE----KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 757 ELRIELKKANNKLSNsesvqqqmefLNRQLLVLG-EVNEL--YLEQLQNKHSDTTKEVEMMKaayrKELEKNRSHVLQQT 833
Cdd:TIGR04523 430 RLKETIIKNNSEIKD----------LTNQDSVKElIIKNLdnTRESLETQLKVLSRSINKIK----QNLEQKQKELKSKE 495
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2240436685 834 QRLD--TSQKRILELE-SHLAKKDHLLLEQKKYLEDVKLQ 870
Cdd:TIGR04523 496 KELKklNEEKKELEEKvKDLTKKISSLKEKIEKLESEKKE 535
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
689-905 |
2.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 689 KLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklhSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRIELKKANNK 768
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELE--------EELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 769 LSNSESVQQ------QMEFLNRQLLVLGEVnelyLEQLQNKHsDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKR 842
Cdd:COG4717 118 LEKLEKLLQllplyqELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436685 843 ilELESHLAKKDHLLLEQKKYLEDVKlQARGQLQAAESRYEAQKRitqvfELEILDLYGRLEK 905
Cdd:COG4717 193 --ELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLEN-----ELEAAALEERLKE 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
664-801 |
2.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 664 NRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYNQLQEQRDTMVTKL---HSQIRQLQHDREEFY 738
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 739 NQSQ--------ELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 801
Cdd:COG3206 305 AQLQqeaqrilaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
654-890 |
3.79e-06 |
|
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: 51.28 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 654 RFKRQQHALRNRRLLRKVIKAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQ---EQRDtmvtklhsqiRQL 730
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 731 QHDREEfynqSQELQTKLEDCRNMIAelriELKKANNKLSNSESVQQQMEFLNRQLLvlgevnELYLEQLQNKHSDTTKE 810
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEE----ERKRKKLELEKEKRDRKRAEEQRRKIL------EKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 811 VEMMKaayrKELEKNRSHVLQQTQRLDTSQKRILELEshlakkdhllLEQKKYLEDVKLQA---RGQLQAAESRYEAQKR 887
Cdd:pfam17380 515 RKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
...
gi 2240436685 888 ITQ 890
Cdd:pfam17380 581 IVE 583
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
666-896 |
4.54e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 666 RLLRKVIKAAA--------LEEHNAaMKDQLKLQEKDI-QMWKVSLQKEQARYN----QLQEQRDTMVTKLHSQIRQLQH 732
Cdd:pfam13868 9 RELNSKLLAAKcnkerdaqIAEKKR-IKAEEKEEERRLdEMMEEERERALEEEEekeeERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 733 DREEFYNQS-QELQTKLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVN--ELYLEQLQNKhsDTTK 809
Cdd:pfam13868 88 KRQEEYEEKlQEREQMDEIVERIQEE---DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEkeEEREEDERIL--EYLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 810 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILElesHLAKKDHLLLeqKKYLEDVKLQARGQ-LQAAESRYEAQKRI 888
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---EKAERDELRA--KLYQEEQERKERQKeREEAEKKARQRQEL 237
|
....*...
gi 2240436685 889 TQVFELEI 896
Cdd:pfam13868 238 QQAREEQI 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-906 |
6.10e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 657 RQQHALRNRRLLRKVIKAA-----ALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ---RDTMVTKLHSQIR 728
Cdd:COG4372 39 ELDKLQEELEQLREELEQAreeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 729 QLQHDREEFYNQSQELQTKledcrnmIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQlqnkhsDTT 808
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQ-------IAELQSEIAEREEEL---KELEEQLESLQEELAALEQELQALSEA------EAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 809 KEVEMMKAAYRKELEKNRSHvlqQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRI 888
Cdd:COG4372 183 QALDELLKEANRNAEKEEEL---AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*...
gi 2240436685 889 TQVFELEILDLYGRLEKD 906
Cdd:COG4372 260 IEELELAILVEKDTEEEE 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
725-906 |
8.41e-06 |
|
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: 49.38 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 725 SQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 800
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 801 QNKHSDTTKEV-EMMKAAYRKELEKNRSHVLQQTQRLDTSqkRILELESHLAKKDHLLLEQ----KKYLEDVK---LQAR 872
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELAALRaelEAER 173
|
170 180 190
....*....|....*....|....*....|....
gi 2240436685 873 GQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 906
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-907 |
1.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 673 KAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYNQLQEQRDTMV-----------------TKLHSQIRQLQHDRE 735
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEeliaerretieekreraEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 736 EFYNQSQELQTKLEDCRNMIAEL---RIELKKANNKLSNSESVQ-------QQMEFLNRQLLVLGEVNELYLEQLQNKhS 805
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELnskLAELKERIESLERIRTLLaaiadaeDEIERLREKREALAELNDERRERLAEK-R 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 806 DTTKEVE-------MMKAAYRKE-----LEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------LLEQKKYLEDV 867
Cdd:PRK02224 634 ERKRELEaefdearIEEAREDKEraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerreaLENRVEALEAL 713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 868 KLQARgQLQAAESRYEAQKRITQVFELEIL-----------DLYGRLEKDG 907
Cdd:PRK02224 714 YDEAE-ELESMYGDLRAELRQRNVETLERMlnetfdlvyqnDAYSHIELDG 763
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
656-896 |
1.29e-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: 49.58 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 656 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM--VTKLHSQIRQLQHD 733
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 734 REEFYNQSQEL-------------------QTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNE 794
Cdd:TIGR00618 269 IEELRAQEAVLeetqerinrarkaaplaahIKAVTQIEQQAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 795 LyLEQLQNKHSDTTKEVEmmKAAYRKElEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQA--- 871
Cdd:TIGR00618 346 L-LQTLHSQEIHIRDAHE--VATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrd 421
|
250 260
....*....|....*....|....*.
gi 2240436685 872 -RGQLQAAESRYEAQKRITQVFELEI 896
Cdd:TIGR00618 422 lQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
633-824 |
2.03e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 633 SDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIKAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 708
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 709 YNQLQEQRDTMVTklhsQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIEL-------------------KKANNKL 769
Cdd:TIGR02168 889 LALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqerlseeysltleeaeALENKIE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436685 770 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN---KHSDTTKEVEMMKAAyRKELEK 824
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEElkeRYDFLTAQKEDLTEA-KETLEE 1021
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
669-905 |
2.17e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 669 RKVIKAaaLEEHNAAMKDQLKlqekDI-QMWKvSLQKEqarynqLQEQrdtmVTKLHSQIRQLQhdrEEFYN-------- 739
Cdd:PRK04778 197 REILDQ--LEEELAALEQIME----EIpELLK-ELQTE------LPDQ----LQELKAGYRELV---EEGYHldhldiek 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 740 QSQELQTKLEDCRNMIAELriELKKANNKLSNSESVQQQM------EFLNRQlLVLGEVNEL--YLEQLQNKHSDTTKEV 811
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilerEVKARK-YVEKNSDTLpdFLEHAKEQNKELKEEI 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 812 EMMKAAYR---KELEKNRSH----------VLQQTQRLDTSQKRILELESHLAK-KDHLL---LEQKKYLEDVKlqargQ 874
Cdd:PRK04778 334 DRVKQSYTlneSELESVRQLekqleslekqYDEITERIAEQEIAYSELQEELEEiLKQLEeieKEQEKLSEMLQ-----G 408
|
250 260 270
....*....|....*....|....*....|.
gi 2240436685 875 LQAAESryEAQKRItQVFELEILDLYGRLEK 905
Cdd:PRK04778 409 LRKDEL--EAREKL-ERYRNKLHEIKRYLEK 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
684-896 |
2.22e-05 |
|
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: 48.89 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 684 MKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQIRQLQHDREEFYNQSQELQTKLEDcrnmIAELRIELK 763
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIVKSYENELDPLKNRLKE----IEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 764 KANNKLSNSESVQQQMEFLNRQL-LVLGEV---NELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTS 839
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELeLKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLN----KERRLLNQE 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436685 840 QKRILELESHLAKKDHLLLEQ--KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEI 896
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
653-795 |
2.66e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRNR-RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTM---VTKLHSQIR 728
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELeaeLAELQEELE 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436685 729 QL-QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNEL 795
Cdd:COG4717 181 ELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQLENELEAAALEERL 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
652-836 |
2.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 652 YERFKRQQHALRNRRllrkvikaAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQAR--YNQLQEQRDTMVTKLHsQIRQ 729
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALEaeLAELPERLEELEERLE-ELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 730 LQHDREEFYNQSQELQTKLEDCRNMI-AELRIELKKANNKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTT 808
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL---EELQQRLAELEEE-----------LEEAQEELEELE 226
|
170 180
....*....|....*....|....*...
gi 2240436685 809 KEVEMMKAAYRKELEKNRshvLQQTQRL 836
Cdd:COG4717 227 EELEQLENELEAAALEER---LKEARLL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
673-904 |
3.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 673 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCR 752
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 753 NMIAELRIELKKANNKLSNsesvqqqmeflNRQLLVLG-----------------------EVNEL--YLEQLQNKHSDT 807
Cdd:PRK02224 426 EREAELEATLRTARERVEE-----------AEALLEAGkcpecgqpvegsphvetieedreRVEELeaELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 808 TKEVEMMKAAyrKELEKNRSHVLQQ----TQRLDTSQKRILELESHLAKKDhlllEQKKYLEDVKLQARGQLQAAESRYE 883
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEERredlEELIAERRETIEEKRERAEELR----ERAAELEAEAEEKREAAAEAEEEAE 568
|
250 260
....*....|....*....|.
gi 2240436685 884 AQKRITQVFELEILDLYGRLE 904
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIE 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
677-903 |
3.77e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 677 LEEHNAAMKDQLKLQEKDIQMWKvslQKEQARYNQLQEQRDTmvtklHSQIR-QLQHDREEFYNQSQELQTKL----EDC 751
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEK-----EMNLRdELESVREEFIQKGDEVKCKLdkseENA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 752 RNMIAELRIEL--------------KKANNKLSNSESVQQQMEFL-------NRQLlvlgEVNELYLEQLQNKHSDTTKE 810
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlkKQIENKNKNIEELHQENKALkkkgsaeNKQL----NAYEIKVNKLELELASAKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 811 VEMMKAAYRKELEKNR---SHVLQQTQRLDTSQKRILELESHLAKK-DH------LLLEQKKYLEDVKLQAR-GQLQAAE 879
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHkiaemvALMEKHKHQYDKIIEERdSELGLYK 731
|
250 260
....*....|....*....|....
gi 2240436685 880 SRYEAQKRITQVFELEILDLYGRL 903
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
665-890 |
3.77e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 665 RRLLRKVIKAAALEEHNAAMKD----QLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEF 737
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvVEELTAKKMTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 738 YNQSQELQTK---LEDCRNMIAELRI-------ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN----- 802
Cdd:pfam15921 499 SDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtqlv 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 803 -KHSDTTKEVEMMKAAYRKELEKNRSHvLQQTQRL-DTSQKRILELESHLAKkdhllLEqkkyLEDVKLqargqLQAAES 880
Cdd:pfam15921 579 gQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILkDKKDAKIRELEARVSD-----LE----LEKVKL-----VNAGSE 643
|
250
....*....|
gi 2240436685 881 RYEAQKRITQ 890
Cdd:pfam15921 644 RLRAVKDIKQ 653
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
653-899 |
4.74e-05 |
|
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: 46.84 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRNRRLLRKVIKAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYNQLQE------------------ 714
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAewkelekeeereederil 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 715 ----QRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKlsnSESVQQQMEFLNRQLLVLG 790
Cdd:pfam13868 159 eylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE---RKERQKEREEAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 791 EVNELYLEQLQNKhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDtsQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 870
Cdd:pfam13868 236 ELQQAREEQIELK--------ERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
250 260 270
....*....|....*....|....*....|...
gi 2240436685 871 ARGQ----LQAAESRYEAQKRITQVFELEILDL 899
Cdd:pfam13868 306 RAAEreeeLEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
656-853 |
9.80e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 656 KRQQHALRNRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ---- 731
Cdd:COG4942 41 KELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 732 ----------HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgEVNELYLEQLQ 801
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL----EEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2240436685 802 NKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTSQKRILELESHLAKK 853
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
684-886 |
1.29e-04 |
|
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: 44.37 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 684 MKDQLKLQEKDIQMWKVSLQKeqarYNQLQEQRDTMVTKLHSQIrqlqhdreefynqsQELQTKLEDCRNMIAELRIELK 763
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQE----CEEIERRRQELASRYTQQT--------------AELQTQLLQKEKEQASLKKELQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 764 KANNKLSNSESVQQQMEFLnrqllvlgevnELYLEQLQNKHSDTTKEVEMM----KAAYRKEL---------EKNRSHVL 830
Cdd:pfam14988 72 ALRPFAKLKESQEREIQDL-----------EEEKEKVRAETAEKDREAHLQflkeKALLEKQLqelrilelgERATRELK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436685 831 QQTQRLDTSQKRILELESHLAKKDHLLLeQKKYLEdvKLQARGQLQAAESRYEAQK 886
Cdd:pfam14988 141 RKAQALKLAAKQALSEFCRSIKRENRQL-QKELLQ--LIQETQALEAIKSKLENRK 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
684-905 |
1.34e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 684 MKDQLKLQEKDIQmwkvsLQKEQAR--YNQLQEQRDT---MVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 758
Cdd:COG1340 2 KTDELSSSLEELE-----EKIEELReeIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 759 RIELKKANNKLSnseSVQQQMEFLNRQLLVLGEVNELyLEQLQnkhsdttKEVEmmkaayrkELEKNrshvlQQTQRLDT 838
Cdd:COG1340 77 KEERDELNEKLN---ELREELDELRKELAELNKAGGS-IDKLR-------KEIE--------RLEWR-----QQTEVLSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 839 SQ-----KRILELESHLAKKDHLLLEQKKYLEDVKlqargqlQAAESRYEAQ---KRITQVFE------LEILDLYGRLE 904
Cdd:COG1340 133 EEekelvEKIKELEKELEKAKKALEKNEKLKELRA-------ELKELRKEAEeihKKIKELAEeaqelhEEMIELYKEAD 205
|
.
gi 2240436685 905 K 905
Cdd:COG1340 206 E 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
666-870 |
1.49e-04 |
|
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: 45.78 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 666 RLLRKVIKAAA----LEEHNAAMKDQLK-------LQEKDIQMWKVSLQKEQARYNQLQ---EQRDTMVTKLHSQIRQLQ 731
Cdd:TIGR04523 430 RLKETIIKNNSeikdLTNQDSVKELIIKnldntreSLETQLKVLSRSINKIKQNLEQKQkelKSKEKELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 732 hdreefyNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ--LQN 802
Cdd:TIGR04523 510 -------EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQksLKK 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 803 KHS---DTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 870
Cdd:TIGR04523 583 KQEekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
653-837 |
1.50e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRN----RRLLRKviKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQ-KEQARYNQlQEQ-RDTMVTKLHSQ 726
Cdd:PRK10929 65 ERAKQYQQVIDNfpklSAELRQ--QLNNERDEPRSVPPNMSTDALEQEILQVSSQlLEKSRQAQ-QEQdRAREISDSLSQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 727 IRQLQHD-REEFYNQSQELQTkledcrnmiaelrieLKKANNKLSNSESVQQQMEFLNRQLLVlgevNELYLEQLQnkhs 805
Cdd:PRK10929 142 LPQQQTEaRRQLNEIERRLQT---------------LGTPNTPLAQAQLTALQAESAALKALV----DELELAQLS---- 198
|
170 180 190
....*....|....*....|....*....|...
gi 2240436685 806 dttkevemmkAAYRKELEKNRSHVLQ-QTQRLD 837
Cdd:PRK10929 199 ----------ANNRQELARLRSELAKkRSQQLD 221
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
658-763 |
1.66e-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: 44.13 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 658 QQHALRNRRLlrkVIKAAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYNQLQEQRDTMvtKLHSQ-----IRQLQH 732
Cdd:pfam13851 50 SEIQQENKRL---TEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 2240436685 733 DREEFYNQS----QELQTKLEdCRNMIAELRIELK 763
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
665-848 |
2.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 665 RRLLRKVIK-AAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTklhsqirqLQHDREEFYNQSQE 743
Cdd:PRK03918 244 EKELESLEGsKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 744 LQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELY---------LEQLQNKHSDTTKE--VE 812
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEklEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436685 813 MMKAA--YRKELEKNRSHVLQQTQRLDTSQKR----ILELES 848
Cdd:PRK03918 392 ELEELekAKEEIEEEISKITARIGELKKEIKElkkaIEELKK 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
685-893 |
2.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 685 KDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEfyNQSQELQTKLEDCRNMIAELRielkK 764
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREIAELEAELERLD----A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 765 ANNKLsnsESVQQQmeflnrqllvlgevnelyLEQLQNKHSDTTKEVEMMKAAyRKELEKNRShvlQQTQRLDTSQKRIL 844
Cdd:COG4913 683 SSDDL---AALEEQ------------------LEELEAELEELEEELDELKGE-IGRLEKELE---QAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2240436685 845 ELESHLAKKDHLLLEQK-------KYLEDVKLQARGQLQAAESRYE-AQKRITQVFE 893
Cdd:COG4913 738 AAEDLARLELRALLEERfaaalgdAVERELRENLEERIDALRARLNrAEEELERAMR 794
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
682-887 |
3.81e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 682 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEfynqsQElqtkledcRNMIAELRIE 761
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLEQQQAA-----QE--------RLLAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 762 LKKANNK-----LSNSESvqQQMEflnRQLLVLGEVNEL---YLEQLQNkhsdTTKEVemmkAAYRKELEKNRSH---VL 830
Cdd:PRK11637 134 FRQGEHTglqliLSGEES--QRGE---RILAYFGYLNQArqeTIAELKQ----TREEL----AAQKAELEEKQSQqktLL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436685 831 ----QQTQRLDTS----QKRILELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESryEAQKR 887
Cdd:PRK11637 201 yeqqAQQQKLEQArnerKKTLTGLESSLQKDQQQLSE----LRANESRLRDSIARAER--EAKAR 259
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
755-883 |
6.66e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.70 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 755 IAELRIELKKANNKLSNSES-VQQQMEFLNRQLLVLGEVNELYLEQLQnKHSDTTKEVEmmkaAYRKELEKNRSHVLQQT 833
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAqLQKLQEDLEKQAEIAREAQQNYERELV-LHAEDIKALQ----ALREELNELKAEIAELK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2240436685 834 QRLDTSQKRILELESHLAkkdhlllEQKKYLEDvklqargQLQAAESRYE 883
Cdd:pfam07926 78 AEAESAKAELEESEESWE-------EQKKELEK-------ELSELEKRIE 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
652-836 |
8.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 652 YERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKD----IQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQI 727
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 728 RQlqHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDT 807
Cdd:COG4717 423 EA--LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
170 180
....*....|....*....|....*....
gi 2240436685 808 TkeVEMMKAAYRKElekNRSHVLQQTQRL 836
Cdd:COG4717 501 L--LEEAREEYREE---RLPPVLERASEY 524
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
673-891 |
8.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 673 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYN--QLQEQRDTMVTK---LHSQIRQLQHDREEFYNQSQELQTK 747
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQlseLESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 748 LEDCRNMIAELrielkkannklSNSESVQQQMEFLNRQLLVLGEVNELYLE----------QLQNKHSDTTKEVEMMKAA 817
Cdd:COG3206 249 LGSGPDALPEL-----------LQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436685 818 YRKELEKNRSHVLQQTQRLDTSQKRILELESHlakkdhllleQKKYLEdvkLQArgQLQAAESRYEA-QKRITQV 891
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPEL----------EAELRR---LER--EVEVARELYESlLQRLEEA 377
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
668-884 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 668 LRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ-RDTMVTKlhsqirqlqHDREEfynqsqelqt 746
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlREVENEK---------NDKDK---------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 747 KLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQNKHSDTTKEvEMMKAayrkeLEKNR 826
Cdd:pfam10174 601 KIAELESLTLR---QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-ELMGA-----LEKTR 668
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 827 SHVLQQTQRLDTSQKRILELESHLAKkdhLLLEQKKYLEDV---KLQArgqLQAAESRYEA 884
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
678-850 |
1.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 678 EEHNAAMKDQL-KLQEKDIQMWKvsLQKEQARYNQLQEQRDTMVTKLHSQIRQLQhDREEFYNQSQELQTKLEDCRNMIA 756
Cdd:PRK01156 280 ERHMKIINDPVyKNRNYINDYFK--YKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQIL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 757 ELRIELKKANNKLSNSESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRL 836
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKN-----------IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
170
....*....|....
gi 2240436685 837 DTSQKRILELESHL 850
Cdd:PRK01156 426 SSLNQRIRALRENL 439
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
658-835 |
1.40e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 658 QQHALRNRRLLRKVIKaaaLEEHNAAMKDqLKLQEKDIQMWKVSLQKEQARYN---------QLQEQRDTMVTKLHSQIR 728
Cdd:PHA02562 234 AEIEELTDELLNLVMD---IEDPSAALNK-LNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 729 QLQHDREEFYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSesvQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTT 808
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTN---KQSLITLVDKAKKV----KAAIEELQAEFVDNA 378
|
170 180
....*....|....*....|....*..
gi 2240436685 809 KEVEMMKAAYRKELEKNRSHVLQQTQR 835
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
662-904 |
1.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 662 LRNRRLLRKVIkaaaleehnaamkDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLhSQIRQLQ---HDRE--- 735
Cdd:COG3206 90 LKSRPVLERVV-------------DKLNLDEDPLG----EEASREAAIERLRKNLTVEPVKG-SNVIEISytsPDPElaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 736 -------EFYNQSQeLQTKLEDCRNMIAELRIELKKANNKLSNSEsvQQQMEFLNRQLLV-LGEVNELYLEQ---LQNKH 804
Cdd:COG3206 152 avanalaEAYLEQN-LELRREEARKALEFLEEQLPELRKELEEAE--AALEEFRQKNGLVdLSEEAKLLLQQlseLESQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 805 SDTTKEVEMMKAAY---RKELEKNRSHV--LQQTQRLDTSQKRILELESHLAKkdhlllEQKKYLE---DVKlQARGQLQ 876
Cdd:COG3206 229 AEARAELAEAEARLaalRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAE------LSARYTPnhpDVI-ALRAQIA 301
|
250 260
....*....|....*....|....*....
gi 2240436685 877 AAESRYEAQ-KRITQVFELEILDLYGRLE 904
Cdd:COG3206 302 ALRAQLQQEaQRILASLEAELEALQAREA 330
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
654-886 |
1.72e-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: 42.73 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 654 RFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHD 733
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 734 REEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgevnelyLEQLQNKHSDTTKEVEM 813
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----------ENKIQDGKDDYLKQKET 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 814 MKAAYRKELEKNRSH-------VLQQTQRLDTS--QKRILELESHLAKKDHLLLEQKKYLEDvKLQARGQLQAAESRYEA 884
Cdd:TIGR00606 978 ELNTVNAQLEECEKHqekinedMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQ-HLKEMGQMQVLQMKQEH 1056
|
..
gi 2240436685 885 QK 886
Cdd:TIGR00606 1057 QK 1058
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
674-765 |
2.26e-03 |
|
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: 39.49 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 674 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNqlQEQRDTMVTKLHSQIRQLQHDREEFynqSQELQTKLedcRN 753
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|..
gi 2240436685 754 MIAELRIELKKA 765
Cdd:smart00935 92 ELQKILDKINKA 103
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
684-905 |
2.38e-03 |
|
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: 41.98 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 684 MKDQLKLQEKDIQMW---KVSLQKEQARYNQLQEQRDTmvtklhsqirqlqhdreeFYNQSQELQTKLEDCRNMIAELRI 760
Cdd:pfam05622 150 LRRQVKLLEERNAEYmqrTLQLEEELKKANALRGQLET------------------YKRQVQELHGKLSEESKKADKLEF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 761 ELKKANNKLsnsESVQQQMEFLNRQLLVLGEVN-ELYLEQLQNKH----------SDTTKEV---EMMKAAYRKELEK-- 824
Cdd:pfam05622 212 EYKKLEEKL---EALQKEKERLIIERDTLRETNeELRCAQLQQAElsqadallspSSDPGDNlaaEIMPAEIREKLIRlq 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 825 --NRSHVLQQT-----------QRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQV 891
Cdd:pfam05622 289 heNKMLRLGQEgsyrerltelqQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEH 368
|
250
....*....|....
gi 2240436685 892 FElEILDLYGRLEK 905
Cdd:pfam05622 369 LE-KLHEAQSELQK 381
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
656-843 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 656 KRQQHALRNRRLlRKVIKAA-----ALEEHNAAMKDQLKLQEKDIqMWKVSLQKEQARYNQLQeqrdtmvtklhSQIRQL 730
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDApaelrELRQELAALQAKAEAAPKEI-LASLSLEELEQRLLQTS-----------AQLQEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 731 QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQ------QQMEFLNRQLLVLGEVNELYLEQLQNkh 804
Cdd:pfam12795 98 QNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGeplseaQRWALQAELAALKAQIDMLEQELLSN-- 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2240436685 805 sdttkevEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRI 843
Cdd:pfam12795 176 -------NNRQDLLKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-906 |
3.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 702 LQKEQARYNQLQEQRdTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 781
Cdd:PRK03918 157 LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 782 LnRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVlQQTQRLDTSQKRILELESHLAKKDHLLLEQK 861
Cdd:PRK03918 236 L-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2240436685 862 KYLEDVKLQARG---QLQAAESRYEAQKRITQVFElEILDLYGRLEKD 906
Cdd:PRK03918 314 KRLSRLEEEINGieeRIKELEEKEERLEELKKKLK-ELEKRLEELEER 360
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
653-895 |
3.22e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRNRRLLRKVIKAAalEEHNaAMKDQLKLQEKDIQMWKVSLQKEQaRYNQLQEQRDTMVTKLHSQIRQLQH 732
Cdd:pfam05557 330 LNKKLKRHKALVRRLQRRVLLLT--KERD-GYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 733 DREEFYNQSQELQTkledcrnmiAELRIELKKANNKLSNSESVQQQMEFLNRqllvlgEVNELYLEQLQNKHSDTTKEVE 812
Cdd:pfam05557 406 AEEELGGYKQQAQT---------LERELQALRQQESLADPSYSKEEVDSLRR------KLETLELERQRLREQKNELEME 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 813 MMKAAYRKELEKNRSHVLQ---------------QTQRLD---TSQKRILE-LESHLAKKDHLLLEQKKYLEDVKLQARG 873
Cdd:pfam05557 471 LERRCLQGDYDPKKTKVLHlsmnpaaeayqqrknQLEKLQaeiERLKRLLKkLEDDLEQVLRLPETTSTMNFKEVLDLRK 550
|
250 260
....*....|....*....|..
gi 2240436685 874 QLQAAESRYEAQKRITQVFELE 895
Cdd:pfam05557 551 ELESAELKNQRLKEVFQAKIQE 572
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
700-887 |
3.72e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 700 VSLQKEQARYNQLQEQRDTMvtklhsqiRQLQ--HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANN-----KLSNS 772
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEM--------RRLEveRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEeirlrKQRLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 773 ESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHsdttkevemmkaayRKELEKNRSHVLQQTQRLDTSQKRILELESHLAK 852
Cdd:pfam15709 398 EERQRQEEEERKQRLQLQAAQERARQQQEEFR--------------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAE 463
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436685 853 KDHLLLEQKKYlEDVKLQARGQLQAAESRYEAQKR 887
Cdd:pfam15709 464 EQKRLMEMAEE-ERLEYQRQKQEAEEKARLEAEER 497
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
687-861 |
3.89e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 687 QLKLQEKDIQMWKVSLQK---EQARYNQLQEQRDtmVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELK 763
Cdd:COG5022 922 NLEFKTELIARLKKLLNNidlEEGPSIEYVKLPE--LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 764 KANNKLSNSESVQ---QQMEFLNRQLLVLGEVNELYLEQ---------LQNKHSDTTKEVEMMKA-----AYRKELEKNR 826
Cdd:COG5022 1000 ELAELSKQYGALQestKQLKELPVEVAELQSASKIISSEstelsilkpLQKLKGLLLLENNQLQArykalKLRRENSLLD 1079
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436685 827 SHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQK 861
Cdd:COG5022 1080 DKQLYQLESTENLLKTINVKDLEVTNRNLVKPANV 1114
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
706-871 |
4.12e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 706 QARYNQLQEQRDTMVTKLHSqirqLQHDREEFYNQSQELQTKLEDCRNMIAEL--RIE--LKKANNKLSNSESVQQQMef 781
Cdd:pfam10168 560 QKRVKLLKLQKEQQLQELQS----LEEERKSLSERAEKLAEKYEEIKDKQEKLmrRCKkvLQRLNSQLPVLSDAEREM-- 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 782 lNRQLLVLGEVnelyLEQLQNkhsdTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRIL-ELESHLAKKdhlLLEQ 860
Cdd:pfam10168 634 -KKELETINEQ----LKHLAN----AIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIkEILKQLGSE---IDEL 701
|
170
....*....|.
gi 2240436685 861 KKYLEDVKLQA 871
Cdd:pfam10168 702 IKQVKDINKHV 712
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
677-867 |
4.60e-03 |
|
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: 40.83 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 677 LEEHNAAMKDQLKLQEKDIQMwkvSLQKE----QARYNQLQEQrdtmvTKLHSQ-IRQLQHDREEFYNQSQELQTKLEDC 751
Cdd:pfam05622 287 LQHENKMLRLGQEGSYRERLT---ELQQLledaNRRKNELETQ-----NRLANQrILELQQQVEELQKALQEQGSKAEDS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 752 RNMIAELRIELKKANNKLSNSESVQQQMEflnrqllvlgevnELYLEQLQNKHSDTT--------KEVEM--MKAAYRKE 821
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIE-------------ELEPKQDSNLAQKIDelqealrkKDEDMkaMEERYKKY 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2240436685 822 LEKNRSHVlqqtQRLDTSQKRILELESHLAKKDhlLLEQKKYLEDV 867
Cdd:pfam05622 426 VEKAKSVI----KTLDPKQNPASPPEIQALKNQ--LLEKDKKIEHL 465
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
723-875 |
5.50e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.72 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 723 LHSQIRQLQHDREEFYNQSQELQTKLEDCRnmiaelrielKKANNKLSNSESVQQQMEFLN-------RQLLVLgevnEL 795
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQ----------QKESKFLENLASLKHENDNLSsmlnrkeRRLKDL----ED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 796 YLEQLQNKHsdttKEVEMMKAAYRKELEKNRSH---VLQQTQRLDTSQKRIleLESHLAKKDHLLLE---QKKYLEDVKL 869
Cdd:pfam17078 74 QLSELKNSY----EELTESNKQLKKRLENSSASettLEAELERLQIQYDAL--VDSQNEYKDHYQQEintLQESLEDLKL 147
|
....*.
gi 2240436685 870 QARGQL 875
Cdd:pfam17078 148 ENEKQL 153
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
770-887 |
7.08e-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: 38.05 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 770 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN--KHSDTTKEVEMMKAAYRKELEKNRSHVLQQ----TQRLDTSQKRI 843
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQELAILEAENskAEVETLKAEIEEMAQNLRDLELDLVTLRSEkenlTKELQKKQERV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2240436685 844 LELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESRYEAQKR 887
Cdd:pfam10473 97 SELESLNSSLENLLEE----KEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
674-905 |
8.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 674 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQaryNQLQEQRDTMvtklhSQIRQ-LQHDREEFYNQSQELQTKLEDC- 751
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESEN---AELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESe 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 752 --RNMIAE----LRIELKKANNKLSNSES----VQQQMEFLNRQllvLGEVNELYLEQLQNKHSDTTKevemmkaayRKE 821
Cdd:pfam01576 426 rqRAELAEklskLQSELESVSSLLNEAEGknikLSKDVSSLESQ---LQDTQELLQEETRQKLNLSTR---------LRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 822 LEKNRSHVLQQTQRLDTSQKRileLESHLAKKDHLLLEQKKYLEDVKlqarGQLQAAEsryEAQKRITQVFELEILDL-- 899
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRN---VERQLSTLQAQLSDMKKKLEEDA----GTLEALE---EGKKRLQRELEALTQQLee 563
|
250
....*....|
gi 2240436685 900 ----YGRLEK 905
Cdd:pfam01576 564 kaaaYDKLEK 573
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
632-905 |
8.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 632 PSDEIRTLRDQLLLLHNQLLYERFKRQQH-----ALRNR-RLLRKVIKAAAL--EEHNAAMKDQLKLQEKDIQMWKVSLQ 703
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQrsqleQAKEGlSALNRLLPRLNLlaDETLADRVEEIREQLDEAEEAKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 704 KEQARYNQLqeqrDTMVTKLHS---QIRQLQHDreefYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSESVQqqme 780
Cdd:PRK04863 915 QHGNALAQL----EPIVSVLQSdpeQFEQLKQD----YQQAQQTQRDA----KQQAFALTEVVQRRAHFSYEDAAE---- 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 781 flnrqllVLGEVNELyLEQLQNKHsdttKEVEMMKAAYRKELEknrshvlQQTQRLDTSQKRILELESHLAKKDHLLLEQ 860
Cdd:PRK04863 979 -------MLAKNSDL-NEKLRQRL----EQAEQERTRAREQLR-------QAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436685 861 KKYLEDVKLQA-----------RGQLQAAES-----RYEAQKRITqVFELEILDLYGRLEK 905
Cdd:PRK04863 1040 KQELQDLGVPAdsgaeerararRDELHARLSanrsrRNQLEKQLT-FCEAEMDNLTKKLRK 1099
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
653-824 |
9.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 653 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQH 732
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436685 733 DREEFYNQSQELQTKLEdcrnmIAELRIELKKANNKLSNsesvqqqmeflnrqllvLGEVNELYLE---QLQNKHSDTTK 809
Cdd:COG1196 745 EELLEEEALEELPEPPD-----LEELERELERLEREIEA-----------------LGPVNLLAIEeyeELEERYDFLSE 802
|
170
....*....|....*
gi 2240436685 810 EVEMMKAAyRKELEK 824
Cdd:COG1196 803 QREDLEEA-RETLEE 816
|
|
| |
