|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
16-597 |
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: 825.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 16 ITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETF 95
Cdd:pfam04388 131 ITLLPMIPQLVKQYLPDIFEIFGRLASWNLKNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 96 EEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVShqisarfphrSADVTTSP 175
Cdd:pfam04388 211 EETIKPMLEHVRIHPELVTGTKDHELDPTRWKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 176 YADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPqaTLWSPSMVCGMTTPPTSPGNVP-------PDL 248
Cdd:pfam04388 281 YTDQQSSYGSSTSTPSSTPRLQLSSSSGTSPPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPttpselsPSS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 249 SHPYSKVFGTTG--GKGTPLG--TPATSPPPAPLCHSDDYVHISLP--QATVTPPRKEERMDSARPCLHRQHHL-LNDRG 321
Cdd:pfam04388 359 SHLSSRGSSPPEaaGEATPETtpAKDSPYLKQPPPLSDSHVHRALPasSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 322 SEEPPGSKGSVTLSDLPGFLGDLA-SEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYR--DSLPGSQRK-- 396
Cdd:pfam04388 439 LLEPPGDKSSVTLSELPDFIKDLAlSSEDSVEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrn 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 397 ------THSAASSSQGASVNPE-----PLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCK 465
Cdd:pfam04388 519 riasycSSTSQSDSHGPATTPEskpsaLAEDGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 466 IPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKL 545
Cdd:pfam04388 599 IPSRQKVSTQSGQPLPYEHLFDLALPKTASLFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRL 678
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2240436701 546 PLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRL 597
Cdd:pfam04388 679 PLPSKSADWTHFGGSAPSDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-820 |
1.58e-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: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQ 659
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELeleLEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 660 LQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELyLEQLQNKHSDTTK 739
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELEEAEEELEE-AEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 740 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRIT 819
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
.
gi 2240436701 820 Q 820
Cdd:COG1196 449 E 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
564-825 |
1.68e-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: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 564 DEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIqmwKVSLQKEQARYNQLQ 643
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 644 EQRDT---MVTKLHSQIRQLqhdREEFynqsQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNrqllvlG 720
Cdd:TIGR02168 796 EELKAlreALDELRAELTLL---NEEA----ANLRERLESLERRIAATERRLEDLEEQI---EELSEDIESLA------A 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 721 EVNELylEQLQNKHSDTTKEVEMMKAAYRKELEKNRShvlqqtqRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLq 800
Cdd:TIGR02168 860 EIEEL--EELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLAQLEL- 929
|
250 260
....*....|....*....|....*.
gi 2240436701 801 argQLQAAESRY-EAQKRITQVFELE 825
Cdd:TIGR02168 930 ---RLEGLEVRIdNLQERLSEEYSLT 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
583-835 |
2.41e-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: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRN----------------RRLLRKVIKAAA--LEEHNAAMKD-QLKLQEKDIQMWKVS--LQKEQARYNQ 641
Cdd:TIGR02168 213 ERYKELKAELRElelallvlrleelreeLEELQEELKEAEeeLEELTAELQElEEKLEELRLEVSELEeeIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 642 LQEQRDTMVTK----------LHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 711
Cdd:TIGR02168 293 LANEISRLEQQkqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 712 LNRQLlvlgevnELYLEQLQNKHSDTTKEVemmkAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD-HLLLEQ 790
Cdd:TIGR02168 373 RLEEL-------EEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2240436701 791 KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 835
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
632-825 |
5.39e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 632 LQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEF 711
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL---EQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 712 LNRQLLVLGEVNELY---LEQLQNKHSDTTKEVEMMKAAyRKELEKNRSHVLQQTQRLDTS----QKRILELESHLAKKD 784
Cdd:COG4372 85 LNEQLQAAQAELAQAqeeLESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLESLQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436701 785 HLLLEQKKYLEDVKLQ-ARGQLQAAESryEAQKRITQVFELE 825
Cdd:COG4372 164 EELAALEQELQALSEAeAEQALDELLK--EANRNAEKEEELA 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
586-835 |
8.26e-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: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 586 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDRE 665
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 666 EFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLvlgEVNELYLEQLQNKHSDTTKEVEMMK 745
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALL---EAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 746 AA--YRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFE 823
Cdd:COG1196 394 AAaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250
....*....|..
gi 2240436701 824 LEILDLYGRLEK 835
Cdd:COG1196 474 LLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
582-823 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 582 YERFKRQQHAlrNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHS------ 655
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeele 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 656 ----QIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESvqqQMEFLNRQLLVLGEVNElylEQLQ 731
Cdd:TIGR02168 355 sleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEIE---ELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 732 NKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLakkdhllleqkkyledvkLQARGQLQAAESR 811
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL------------------DAAERELAQLQAR 490
|
250
....*....|..
gi 2240436701 812 YEAQKRITQVFE 823
Cdd:TIGR02168 491 LDSLERLQENLE 502
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
612-833 |
1.21e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.94 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 612 AAMKDQLKLqekdiqmwkVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 688
Cdd:COG1579 1 AMPEDLRAL---------LDLQELDSELDRLEHRLKELpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 689 RIELKKANNKLSNSESvqqqmeflNRQllvlgevnelyLEQLQnkhsdttKEVEMMKAAyRKELEKnrsHVLQQTQRLDT 768
Cdd:COG1579 72 EARIKKYEEQLGNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436701 769 SQKRILELESHLAKKDHLLLEQKKYLEdvklQARGQLQAAESRYEAQ-KRITQVFELEILDLYGRL 833
Cdd:COG1579 122 LEEELAELEAELAELEAELEEKKAELD----EELAELEAELEELEAErEELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
593-791 |
5.59e-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: 60.03 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 593 RNRRLLRKVIKaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQL-QHDR--EEFYN 669
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 670 QSQELQTKLEDCRN-----MIAELRIELKKANNKLSNSES----VQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTTKE 740
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNqisqNNKIISQLNEQISQL----KKELTNSESENSEKQRE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 741 VEMMKAAYRKELEKNRSHvLQQTQRLdTSQKRILELESHLAKKDHLLLEQK 791
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSY-KQEIKNL-ESQINDLESKIQNQEKLNQQKDEQ 413
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
603-824 |
1.11e-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: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 603 KAAALEEHNAamkdQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCR 682
Cdd:TIGR02168 675 RRREIEELEE----KIEELEEKIA----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 683 NMIAELRIELKKANNKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQ 762
Cdd:TIGR02168 747 ERIAQLSKELTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436701 763 TQRLDTSQKRILELESHLAKkdhlLLEQKKYLEDVKLQARGQL-QAAESRYEAQKRITQVFEL 824
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIeELEELIEELESELEALLNE 881
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
558-825 |
1.30e-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: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 558 GGS--PPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKvikaAALEEHNAAMKD---QLKLQEKDIQMwkvsL 632
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDasrKIGEIEKEIEQ----L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 633 QKEQARYNQLQEQrdtmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNS--ESVQQQME 710
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 711 FLNRQLlvlgEVNELYLEQLQNKHSDTTKEVEMM------KAAYRKELEKNRSHVlqqTQRLDTSQKRILELESHLAKKD 784
Cdd:TIGR02169 802 KLEEEV----SRIEARLREIEQKLNRLTLEKEYLekeiqeLQEQRIDLKEQIKSI---EKEIENLNGKKEELEEELEELE 874
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2240436701 785 HLLLEQKKYLEDVK---LQARGQLQAAESRYEAQKriTQVFELE 825
Cdd:TIGR02169 875 AALRDLESRLGDLKkerDELEAQLRELERKIEELE--AQIEKKR 916
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
612-835 |
5.77e-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: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 612 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIE 691
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 692 LKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAaYRKELEKNRSHVLQQTQRLDTSQK 771
Cdd:COG4942 92 IAELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2240436701 772 RILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 835
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
622-820 |
9.13e-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: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 622 EKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKK---- 694
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 695 ------ANNKLS---NSESVQqqmEFLNRQllvlgevneLYLEQLQNKHSDTTKEVemmKAAyRKELEKNRSHVLQQTQR 765
Cdd:COG3883 95 lyrsggSVSYLDvllGSESFS---DFLDRL---------SALSKIADADADLLEEL---KAD-KAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2240436701 766 LDTSQKrilELESHLAKKDHLLLEQKKYLEDVKLQaRGQLQAAESRYEAQKRITQ 820
Cdd:COG3883 159 LEALKA---ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
616-788 |
1.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 616 DQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLH---SQIRQLQHDRE--EFYNQSQELQTKLEDCRNMIAELRI 690
Cdd:COG4717 71 KELKELEEELK----EAEEKEEEYAELQEELEELEEELEeleAELEELREELEklEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 691 ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKH----SDTTKEVEMM---KAAYRKELEKNRSHVLQQT 763
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELqqrLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*..
gi 2240436701 764 QRLD--TSQKRILELESHLAKKDHLLL 788
Cdd:COG4717 227 EELEqlENELEAAALEERLKEARLLLL 253
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
594-815 |
4.57e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 53.00 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 594 NRRLLRKVIKAAALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYNQLQEQRDTMVT------KLHSQIRQLQHDREE 666
Cdd:pfam00038 10 NDRLASYIDKVRFLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 667 FYNQSQELQTKLEDCRNMIAELRIELKKANnkLSNSEsVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEM--- 743
Cdd:pfam00038 87 FRQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVD-LEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 744 -----------MKAAY-------RKELEKN---RSHVLQQ-----TQRLDTSQKRILE-------LESHLAKkdhlLLEQ 790
Cdd:pfam00038 164 rkldltsalaeIRAQYeeiaaknREEAEEWyqsKLEELQQaaarnGDALRSAKEEITElrrtiqsLEIELQS----LKKQ 239
|
250 260
....*....|....*....|....*
gi 2240436701 791 KKYLEDvklqargQLQAAESRYEAQ 815
Cdd:pfam00038 240 KASLER-------QLAETEERYELQ 257
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
603-732 |
1.28e-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: 48.40 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 603 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQ-IRQLQHDREEFynqsQELQTKledc 681
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVL-HAEdIKALQALREEL----NELKAE---- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436701 682 rnmIAELRIELKKANNKLSNSES--------VQQQMEFLNRQLLVLGEVNELYLEQLQN 732
Cdd:pfam07926 73 ---IAELKAEAESAKAELEESEEsweeqkkeLEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
594-731 |
1.83e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 594 NRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYNQLQEQRDTMVTKL---HSQIRQLQHDREEFY 668
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 669 NQSQ--------ELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 731
Cdd:COG3206 305 AQLQqeaqrilaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
619-835 |
1.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 619 KLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklhSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRIELKKANNK 698
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELE--------EELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 699 LSNSESVQQ------QMEFLNRQLLVLGEVnelyLEQLQNKHsDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKR 772
Cdd:COG4717 118 LEKLEKLLQllplyqELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436701 773 ilELESHLAKKDHLLLEQKKYLEDVKlQARGQLQAAESRYEAQKRitqvfELEILDLYGRLEK 835
Cdd:COG4717 193 --ELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLEN-----ELEAAALEERLKE 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
607-800 |
1.86e-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: 51.94 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 607 LEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIA 686
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIE----KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 687 ELRIELKKANNKLSNsesvqqqmefLNRQLLVLG-EVNEL--YLEQLQNKHSDTTKEVEMMKaayrKELEKNRSHVLQQT 763
Cdd:TIGR04523 430 RLKETIIKNNSEIKD----------LTNQDSVKElIIKNLdnTRESLETQLKVLSRSINKIK----QNLEQKQKELKSKE 495
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2240436701 764 QRLD--TSQKRILELE-SHLAKKDHLLLEQKKYLEDVKLQ 800
Cdd:TIGR04523 496 KELKklNEEKKELEEKvKDLTKKISSLKEKIEKLESEKKE 535
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
587-836 |
5.63e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 587 RQQHALRNRRLLRKVIKAA-----ALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ---RDTMVTKLHSQIR 658
Cdd:COG4372 39 ELDKLQEELEQLREELEQAreeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 659 QLQHDREEFYNQSQELQTKledcrnmIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQlqnkhsDTT 738
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQ-------IAELQSEIAEREEEL---KELEEQLESLQEELAALEQELQALSEA------EAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 739 KEVEMMKAAYRKELEKNRSHvlqQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRI 818
Cdd:COG4372 183 QALDELLKEANRNAEKEEEL---AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*...
gi 2240436701 819 TQVFELEILDLYGRLEKD 836
Cdd:COG4372 260 IEELELAILVEKDTEEEE 277
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
584-820 |
6.73e-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: 50.12 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 584 RFKRQQHALRNRRLLRKVIKAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQ---EQRDtmvtklhsqiRQL 660
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 661 QHDREEfynqSQELQTKLEDCRNMIAelriELKKANNKLSNSESVQQQMEFLNRQLLvlgevnELYLEQLQNKHSDTTKE 740
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEE----ERKRKKLELEKEKRDRKRAEEQRRKIL------EKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 741 VEMMKaayrKELEKNRSHVLQQTQRLDTSQKRILELEshlakkdhllLEQKKYLEDVKLQA---RGQLQAAESRYEAQKR 817
Cdd:pfam17380 515 RKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
...
gi 2240436701 818 ITQ 820
Cdd:pfam17380 581 IVE 583
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
596-826 |
6.75e-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: 49.53 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 596 RLLRKVIKAAA--------LEEHNAaMKDQLKLQEKDI-QMWKVSLQKEQARYN----QLQEQRDTMVTKLHSQIRQLQH 662
Cdd:pfam13868 9 RELNSKLLAAKcnkerdaqIAEKKR-IKAEEKEEERRLdEMMEEERERALEEEEekeeERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 663 DREEFYNQS-QELQTKLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEV 741
Cdd:pfam13868 88 KRQEEYEEKlQEREQMDEIVERIQEE---DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 742 EMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILElesHLAKKDHLLLeqKKYLEDVKLQARGQ-LQAAESRYEAQKRITQ 820
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQQEKAQD---EKAERDELRA--KLYQEEQERKERQKeREEAEKKARQRQELQQ 239
|
....*.
gi 2240436701 821 VFELEI 826
Cdd:pfam13868 240 AREEQI 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
655-836 |
7.77e-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: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 655 SQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 730
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 731 QNKHSDTTKEV-EMMKAAYRKELEKNRSHVLQQTQRLDTSqkRILELESHLAKKDHLLLEQ----KKYLEDVK---LQAR 802
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELAALRaelEAER 173
|
170 180 190
....*....|....*....|....*....|....
gi 2240436701 803 GQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 836
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
603-837 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 603 KAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYNQLQEQRDTMV-----------------TKLHSQIRQLQHDRE 665
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEeliaerretieekreraEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 666 EFYNQSQELQTKLEDCRNMIAEL---RIELKKANNKLSNSESVQ-------QQMEFLNRQLLVLGEVNELYLEQLQNKhS 735
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELnskLAELKERIESLERIRTLLaaiadaeDEIERLREKREALAELNDERRERLAEK-R 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 736 DTTKEVE-------MMKAAYRKE-----LEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------LLEQKKYLEDV 797
Cdd:PRK02224 634 ERKRELEaefdearIEEAREDKEraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerreaLENRVEALEAL 713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 798 KLQARgQLQAAESRYEAQKRITQVFELEIL-----------DLYGRLEKDG 837
Cdd:PRK02224 714 YDEAE-ELESMYGDLRAELRQRNVETLERMlnetfdlvyqnDAYSHIELDG 763
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
586-826 |
1.47e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 586 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM--VTKLHSQIRQLQHD 663
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 664 REEFYNQSQEL-------------------QTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNE 724
Cdd:TIGR00618 269 IEELRAQEAVLeetqerinrarkaaplaahIKAVTQIEQQAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 725 LyLEQLQNKHSDTTKEVEmmKAAYRKElEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQA--- 801
Cdd:TIGR00618 346 L-LQTLHSQEIHIRDAHE--VATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrd 421
|
250 260
....*....|....*....|....*.
gi 2240436701 802 -RGQLQAAESRYEAQKRITQVFELEI 826
Cdd:TIGR00618 422 lQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
599-835 |
1.72e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 599 RKVIKAaaLEEHNAAMKDQLKlqekDI-QMWKvSLQKEqarynqLQEQrdtmVTKLHSQIRQLQhdrEEFYN-------- 669
Cdd:PRK04778 197 REILDQ--LEEELAALEQIME----EIpELLK-ELQTE------LPDQ----LQELKAGYRELV---EEGYHldhldiek 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 670 QSQELQTKLEDCRNMIAELriELKKANNKLSNSESVQQQM------EFLNRQlLVLGEVNEL--YLEQLQNKHSDTTKEV 741
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilerEVKARK-YVEKNSDTLpdFLEHAKEQNKELKEEI 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 742 EMMKAAYR---KELEKNRSH----------VLQQTQRLDTSQKRILELESHLAK-KDHLL---LEQKKYLEDVKlqargQ 804
Cdd:PRK04778 334 DRVKQSYTlneSELESVRQLekqleslekqYDEITERIAEQEIAYSELQEELEEiLKQLEeieKEQEKLSEMLQ-----G 408
|
250 260 270
....*....|....*....|....*....|.
gi 2240436701 805 LQAAESryEAQKRItQVFELEILDLYGRLEK 835
Cdd:PRK04778 409 LRKDEL--EAREKL-ERYRNKLHEIKRYLEK 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
563-754 |
1.89e-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: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 563 SDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIKAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 638
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 639 YNQLQEQRDTMVTklhsQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIEL-------------------KKANNKL 699
Cdd:TIGR02168 889 LALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqerlseeysltleeaeALENKIE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436701 700 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN---KHSDTTKEVEMMKAAyRKELEK 754
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEElkeRYDFLTAQKEDLTEA-KETLEE 1021
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
583-725 |
2.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRNR-RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTM---VTKLHSQIR 658
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELeaeLAELQEELE 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436701 659 QL-QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNEL 725
Cdd:COG4717 181 ELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQLENELEAAALEERL 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
582-766 |
2.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 582 YERFKRQQHALRNRRllrkvikaAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQAR--YNQLQEQRDTMVTKLHsQIRQ 659
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALEaeLAELPERLEELEERLE-ELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 660 LQHDREEFYNQSQELQTKLEDCRNMI-AELRIELKKANNKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTT 738
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL---EELQQRLAELEEE-----------LEEAQEELEELE 226
|
170 180
....*....|....*....|....*...
gi 2240436701 739 KEVEMMKAAYRKELEKNRshvLQQTQRL 766
Cdd:COG4717 227 EELEQLENELEAAALEER---LKEARLL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
614-826 |
2.62e-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: 48.50 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 614 MKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQIRQLQHDREEFYNQSQELQTKLEDcrnmIAELRIELK 693
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIVKSYENELDPLKNRLKE----IEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 694 KANNKLSNSESVQQQMEFLNRQL-LVLGEV---NELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTS 769
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELeLKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLN----KERRLLNQE 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436701 770 QKRILELESHLAKKDHLLLEQ--KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEI 826
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
603-834 |
3.18e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 603 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCR 682
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 683 NMIAELRIELKKANNKLSNsesvqqqmeflNRQLLVLG-----------------------EVNEL--YLEQLQNKHSDT 737
Cdd:PRK02224 426 EREAELEATLRTARERVEE-----------AEALLEAGkcpecgqpvegsphvetieedreRVEELeaELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 738 TKEVEMMKAAyrKELEKNRSHVLQQ----TQRLDTSQKRILELESHLAKKDhlllEQKKYLEDVKLQARGQLQAAESRYE 813
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEERredlEELIAERRETIEEKRERAEELR----ERAAELEAEAEEKREAAAEAEEEAE 568
|
250 260
....*....|....*....|.
gi 2240436701 814 AQKRITQVFELEILDLYGRLE 834
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIE 589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
595-820 |
4.76e-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: 47.42 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 595 RRLLRKVIKAAALEEHNAAMKD----QLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEF 667
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvVEELTAKKMTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 668 YNQSQELQTK---LEDCRNMIAELRI-------ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN----- 732
Cdd:pfam15921 499 SDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtqlv 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 733 -KHSDTTKEVEMMKAAYRKELEKNRSHvLQQTQRL-DTSQKRILELESHLAKkdhllLEqkkyLEDVKLqargqLQAAES 810
Cdd:pfam15921 579 gQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILkDKKDAKIRELEARVSD-----LE----LEKVKL-----VNAGSE 643
|
250
....*....|
gi 2240436701 811 RYEAQKRITQ 820
Cdd:pfam15921 644 RLRAVKDIKQ 653
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
607-833 |
5.10e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 607 LEEHNAAMKDQLKLQEKDIQMWKvslQKEQARYNQLQEQRDTmvtklHSQIR-QLQHDREEFYNQSQELQTKL----EDC 681
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEK-----EMNLRdELESVREEFIQKGDEVKCKLdkseENA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 682 RNMIAELRIEL--------------KKANNKLSNSESVQQQMEFL-------NRQLlvlgEVNELYLEQLQNKHSDTTKE 740
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlkKQIENKNKNIEELHQENKALkkkgsaeNKQL----NAYEIKVNKLELELASAKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 741 VEMMKAAYRKELEKNR---SHVLQQTQRLDTSQKRILELESHLAKK-DH------LLLEQKKYLEDVKLQAR-GQLQAAE 809
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHkiaemvALMEKHKHQYDKIIEERdSELGLYK 731
|
250 260
....*....|....*....|....
gi 2240436701 810 SRYEAQKRITQVFELEILDLYGRL 833
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
583-829 |
6.28e-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: 46.45 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRNRRLLRKVIKAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYNQLQE------------------ 644
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAewkelekeeereederil 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 645 ----QRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKlsnSESVQQQMEFLNRQLLVLG 720
Cdd:pfam13868 159 eylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE---RKERQKEREEAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 721 EVNELYLEQLQNKhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDtsQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 800
Cdd:pfam13868 236 ELQQAREEQIELK--------ERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
250 260 270
....*....|....*....|....*....|...
gi 2240436701 801 ARGQ----LQAAESRYEAQKRITQVFELEILDL 829
Cdd:pfam13868 306 RAAEreeeLEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-783 |
9.07e-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: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 586 KRQQHALRNRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ---- 661
Cdd:COG4942 41 KELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 662 ----------HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgEVNELYLEQLQ 731
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL----EEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2240436701 732 NKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTSQKRILELESHLAKK 783
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
583-767 |
1.22e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRN----RRLLRKviKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQ-KEQARYNQlQEQ-RDTMVTKLHSQ 656
Cdd:PRK10929 65 ERAKQYQQVIDNfpklSAELRQ--QLNNERDEPRSVPPNMSTDALEQEILQVSSQlLEKSRQAQ-QEQdRAREISDSLSQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 657 IRQLQHD-REEFYNQSQELQTkledcrnmiaelrieLKKANNKLSNSESVQQQMEFLNRQLLVlgevNELYLEQLQnkhs 735
Cdd:PRK10929 142 LPQQQTEaRRQLNEIERRLQT---------------LGTPNTPLAQAQLTALQAESAALKALV----DELELAQLS---- 198
|
170 180 190
....*....|....*....|....*....|...
gi 2240436701 736 dttkevemmkAAYRKELEKNRSHVLQ-QTQRLD 767
Cdd:PRK10929 199 ----------ANNRQELARLRSELAKkRSQQLD 221
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
588-693 |
1.46e-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: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 588 QQHALRNRRLlrkVIKAAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYNQLQEQRDTMvtKLHSQ-----IRQLQH 662
Cdd:pfam13851 50 SEIQQENKRL---TEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 2240436701 663 DREEFYNQS----QELQTKLEdCRNMIAELRIELK 693
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
596-800 |
1.79e-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: 45.40 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 596 RLLRKVIKAAA----LEEHNAAMKDQLK-------LQEKDIQMWKVSLQKEQARYNQLQ---EQRDTMVTKLHSQIRQLQ 661
Cdd:TIGR04523 430 RLKETIIKNNSeikdLTNQDSVKELIIKnldntreSLETQLKVLSRSINKIKQNLEQKQkelKSKEKELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 662 hdreefyNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ--LQN 732
Cdd:TIGR04523 510 -------EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQksLKK 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 733 KHS---DTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 800
Cdd:TIGR04523 583 KQEekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
614-816 |
1.83e-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: 43.99 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 614 MKDQLKLQEKDIQMWKVSLQKeqarYNQLQEQRDTMVTKLHSQIrqlqhdreefynqsQELQTKLEDCRNMIAELRIELK 693
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQE----CEEIERRRQELASRYTQQT--------------AELQTQLLQKEKEQASLKKELQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 694 KANNKLSNSESVQQQMEFLnrqllvlgevnELYLEQLQNKHSDTTKEVEMM----KAAYRKEL---------EKNRSHVL 760
Cdd:pfam14988 72 ALRPFAKLKESQEREIQDL-----------EEEKEKVRAETAEKDREAHLQflkeKALLEKQLqelrilelgERATRELK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436701 761 QQTQRLDTSQKRILELESHLAKKDHLLLeQKKYLEdvKLQARGQLQAAESRYEAQK 816
Cdd:pfam14988 141 RKAQALKLAAKQALSEFCRSIKRENRQL-QKELLQ--LIQETQALEAIKSKLENRK 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
614-835 |
1.89e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 614 MKDQLKLQEKDIQmwkvsLQKEQAR--YNQLQEQRDT---MVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 688
Cdd:COG1340 2 KTDELSSSLEELE-----EKIEELReeIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 689 RIELKKANNKLSnseSVQQQMEFLNRQLLVLGEVNELyLEQLQnkhsdttKEVEmmkaayrkELEKNrshvlQQTQRLDT 768
Cdd:COG1340 77 KEERDELNEKLN---ELREELDELRKELAELNKAGGS-IDKLR-------KEIE--------RLEWR-----QQTEVLSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 769 SQ-----KRILELESHLAKKDHLLLEQKKYLEDVKlqargqlQAAESRYEAQ---KRITQVFE------LEILDLYGRLE 834
Cdd:COG1340 133 EEekelvEKIKELEKELEKAKKALEKNEKLKELRA-------ELKELRKEAEeihKKIKELAEeaqelhEEMIELYKEAD 205
|
.
gi 2240436701 835 K 835
Cdd:COG1340 206 E 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
615-823 |
2.57e-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: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 615 KDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEfyNQSQELQTKLEDCRNMIAELRielkK 694
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREIAELEAELERLD----A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 695 ANNKLsnsESVQQQmeflnrqllvlgevnelyLEQLQNKHSDTTKEVEMMKAAyRKELEKNRShvlQQTQRLDTSQKRIL 774
Cdd:COG4913 683 SSDDL---AALEEQ------------------LEELEAELEELEEELDELKGE-IGRLEKELE---QAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2240436701 775 ELESHLAKKDHLLLEQK-------KYLEDVKLQARGQLQAAESRYE-AQKRITQVFE 823
Cdd:COG4913 738 AAEDLARLELRALLEERfaaalgdAVERELRENLEERIDALRARLNrAEEELERAMR 794
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
595-778 |
3.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 595 RRLLRKVIK-AAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTklhsqirqLQHDREEFYNQSQE 673
Cdd:PRK03918 244 EKELESLEGsKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 674 LQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELY---------LEQLQNKHSDTTKE--VE 742
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEklEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436701 743 MMKAA--YRKELEKNRSHVLQQTQRLDTSQKR----ILELES 778
Cdd:PRK03918 392 ELEELekAKEEIEEEISKITARIGELKKEIKElkkaIEELKK 433
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
612-817 |
3.91e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 612 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEfynqsQElqtkledcRNMIAELRIE 691
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLEQQQAA-----QE--------RLLAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 692 LKKANNK-----LSNSESvqQQMEflnRQLLVLGEVNEL---YLEQLQNkhsdTTKEVemmkAAYRKELEKNRSH---VL 760
Cdd:PRK11637 134 FRQGEHTglqliLSGEES--QRGE---RILAYFGYLNQArqeTIAELKQ----TREEL----AAQKAELEEKQSQqktLL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436701 761 ----QQTQRLDTS----QKRILELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESryEAQKR 817
Cdd:PRK11637 201 yeqqAQQQKLEQArnerKKTLTGLESSLQKDQQQLSE----LRANESRLRDSIARAER--EAKAR 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
603-821 |
5.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 603 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYN--QLQEQRDTMVTK---LHSQIRQLQHDREEFYNQSQELQTK 677
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQlseLESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 678 LEDCRNMIAELrielkkannklSNSESVQQQMEFLNRQLLVLGEVNELYLE----------QLQNKHSDTTKEVEMMKAA 747
Cdd:COG3206 249 LGSGPDALPEL-----------LQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436701 748 YRKELEKNRSHVLQQTQRLDTSQKRILELESHlakkdhllleQKKYLEdvkLQArgQLQAAESRYEA-QKRITQV 821
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPEL----------EAELRR---LER--EVEVARELYESlLQRLEEA 377
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
685-813 |
6.15e-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: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 685 IAELRIELKKANNKLSNSES-VQQQMEFLNRQLLVLGEVNELYLEQLQnKHSDTTKEVEmmkaAYRKELEKNRSHVLQQT 763
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAqLQKLQEDLEKQAEIAREAQQNYERELV-LHAEDIKALQ----ALREELNELKAEIAELK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2240436701 764 QRLDTSQKRILELESHLAkkdhlllEQKKYLEDvklqargQLQAAESRYE 813
Cdd:pfam07926 78 AEAESAKAELEESEESWE-------EQKKELEK-------ELSELEKRIE 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
582-766 |
7.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 582 YERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKD----IQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQI 657
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 658 RQlqHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDT 737
Cdd:COG4717 423 EA--LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
170 180
....*....|....*....|....*....
gi 2240436701 738 TkeVEMMKAAYRKElekNRSHVLQQTQRL 766
Cdd:COG4717 501 L--LEEAREEYREE---RLPPVLERASEY 524
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
592-834 |
8.08e-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: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 592 LRNRRLLRKVIkaaaleehnaamkDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLhSQIRQLQ---HDRE--- 665
Cdd:COG3206 90 LKSRPVLERVV-------------DKLNLDEDPLG----EEASREAAIERLRKNLTVEPVKG-SNVIEISytsPDPElaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 666 -------EFYNQSQeLQTKLEDCRNMIAELRIELKKANNKLSNSEsvQQQMEFLNRQLLV-LGEVNELYLEQ---LQNKH 734
Cdd:COG3206 152 avanalaEAYLEQN-LELRREEARKALEFLEEQLPELRKELEEAE--AALEEFRQKNGLVdLSEEAKLLLQQlseLESQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 735 SDTTKEVEMMKAAY---RKELEKNRSHV--LQQTQRLDTSQKRILELESHLAKkdhlllEQKKYLE---DVKlQARGQLQ 806
Cdd:COG3206 229 AEARAELAEAEARLaalRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAE------LSARYTPnhpDVI-ALRAQIA 301
|
250 260
....*....|....*....|....*....
gi 2240436701 807 AAESRYEAQ-KRITQVFELEILDLYGRLE 834
Cdd:COG3206 302 ALRAQLQQEaQRILASLEAELEALQAREA 330
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
598-814 |
1.22e-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: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 598 LRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ-RDTMVTKlhsqirqlqHDREEfynqsqelqt 676
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlREVENEK---------NDKDK---------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 677 KLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQNKHSDTTKEvEMMKAayrkeLEKNR 756
Cdd:pfam10174 601 KIAELESLTLR---QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-ELMGA-----LEKTR 668
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 757 SHVLQQTQRLDTSQKRILELESHLAKkdhLLLEQKKYLEDV---KLQArgqLQAAESRYEA 814
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
598-780 |
1.25e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 598 LRKVIKAAALEE-HNAAMKDQL-KLQEKDIQMWKvsLQKEQARYNQLQEQRDTMVTKLHSQIRQLQhDREEFYNQSQELQ 675
Cdd:PRK01156 269 LEKNNYYKELEErHMKIINDPVyKNRNYINDYFK--YKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 676 TKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTTKEVEMMKAAYRKELEKN 755
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN-----------IERMSAFISEILKIQEIDPDAIKKELNEI 414
|
170 180
....*....|....*....|....*
gi 2240436701 756 RSHVLQQTQRLDTSQKRILELESHL 780
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENL 439
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
588-765 |
1.29e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 588 QQHALRNRRLLRKVIKaaaLEEHNAAMKDqLKLQEKDIQMWKVSLQKEQARYN---------QLQEQRDTMVTKLHSQIR 658
Cdd:PHA02562 234 AEIEELTDELLNLVMD---IEDPSAALNK-LNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 659 QLQHDREEFYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSesvQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTT 738
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTN---KQSLITLVDKAKKV----KAAIEELQAEFVDNA 378
|
170 180
....*....|....*....|....*..
gi 2240436701 739 KEVEMMKAAYRKELEKNRSHVLQQTQR 765
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
604-695 |
1.81e-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: 39.87 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 604 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNqlQEQRDTMVTKLHSQIRQLQHDREEFynqSQELQTKLedcRN 683
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|..
gi 2240436701 684 MIAELRIELKKA 695
Cdd:smart00935 92 ELQKILDKINKA 103
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
586-773 |
1.87e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 586 KRQQHALRNRRLlRKVIKAA-----ALEEHNAAMKDQLKLQEKDIqMWKVSLQKEQARYNQLQeqrdtmvtklhSQIRQL 660
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDApaelrELRQELAALQAKAEAAPKEI-LASLSLEELEQRLLQTS-----------AQLQEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 661 QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQ------QQMEFLNRQLLVLGEVNELYLEQLQNkh 734
Cdd:pfam12795 98 QNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGeplseaQRWALQAELAALKAQIDMLEQELLSN-- 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2240436701 735 sdttkevEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRI 773
Cdd:pfam12795 176 -------NNRQDLLKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
584-816 |
1.93e-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: 42.34 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 584 RFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHD 663
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 664 REEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgevnelyLEQLQNKHSDTTKEVEM 743
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----------ENKIQDGKDDYLKQKET 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 744 MKAAYRKELEKNRSH-------VLQQTQRLDTS--QKRILELESHLAKKDHLLLEQKKYLEDvKLQARGQLQAAESRYEA 814
Cdd:TIGR00606 978 ELNTVNAQLEECEKHqekinedMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQ-HLKEMGQMQVLQMKQEH 1056
|
..
gi 2240436701 815 QK 816
Cdd:TIGR00606 1057 QK 1058
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
614-835 |
2.26e-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: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 614 MKDQLKLQEKDIQMW---KVSLQKEQARYNQLQEQRDTmvtklhsqirqlqhdreeFYNQSQELQTKLEDCRNMIAELRI 690
Cdd:pfam05622 150 LRRQVKLLEERNAEYmqrTLQLEEELKKANALRGQLET------------------YKRQVQELHGKLSEESKKADKLEF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 691 ELKKANNKLsnsESVQQQMEFLNRQLLVLGEVN-ELYLEQLQNKH----------SDTTKEV---EMMKAAYRKELEK-- 754
Cdd:pfam05622 212 EYKKLEEKL---EALQKEKERLIIERDTLRETNeELRCAQLQQAElsqadallspSSDPGDNlaaEIMPAEIREKLIRlq 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 755 --NRSHVLQQT-----------QRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQV 821
Cdd:pfam05622 289 heNKMLRLGQEgsyrerltelqQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEH 368
|
250
....*....|....
gi 2240436701 822 FElEILDLYGRLEK 835
Cdd:pfam05622 369 LE-KLHEAQSELQK 381
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
583-825 |
3.05e-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: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRNRRLLRKVIKAAalEEHNaAMKDQLKLQEKDIQMWKVSLQKEQaRYNQLQEQRDTMVTKLHSQIRQLQH 662
Cdd:pfam05557 330 LNKKLKRHKALVRRLQRRVLLLT--KERD-GYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 663 DREEFYNQSQELQTkledcrnmiAELRIELKKANNKLSNSESVQQQMEFLNRqllvlgEVNELYLEQLQNKHSDTTKEVE 742
Cdd:pfam05557 406 AEEELGGYKQQAQT---------LERELQALRQQESLADPSYSKEEVDSLRR------KLETLELERQRLREQKNELEME 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 743 MMKAAYRKELEKNRSHVLQ---------------QTQRLD---TSQKRILE-LESHLAKKDHLLLEQKKYLEDVKLQARG 803
Cdd:pfam05557 471 LERRCLQGDYDPKKTKVLHlsmnpaaeayqqrknQLEKLQaeiERLKRLLKkLEDDLEQVLRLPETTSTMNFKEVLDLRK 550
|
250 260
....*....|....*....|..
gi 2240436701 804 QLQAAESRYEAQKRITQVFELE 825
Cdd:pfam05557 551 ELESAELKNQRLKEVFQAKIQE 572
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
617-791 |
3.88e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 617 QLKLQEKDIQMWKVSLQK---EQARYNQLQEQRDtmVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELK 693
Cdd:COG5022 922 NLEFKTELIARLKKLLNNidlEEGPSIEYVKLPE--LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 694 KANNKLSNSESVQ---QQMEFLNRQLLVLGEVNELYLEQ---------LQNKHSDTTKEVEMMKA-----AYRKELEKNR 756
Cdd:COG5022 1000 ELAELSKQYGALQestKQLKELPVEVAELQSASKIISSEstelsilkpLQKLKGLLLLENNQLQArykalKLRRENSLLD 1079
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436701 757 SHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQK 791
Cdd:COG5022 1080 DKQLYQLESTENLLKTINVKDLEVTNRNLVKPANV 1114
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
636-801 |
3.89e-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: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 636 QARYNQLQEQRDTMVTKLHSqirqLQHDREEFYNQSQELQTKLEDCRNMIAEL--RIE--LKKANNKLSNSESVQQQMef 711
Cdd:pfam10168 560 QKRVKLLKLQKEQQLQELQS----LEEERKSLSERAEKLAEKYEEIKDKQEKLmrRCKkvLQRLNSQLPVLSDAEREM-- 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 712 lNRQLLVLGEVnelyLEQLQNkhsdTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRIL-ELESHLAKKdhlLLEQ 790
Cdd:pfam10168 634 -KKELETINEQ----LKHLAN----AIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIkEILKQLGSE---IDEL 701
|
170
....*....|.
gi 2240436701 791 KKYLEDVKLQA 801
Cdd:pfam10168 702 IKQVKDINKHV 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
632-836 |
4.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 632 LQKEQARYNQLQEQRdTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 711
Cdd:PRK03918 157 LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 712 LnRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVlQQTQRLDTSQKRILELESHLAKKDHLLLEQK 791
Cdd:PRK03918 236 L-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2240436701 792 KYLEDVKLQARG---QLQAAESRYEAQKRITQVFElEILDLYGRLEKD 836
Cdd:PRK03918 314 KRLSRLEEEINGieeRIKELEEKEERLEELKKKLK-ELEKRLEELEER 360
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
607-797 |
4.37e-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: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 607 LEEHNAAMKDQLKLQEKDIQMwkvSLQKE----QARYNQLQEQrdtmvTKLHSQ-IRQLQHDREEFYNQSQELQTKLEDC 681
Cdd:pfam05622 287 LQHENKMLRLGQEGSYRERLT---ELQQLledaNRRKNELETQ-----NRLANQrILELQQQVEELQKALQEQGSKAEDS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 682 RNMIAELRIELKKANNKLSNSESVQQQMEflnrqllvlgevnELYLEQLQNKHSDTT--------KEVEM--MKAAYRKE 751
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIE-------------ELEPKQDSNLAQKIDelqealrkKDEDMkaMEERYKKY 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2240436701 752 LEKNRSHVlqqtQRLDTSQKRILELESHLAKKDhlLLEQKKYLEDV 797
Cdd:pfam05622 426 VEKAKSVI----KTLDPKQNPASPPEIQALKNQ--LLEKDKKIEHL 465
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
653-805 |
4.38e-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: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 653 LHSQIRQLQHDREEFYNQSQELQTKLEDCRnmiaelrielKKANNKLSNSESVQQQMEFLN-------RQLLVLgevnEL 725
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQ----------QKESKFLENLASLKHENDNLSsmlnrkeRRLKDL----ED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 726 YLEQLQNKHsdttKEVEMMKAAYRKELEKNRSH---VLQQTQRLDTSQKRIleLESHLAKKDHLLLE---QKKYLEDVKL 799
Cdd:pfam17078 74 QLSELKNSY----EELTESNKQLKKRLENSSASettLEAELERLQIQYDAL--VDSQNEYKDHYQQEintLQESLEDLKL 147
|
....*.
gi 2240436701 800 QARGQL 805
Cdd:pfam17078 148 ENEKQL 153
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
630-817 |
6.33e-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: 40.32 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 630 VSLQKEQARYNQLQEQRDTMvtklhsqiRQLQ--HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANN-----KLSNS 702
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEM--------RRLEveRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEeirlrKQRLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 703 ESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHsdttkevemmkaayRKELEKNRSHVLQQTQRLDTSQKRILELESHLAK 782
Cdd:pfam15709 398 EERQRQEEEERKQRLQLQAAQERARQQQEEFR--------------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAE 463
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436701 783 KDHLLLEQKKYlEDVKLQARGQLQAAESRYEAQKR 817
Cdd:pfam15709 464 EQKRLMEMAEE-ERLEYQRQKQEAEEKARLEAEER 497
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
700-817 |
7.61e-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: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 700 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN--KHSDTTKEVEMMKAAYRKELEKNRSHVLQQ----TQRLDTSQKRI 773
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQELAILEAENskAEVETLKAEIEEMAQNLRDLELDLVTLRSEkenlTKELQKKQERV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2240436701 774 LELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESRYEAQKR 817
Cdd:pfam10473 97 SELESLNSSLENLLEE----KEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
562-835 |
7.77e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 562 PSDEIRTLRDQLLLLHNQLLYERFKRQQH-----ALRNR-RLLRKVIKAAAL--EEHNAAMKDQLKLQEKDIQMWKVSLQ 633
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQrsqleQAKEGlSALNRLLPRLNLlaDETLADRVEEIREQLDEAEEAKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 634 KEQARYNQLqeqrDTMVTKLHS---QIRQLQHDreefYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSESVQqqme 710
Cdd:PRK04863 915 QHGNALAQL----EPIVSVLQSdpeQFEQLKQD----YQQAQQTQRDA----KQQAFALTEVVQRRAHFSYEDAAE---- 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 711 flnrqllVLGEVNELyLEQLQNKHsdttKEVEMMKAAYRKELEknrshvlQQTQRLDTSQKRILELESHLAKKDHLLLEQ 790
Cdd:PRK04863 979 -------MLAKNSDL-NEKLRQRL----EQAEQERTRAREQLR-------QAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 791 KKYLEDVKLQA-----------RGQLQAAES-----RYEAQKRITqVFELEILDLYGRLEK 835
Cdd:PRK04863 1040 KQELQDLGVPAdsgaeerararRDELHARLSanrsrRNQLEKQLT-FCEAEMDNLTKKLRK 1099
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-754 |
8.66e-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: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 583 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQH 662
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 663 DREEFYNQSQELQTKLEdcrnmIAELRIELKKANNKLSNsesvqqqmeflnrqllvLGEVNELYLE---QLQNKHSDTTK 739
Cdd:COG1196 745 EELLEEEALEELPEPPD-----LEELERELERLEREIEA-----------------LGPVNLLAIEeyeELEERYDFLSE 802
|
170
....*....|....*
gi 2240436701 740 EVEMMKAAyRKELEK 754
Cdd:COG1196 803 QREDLEEA-RETLEE 816
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
604-835 |
9.45e-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: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 604 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQaryNQLQEQRDTMvtklhSQIRQ-LQHDREEFYNQSQELQTKLEDC- 681
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESEN---AELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESe 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 682 --RNMIAE----LRIELKKANNKLSNSES----VQQQMEFLNRQllvLGEVNELYLEQLQNKHSDTTKevemmkaayRKE 751
Cdd:pfam01576 426 rqRAELAEklskLQSELESVSSLLNEAEGknikLSKDVSSLESQ---LQDTQELLQEETRQKLNLSTR---------LRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 752 LEKNRSHVLQQTQRLDTSQKRileLESHLAKKDHLLLEQKKYLEDVKlqarGQLQAAEsryEAQKRITQVFELEILDL-- 829
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRN---VERQLSTLQAQLSDMKKKLEEDA----GTLEALE---EGKKRLQRELEALTQQLee 563
|
250
....*....|
gi 2240436701 830 ----YGRLEK 835
Cdd:pfam01576 564 kaaaYDKLEK 573
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
624-748 |
9.68e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436701 624 DIQMWKVSLQKEQARYNQLQEQRdtmvTKLHSQIRQLQHDRE-EFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNS 702
Cdd:PRK10636 514 DYQQWLSDVQKQENQTDEAPKEN----NANSAQARKDQKRREaELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDS 589
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2240436701 703 ESVQQQ-----MEFLNRQLLVLGEVNELYLEQLqnkhsDTTKEVEMMKAAY 748
Cdd:PRK10636 590 ELYDQSrkaelTACLQQQASAKSGLEECEMAWL-----EAQEQLEQMLLEG 635
|
|
| |
