|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
7-718 |
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: 1031.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 7 VGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATR 86
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 87 LSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCL 166
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 167 KKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRR 246
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 247 WKRLETHDVVIECAKISLDPTEASYEDGYSVShqisarfphrSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQL 326
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSS----------AADPTASPYTDQQSSYGSSTSTPSSTPRLQLSSSSGTS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 327 PQTLSSPSTRLITEPPqaTLWSPSMVCGMTTPPTSPGNVP-------PDLSHPYSKVFGTTG--GKGTPLG--TPATSPP 395
Cdd:pfam04388 311 PPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPttpselsPSSSHLSSRGSSPPEaaGEATPETtpAKDSPYL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 396 PAPLCHSDDYVHISLP--QATVTPPRKEERMDSARPCLHRQHHL-LNDRGSEEPPGSKGSVTLSDLPGFLGDLA-SEEDS 471
Cdd:pfam04388 389 KQPPPLSDSHVHRALPasSQPSSPPRKDGRSQSSFPPLSKQAPTnPNSRGLLEPPGDKSSVTLSELPDFIKDLAlSSEDS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 472 IEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYR--DSLPGSQRK--------THSAASSSQGASVNPE-----PLH 536
Cdd:pfam04388 469 VEGAEEEAAISQELSEITTEKNETDCSRGGLDMPFSRtmESLAGSQRSrnriasycSSTSQSDSHGPATTPEskpsaLAE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 537 SSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAH 616
Cdd:pfam04388 549 DGLRRTKSCSFKQSFTPIEQPIESSDDCPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFDLALPKTAS 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 617 HFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLL 696
Cdd:pfam04388 629 LFVGRKTAELLKKAKGNSEEDCVSSTSPLEVLDRYIQQGIDAHSKELKRLPLPSKSADWTHFGGSAPSDELTTLRDQLLL 708
|
730 740
....*....|....*....|..
gi 2240436797 697 LHNQLLYERFKRQQHALRNRRL 718
Cdd:pfam04388 709 LHNQLLYERYKREQHAERNRRL 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
704-941 |
1.84e-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: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQ 780
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELeleLEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 781 LQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELyLEQLQNKHSDTTK 860
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELEEAEEELEE-AEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 861 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRIT 940
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
.
gi 2240436797 941 Q 941
Cdd:COG1196 449 E 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-946 |
1.85e-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: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 685 DEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIqmwKVSLQKEQARYNQLQ 764
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 765 EQRDT---MVTKLHSQIRQLqhdREEFynqsQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNrqllvlG 841
Cdd:TIGR02168 796 EELKAlreALDELRAELTLL---NEEA----ANLRERLESLERRIAATERRLEDLEEQI---EELSEDIESLA------A 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 842 EVNELylEQLQNKHSDTTKEVEMMKAAYRKELEKNRShvlqqtqRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLq 921
Cdd:TIGR02168 860 EIEEL--EELIEELESELEALLNERASLEEALALLRS-------ELEELSEELRELESKRSELRRELEELREKLAQLEL- 929
|
250 260
....*....|....*....|....*.
gi 2240436797 922 argQLQAAESRY-EAQKRITQVFELE 946
Cdd:TIGR02168 930 ---RLEGLEVRIdNLQERLSEEYSLT 952
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-956 |
2.73e-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: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRN----------------RRLLRKVIKAAA--LEEHNAAMKD-QLKLQEKDIQMWKVS--LQKEQARYNQ 762
Cdd:TIGR02168 213 ERYKELKAELRElelallvlrleelreeLEELQEELKEAEeeLEELTAELQElEEKLEELRLEVSELEeeIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 763 LQEQRDTMVTK----------LHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 832
Cdd:TIGR02168 293 LANEISRLEQQkqilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 833 LNRQLlvlgevnELYLEQLQNKHSDTTKEVemmkAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKD-HLLLEQ 911
Cdd:TIGR02168 373 RLEEL-------EEQLETLRSKVAQLELQI----ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAE 441
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2240436797 912 KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 956
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
753-946 |
6.19e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 62.61 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 753 LQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEF 832
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL---EQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 833 LNRQLLVLGEVNELY---LEQLQNKHSDTTKEVEMMKAAyRKELEKNRSHVLQQTQRLDTS----QKRILELESHLAKKD 905
Cdd:COG4372 85 LNEQLQAAQAELAQAqeeLESLQEEAEELQEELEELQKE-RQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLESLQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436797 906 HLLLEQKKYLEDVKLQ-ARGQLQAAESryEAQKRITQVFELE 946
Cdd:COG4372 164 EELAALEQELQALSEAeAEQALDELLK--EANRNAEKEEELA 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
707-956 |
9.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 707 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDRE 786
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----RLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 787 EFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLvlgEVNELYLEQLQNKHSDTTKEVEMMK 866
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALL---EAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 867 AA--YRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFE 944
Cdd:COG1196 394 AAaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250
....*....|..
gi 2240436797 945 LEILDLYGRLEK 956
Cdd:COG1196 474 LLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-944 |
1.21e-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: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 703 YERFKRQQHAlrNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHS------ 776
Cdd:TIGR02168 277 SELEEEIEEL--QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeele 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 777 ----QIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESvqqQMEFLNRQLLVLGEVNElylEQLQ 852
Cdd:TIGR02168 355 sleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEIE---ELLK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 853 NKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLakkdhllleqkkyledvkLQARGQLQAAESR 932
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL------------------DAAERELAQLQAR 490
|
250
....*....|..
gi 2240436797 933 YEAQKRITQVFE 944
Cdd:TIGR02168 491 LDSLERLQENLE 502
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
733-954 |
1.28e-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: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 733 AAMKDQLKLqekdiqmwkVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 809
Cdd:COG1579 1 AMPEDLRAL---------LDLQELDSELDRLEHRLKELpaeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 810 RIELKKANNKLSNSESvqqqmeflNRQllvlgevnelyLEQLQnkhsdttKEVEMMKAAyRKELEKnrsHVLQQTQRLDT 889
Cdd:COG1579 72 EARIKKYEEQLGNVRN--------NKE-----------YEALQ-------KEIESLKRR-ISDLED---EILELMERIEE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436797 890 SQKRILELESHLAKKDHLLLEQKKYLEdvklQARGQLQAAESRYEAQ-KRITQVFELEILDLYGRL 954
Cdd:COG1579 122 LEEELAELEAELAELEAELEEKKAELD----EELAELEAELEELEAErEELAAKIPPELLALYERI 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
714-912 |
6.18e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 714 RNRRLLRKVIKaaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQL-QHDR--EEFYN 790
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeQNNKkiKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 791 QSQELQTKLEDCRN-----MIAELRIELKKANNKLSNSES----VQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTTKE 861
Cdd:TIGR04523 289 QLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNqisqNNKIISQLNEQISQL----KKELTNSESENSEKQRE 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 862 VEMMKAAYRKELEKNRSHvLQQTQRLdTSQKRILELESHLAKKDHLLLEQK 912
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSY-KQEIKNL-ESQINDLESKIQNQEKLNQQKDEQ 413
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
679-946 |
1.13e-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: 59.70 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 679 GGS--PPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKvikaAALEEHNAAMKD---QLKLQEKDIQMwkvsL 753
Cdd:TIGR02169 657 GGSraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE----NRLDELSQELSDasrKIGEIEKEIEQ----L 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 754 QKEQARYNQLQEQrdtmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNS--ESVQQQME 831
Cdd:TIGR02169 729 EQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 832 FLNRQLlvlgEVNELYLEQLQNKHSDTTKEVEMM------KAAYRKELEKNRSHVlqqTQRLDTSQKRILELESHLAKKD 905
Cdd:TIGR02169 802 KLEEEV----SRIEARLREIEQKLNRLTLEKEYLekeiqeLQEQRIDLKEQIKSI---EKEIENLNGKKEELEEELEELE 874
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2240436797 906 HLLLEQKKYLEDVK---LQARGQLQAAESRYEAQKriTQVFELE 946
Cdd:TIGR02169 875 AALRDLESRLGDLKkerDELEAQLRELERKIEELE--AQIEKKR 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
724-945 |
1.22e-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: 59.69 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 724 KAAALEEHNAamkdQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCR 803
Cdd:TIGR02168 675 RRREIEELEE----KIEELEEKIA----ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 804 NMIAELRIELKKANNKlsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQ 883
Cdd:TIGR02168 747 ERIAQLSKELTELEAE----IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436797 884 TQRLDTSQKRILELESHLAKkdhlLLEQKKYLEDVKLQARGQL-QAAESRYEAQKRITQVFEL 945
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIeELEELIEELESELEALLNE 881
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
733-956 |
7.41e-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: 55.93 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 733 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDtmvtKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIE 812
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 813 LKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAaYRKELEKNRSHVLQQTQRLDTSQK 892
Cdd:COG4942 92 IAELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2240436797 893 RILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEK 956
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
743-941 |
1.05e-07 |
|
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: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 743 EKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKK---- 815
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 816 ------ANNKLS---NSESVQqqmEFLNRQllvlgevneLYLEQLQNKHSDTTKEVemmKAAyRKELEKNRSHVLQQTQR 886
Cdd:COG3883 95 lyrsggSVSYLDvllGSESFS---DFLDRL---------SALSKIADADADLLEEL---KAD-KAELEAKKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2240436797 887 LDTSQKrilELESHLAKKDHLLLEQKKYLEDVKLQaRGQLQAAESRYEAQKRITQ 941
Cdd:COG3883 159 LEALKA---ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
737-909 |
1.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 737 DQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLH---SQIRQLQHDRE--EFYNQSQELQTKLEDCRNMIAELRI 811
Cdd:COG4717 71 KELKELEEELK----EAEEKEEEYAELQEELEELEEELEeleAELEELREELEklEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 812 ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKH----SDTTKEVEMM---KAAYRKELEKNRSHVLQQT 884
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELqqrLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*..
gi 2240436797 885 QRLD--TSQKRILELESHLAKKDHLLL 909
Cdd:COG4717 227 EELEqlENELEAAALEERLKEARLLLL 253
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
715-936 |
4.90e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 53.00 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 715 NRRLLRKVIKAAALEEHNAAMKDQLK-LQEKdiQMWKVSlQKEQARYNQLQEQRDTMVT------KLHSQIRQLQHDREE 787
Cdd:pfam00038 10 NDRLASYIDKVRFLEQQNKLLETKISeLRQK--KGAEPS-RLYSLYEKEIEDLRRQLDTltveraRLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 788 FYNQSQELQTKLEDCRNMIAELRIELKKANnkLSNSEsVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEM--- 864
Cdd:pfam00038 87 FRQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVD-LEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 865 -----------MKAAY-------RKELEKN---RSHVLQQ-----TQRLDTSQKRILE-------LESHLAKkdhlLLEQ 911
Cdd:pfam00038 164 rkldltsalaeIRAQYeeiaaknREEAEEWyqsKLEELQQaaarnGDALRSAKEEITElrrtiqsLEIELQS----LKKQ 239
|
250 260
....*....|....*....|....*
gi 2240436797 912 KKYLEDvklqargQLQAAESRYEAQ 936
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 ... |
724-853 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 724 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQ-IRQLQHDREEFynqsQELQTKledc 802
Cdd:pfam07926 2 ELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVL-HAEdIKALQALREEL----NELKAE---- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436797 803 rnmIAELRIELKKANNKLSNSES--------VQQQMEFLNRQLLVLGEVNELYLEQLQN 853
Cdd:pfam07926 73 ---IAELKAEAESAKAELEESEEsweeqkkeLEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
728-921 |
2.10e-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: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 728 LEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIA 807
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIE----KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 808 ELRIELKKANNKLSNsesvqqqmefLNRQLLVLG-EVNEL--YLEQLQNKHSDTTKEVEMMKaayrKELEKNRSHVLQQT 884
Cdd:TIGR04523 430 RLKETIIKNNSEIKD----------LTNQDSVKElIIKNLdnTRESLETQLKVLSRSINKIK----QNLEQKQKELKSKE 495
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2240436797 885 QRLD--TSQKRILELE-SHLAKKDHLLLEQKKYLEDVKLQ 921
Cdd:TIGR04523 496 KELKklNEEKKELEEKvKDLTKKISSLKEKIEKLESEKKE 535
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
705-941 |
2.42e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 705 RFKRQQHALRNRRLLRKVIKAAALEEHNaamkdQLKLQEKDIQMWKVSLQKEQARYNQLQ---EQRDtmvtklhsqiRQL 781
Cdd:pfam17380 384 QMERQQKNERVRQELEAARKVKILEEER-----QRKIQQQKVEMEQIRAEQEEARQREVRrleEERA----------REM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 782 QHDREEfynqSQELQTKLEDCRNMIAelriELKKANNKLSNSESVQQQMEFLNRQLLvlgevnELYLEQLQNKHSDTTKE 861
Cdd:pfam17380 449 ERVRLE----EQERQQQVERLRQQEE----ERKRKKLELEKEKRDRKRAEEQRRKIL------EKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 862 VEMMKaayrKELEKNRSHVLQQTQRLDTSQKRILELEshlakkdhllLEQKKYLEDVKLQA---RGQLQAAESRYEAQKR 938
Cdd:pfam17380 515 RKLLE----KEMEERQKAIYEEERRREAEEERRKQQE----------MEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
...
gi 2240436797 939 ITQ 941
Cdd:pfam17380 581 IVE 583
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-956 |
2.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 740 KLQEKDIQMWKVSLQKEQARYNQLQEQRdtmvtklhSQIRQLQHDREEFynqsQELQTKLEDCRNMIAELRIELKKANNK 819
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELE--------EELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 820 LSNSESVQQ------QMEFLNRQLLVLGEVnelyLEQLQNKHsDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKR 893
Cdd:COG4717 118 LEKLEKLLQllplyqELEALEAELAELPER----LEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2240436797 894 ilELESHLAKKDHLLLEQKKYLEDVKlQARGQLQAAESRYEAQKRitqvfELEILDLYGRLEK 956
Cdd:COG4717 193 --ELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLEN-----ELEAAALEERLKE 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
717-947 |
3.52e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 717 RLLRKVIKAAA--------LEEHNAaMKDQLKLQEKDI-QMWKVSLQKEQARYN----QLQEQRDTMVTKLHSQIRQLQH 783
Cdd:pfam13868 9 RELNSKLLAAKcnkerdaqIAEKKR-IKAEEKEEERRLdEMMEEERERALEEEEekeeERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 784 DREEFYNQS-QELQTKLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVN--ELYLEQLQNKhsDTTK 860
Cdd:pfam13868 88 KRQEEYEEKlQEREQMDEIVERIQEE---DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEkeEEREEDERIL--EYLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 861 EVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILElesHLAKKDHLLLeqKKYLEDVKLQARGQ-LQAAESRYEAQKRI 939
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---EKAERDELRA--KLYQEEQERKERQKeREEAEKKARQRQEL 237
|
....*...
gi 2240436797 940 TQVFELEI 947
Cdd:pfam13868 238 QQAREEQI 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
715-852 |
3.59e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 715 NRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVS--LQKEQARYNQLQEQRDTMVTKL---HSQIRQLQHDREEFY 789
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYtpnHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 790 NQSQ--------ELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQ 852
Cdd:COG3206 305 AQLQqeaqrilaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
708-957 |
6.21e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 708 RQQHALRNRRLLRKVIKAA-----ALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ---RDTMVTKLHSQIR 779
Cdd:COG4372 39 ELDKLQEELEQLREELEQAreeleQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 780 QLQHDREEFYNQSQELQTKledcrnmIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNELYLEQlqnkhsDTT 859
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQ-------IAELQSEIAEREEEL---KELEEQLESLQEELAALEQELQALSEA------EAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 860 KEVEMMKAAYRKELEKNRSHvlqQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRI 939
Cdd:COG4372 183 QALDELLKEANRNAEKEEEL---AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250
....*....|....*...
gi 2240436797 940 TQVFELEILDLYGRLEKD 957
Cdd:COG4372 260 IEELELAILVEKDTEEEE 277
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
724-958 |
7.90e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 724 KAAALEEHNAAMKDQLKLQEKDIQMWKvSLQKEQARYNQLQEQRDTMV-----------------TKLHSQIRQLQHDRE 786
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEeliaerretieekreraEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 787 EFYNQSQELQTKLEDCRNMIAEL---RIELKKANNKLSNSESVQ-------QQMEFLNRQLLVLGEVNELYLEQLQNKhS 856
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELnskLAELKERIESLERIRTLLaaiadaeDEIERLREKREALAELNDERRERLAEK-R 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 857 DTTKEVE-------MMKAAYRKE-----LEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHL------LLEQKKYLEDV 918
Cdd:PRK02224 634 ERKRELEaefdearIEEAREDKEraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerreaLENRVEALEAL 713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 919 KLQARgQLQAAESRYEAQKRITQVFELEIL-----------DLYGRLEKDG 958
Cdd:PRK02224 714 YDEAE-ELESMYGDLRAELRQRNVETLERMlnetfdlvyqnDAYSHIELDG 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
776-957 |
1.01e-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: 49.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 776 SQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSE----SVQQQMEFLNRQLlvlgEVNELYLEQL 851
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAEL----AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 852 QNKHSDTTKEV-EMMKAAYRKELEKNRSHVLQQTQRLDTSqkRILELESHLAKKDHLLLEQ----KKYLEDVK---LQAR 923
Cdd:COG4942 96 RAELEAQKEELaELLRALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEElradLAELAALRaelEAER 173
|
170 180 190
....*....|....*....|....*....|....
gi 2240436797 924 GQLQAAESRYEAQKRITQVFELEILDLYGRLEKD 957
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
707-947 |
1.41e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 707 KRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM--VTKLHSQIRQLQHD 784
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 785 REEFYNQSQEL-------------------QTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNE 845
Cdd:TIGR00618 269 IEELRAQEAVLeetqerinrarkaaplaahIKAVTQIEQQAQRIHTELQSKMRSR---AKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 846 LyLEQLQNKHSDTTKEVEmmKAAYRKElEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQA--- 922
Cdd:TIGR00618 346 L-LQTLHSQEIHIRDAHE--VATSIRE-ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrd 421
|
250 260
....*....|....*....|....*.
gi 2240436797 923 -RGQLQAAESRYEAQKRITQVFELEI 947
Cdd:TIGR00618 422 lQGQLAHAKKQQELQQRYAELCAAAI 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
684-875 |
1.99e-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: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 684 SDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLL-RKVIKAAALEEHNAAMKDQLKLQEK---DIQMWKVSLQKEQAR 759
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEA 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 760 YNQLQEQRDTMVTklhsQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIEL-------------------KKANNKL 820
Cdd:TIGR02168 889 LALLRSELEELSE----ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqerlseeysltleeaeALENKIE 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436797 821 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN---KHSDTTKEVEMMKAAyRKELEK 875
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEElkeRYDFLTAQKEDLTEA-KETLEE 1021
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
720-956 |
2.00e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 720 RKVIKAaaLEEHNAAMKDQLKlqekDI-QMWKvSLQKEqarynqLQEQrdtmVTKLHSQIRQLQhdrEEFYN-------- 790
Cdd:PRK04778 197 REILDQ--LEEELAALEQIME----EIpELLK-ELQTE------LPDQ----LQELKAGYRELV---EEGYHldhldiek 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 791 QSQELQTKLEDCRNMIAELriELKKANNKLSNSESVQQQM------EFLNRQlLVLGEVNEL--YLEQLQNKHSDTTKEV 862
Cdd:PRK04778 257 EIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQLydilerEVKARK-YVEKNSDTLpdFLEHAKEQNKELKEEI 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 863 EMMKAAYR---KELEKNRSH----------VLQQTQRLDTSQKRILELESHLAK-KDHLL---LEQKKYLEDVKlqargQ 925
Cdd:PRK04778 334 DRVKQSYTlneSELESVRQLekqleslekqYDEITERIAEQEIAYSELQEELEEiLKQLEeieKEQEKLSEMLQ-----G 408
|
250 260 270
....*....|....*....|....*....|.
gi 2240436797 926 LQAAESryEAQKRItQVFELEILDLYGRLEK 956
Cdd:PRK04778 409 LRKDEL--EAREKL-ERYRNKLHEIKRYLEK 436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
735-947 |
2.01e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 735 MKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKlHSQIRQLQHDREEFYNQSQELQTKLEDcrnmIAELRIELK 814
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK-EAQLESSREIVKSYENELDPLKNRLKE----IEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 815 KANNKLSNSESVQQQMEFLNRQL-LVLGEV---NELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTS 890
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELeLKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLN----KERRLLNQE 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2240436797 891 QKRILELESHLAKKDHLLLEQ--KKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEI 947
Cdd:TIGR00606 342 KTELLVEQGRLQLQADRHQEHirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
724-955 |
2.59e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 724 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTmvtkLHSQIRQLQHDREEFYNQSQELQTKLEDCR 803
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE----LRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 804 NMIAELRIELKKANNKLSNsesvqqqmeflNRQLLVLG-----------------------EVNEL--YLEQLQNKHSDT 858
Cdd:PRK02224 426 EREAELEATLRTARERVEE-----------AEALLEAGkcpecgqpvegsphvetieedreRVEELeaELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 859 TKEVEMMKAAyrKELEKNRSHVLQQ----TQRLDTSQKRILELESHLAKKDhlllEQKKYLEDVKLQARGQLQAAESRYE 934
Cdd:PRK02224 495 EERLERAEDL--VEAEDRIERLEERredlEELIAERRETIEEKRERAEELR----ERAAELEAEAEEKREAAAEAEEEAE 568
|
250 260
....*....|....*....|.
gi 2240436797 935 AQKRITQVFELEILDLYGRLE 955
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIE 589
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
728-954 |
2.88e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 728 LEEHNAAMKDQLKLQEKDIQMWKvslQKEQARYNQLQEQRDTmvtklHSQIR-QLQHDREEFYNQSQELQTKL----EDC 802
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCK---KQEERMLKQIENLEEK-----EMNLRdELESVREEFIQKGDEVKCKLdkseENA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 803 RNMIAELRIEL--------------KKANNKLSNSESVQQQMEFL-------NRQLlvlgEVNELYLEQLQNKHSDTTKE 861
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlkKQIENKNKNIEELHQENKALkkkgsaeNKQL----NAYEIKVNKLELELASAKQK 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 862 VEMMKAAYRKELEKNR---SHVLQQTQRLDTSQKRILELESHLAKK-DH------LLLEQKKYLEDVKLQAR-GQLQAAE 930
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKLQKEIDKRcQHkiaemvALMEKHKHQYDKIIEERdSELGLYK 731
|
250 260
....*....|....*....|....
gi 2240436797 931 SRYEAQKRITQVFELEILDLYGRL 954
Cdd:pfam05483 732 NKEQEQSSAKAALEIELSNIKAEL 755
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
704-846 |
3.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRNR-RLLRKVIKAAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTM---VTKLHSQIR 779
Cdd:COG4717 105 EELEAELEELREElEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELeaeLAELQEELE 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2240436797 780 QL-QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLsnsESVQQQMEFLNRQLLVLGEVNEL 846
Cdd:COG4717 181 ELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQLENELEAAALEERL 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
716-941 |
3.30e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 716 RRLLRKVIKAAALEEHNAAMKD----QLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTM---VTKLHSQIRQLQHDREEF 788
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvVEELTAKKMTLESSERTV 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 789 YNQSQELQTK---LEDCRNMIAELRI-------ELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN----- 853
Cdd:pfam15921 499 SDLTASLQEKeraIEATNAEITKLRSrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmtqlv 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 854 -KHSDTTKEVEMMKAAYRKELEKNRSHvLQQTQRL-DTSQKRILELESHLAKkdhllLEqkkyLEDVKLqargqLQAAES 931
Cdd:pfam15921 579 gQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILkDKKDAKIRELEARVSD-----LE----LEKVKL-----VNAGSE 643
|
250
....*....|
gi 2240436797 932 RYEAQKRITQ 941
Cdd:pfam15921 644 RLRAVKDIKQ 653
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
704-950 |
3.49e-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: 47.22 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRNRRLLRKVIKAAALEEhnaaMKDQLKLQEKdiqmwKVSLQKEQARYNQLQE------------------ 765
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEED----QAEAEEKLEK-----QRQLREEIDEFNEEQAewkelekeeereederil 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 766 ----QRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKlsnSESVQQQMEFLNRQLLVLG 841
Cdd:pfam13868 159 eylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE---RKERQKEREEAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 842 EVNELYLEQLQNKhsdttkevEMMKAAYRKELEKNRSHVLQQTQRLDtsQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 921
Cdd:pfam13868 236 ELQQAREEQIELK--------ERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
250 260 270
....*....|....*....|....*....|...
gi 2240436797 922 ARGQ----LQAAESRYEAQKRITQVFELEILDL 950
Cdd:pfam13868 306 RAAEreeeLEEGERLREEEAERRERIEEERQKK 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
703-887 |
3.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 703 YERFKRQQHALRNRRllrkvikaAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQAR--YNQLQEQRDTMVTKLHsQIRQ 780
Cdd:COG4717 90 YAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLPLYQELEALEaeLAELPERLEELEERLE-ELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 781 LQHDREEFYNQSQELQTKLEDCRNMI-AELRIELKKANNKLsnsESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTT 859
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL---EELQQRLAELEEE-----------LEEAQEELEELE 226
|
170 180
....*....|....*....|....*...
gi 2240436797 860 KEVEMMKAAYRKELEKNRshvLQQTQRL 887
Cdd:COG4717 227 EELEQLENELEAAALEER---LKEARLL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
707-904 |
1.15e-04 |
|
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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 707 KRQQHALRNRRLLRKVIKAaaLEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQ---- 782
Cdd:COG4942 41 KELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 783 ----------HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgEVNELYLEQLQ 852
Cdd:COG4942 119 qpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL----EEERAALEALK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2240436797 853 NKHSDTTKEVEMMKAAYRKELEKNRshvlQQTQRLDTSQKRILELESHLAKK 904
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAER 242
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
735-937 |
1.46e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 44.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 735 MKDQLKLQEKDIQMWKVSLQKeqarYNQLQEQRDTMVTKLHSQIrqlqhdreefynqsQELQTKLEDCRNMIAELRIELK 814
Cdd:pfam14988 10 AKKTEEKQKKIEKLWNQYVQE----CEEIERRRQELASRYTQQT--------------AELQTQLLQKEKEQASLKKELQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 815 KANNKLSNSESVQQQMEFLnrqllvlgevnELYLEQLQNKHSDTTKEVEMM----KAAYRKEL---------EKNRSHVL 881
Cdd:pfam14988 72 ALRPFAKLKESQEREIQDL-----------EEEKEKVRAETAEKDREAHLQflkeKALLEKQLqelrilelgERATRELK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2240436797 882 QQTQRLDTSQKRILELESHLAKKDHLLLeQKKYLEdvKLQARGQLQAAESRYEAQK 937
Cdd:pfam14988 141 RKAQALKLAAKQALSEFCRSIKRENRQL-QKELLQ--LIQETQALEAIKSKLENRK 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
735-956 |
1.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 735 MKDQLKLQEKDIQmwkvsLQKEQAR--YNQLQEQRDT---MVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAEL 809
Cdd:COG1340 2 KTDELSSSLEELE-----EKIEELReeIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 810 RIELKKANNKLSnseSVQQQMEFLNRQLLVLGEVNELyLEQLQnkhsdttKEVEmmkaayrkELEKNrshvlQQTQRLDT 889
Cdd:COG1340 77 KEERDELNEKLN---ELREELDELRKELAELNKAGGS-IDKLR-------KEIE--------RLEWR-----QQTEVLSP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 890 SQ-----KRILELESHLAKKDHLLLEQKKYLEDVKlqargqlQAAESRYEAQ---KRITQVFE------LEILDLYGRLE 955
Cdd:COG1340 133 EEekelvEKIKELEKELEKAKKALEKNEKLKELRA-------ELKELRKEAEeihKKIKELAEeaqelhEEMIELYKEAD 205
|
.
gi 2240436797 956 K 956
Cdd:COG1340 206 E 206
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
717-921 |
1.97e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 717 RLLRKVIKAAA----LEEHNAAMKDQLK-------LQEKDIQMWKVSLQKEQARYNQLQ---EQRDTMVTKLHSQIRQLQ 782
Cdd:TIGR04523 430 RLKETIIKNNSeikdLTNQDSVKELIIKnldntreSLETQLKVLSRSINKIKQNLEQKQkelKSKEKELKKLNEEKKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 783 hdreefyNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF-LNRQLL---VLG---EVNELYLEQ--LQN 853
Cdd:TIGR04523 510 -------EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLKKENLekeIDEknkEIEELKQTQksLKK 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 854 KHS---DTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQ 921
Cdd:TIGR04523 583 KQEekqELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
704-888 |
1.98e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRN----RRLLRKviKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQ-KEQARYNQlQEQ-RDTMVTKLHSQ 777
Cdd:PRK10929 65 ERAKQYQQVIDNfpklSAELRQ--QLNNERDEPRSVPPNMSTDALEQEILQVSSQlLEKSRQAQ-QEQdRAREISDSLSQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 778 IRQLQHD-REEFYNQSQELQTkledcrnmiaelrieLKKANNKLSNSESVQQQMEFLNRQLLVlgevNELYLEQLQnkhs 856
Cdd:PRK10929 142 LPQQQTEaRRQLNEIERRLQT---------------LGTPNTPLAQAQLTALQAESAALKALV----DELELAQLS---- 198
|
170 180 190
....*....|....*....|....*....|...
gi 2240436797 857 dttkevemmkAAYRKELEKNRSHVLQ-QTQRLD 888
Cdd:PRK10929 199 ----------ANNRQELARLRSELAKkRSQQLD 221
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
709-814 |
2.06e-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: 43.74 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 709 QQHALRNRRLlrkVIKAAALEEHNAAMKDQLKLQEKDiqmwKVSLQKEQARYNQLQEQRDTMvtKLHSQ-----IRQLQH 783
Cdd:pfam13851 50 SEIQQENKRL---TEPLQKAQEEVEELRKQLENYEKD----KQSLKNLKARLKVLEKELKDL--KWEHEvleqrFEKVER 120
|
90 100 110
....*....|....*....|....*....|....*
gi 2240436797 784 DREEFYNQS----QELQTKLEdCRNMIAELRIELK 814
Cdd:pfam13851 121 ERDELYDKFeaaiQDVQQKTG-LKNLLLEKKLQAL 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
716-899 |
2.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 716 RRLLRKVIK-AAALEEHNAAMKDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTklhsqirqLQHDREEFYNQSQE 794
Cdd:PRK03918 244 EKELESLEGsKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 795 LQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELY---------LEQLQNKHSDTTKE--VE 863
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeakakkeeLERLKKRLTGLTPEklEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2240436797 864 MMKAA--YRKELEKNRSHVLQQTQRLDTSQKR----ILELES 899
Cdd:PRK03918 392 ELEELekAKEEIEEEISKITARIGELKKEIKElkkaIEELKK 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
736-944 |
3.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 736 KDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEfyNQSQELQTKLEDCRNMIAELRielkK 815
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE--IDVASAEREIAELEAELERLD----A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 816 ANNKLsnsESVQQQmeflnrqllvlgevnelyLEQLQNKHSDTTKEVEMMKAAyRKELEKNRShvlQQTQRLDTSQKRIL 895
Cdd:COG4913 683 SSDDL---AALEEQ------------------LEELEAELEELEEELDELKGE-IGRLEKELE---QAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2240436797 896 ELESHLAKKDHLLLEQK-------KYLEDVKLQARGQLQAAESRYE-AQKRITQVFE 944
Cdd:COG4913 738 AAEDLARLELRALLEERfaaalgdAVERELRENLEERIDALRARLNrAEEELERAMR 794
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
733-938 |
4.05e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 733 AAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQrdtmVTKLHSQIRQLQHDREEfynqsQElqtkledcRNMIAELRIE 812
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQ----IDELNASIAKLEQQQAA-----QE--------RLLAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 813 LKKANNK-----LSNSESvqQQMEflnRQLLVLGEVNEL---YLEQLQNkhsdTTKEVemmkAAYRKELEKNRSH---VL 881
Cdd:PRK11637 134 FRQGEHTglqliLSGEES--QRGE---RILAYFGYLNQArqeTIAELKQ----TREEL----AAQKAELEEKQSQqktLL 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436797 882 ----QQTQRLDTS----QKRILELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESryEAQKR 938
Cdd:PRK11637 201 yeqqAQQQKLEQArnerKKTLTGLESSLQKDQQQLSE----LRANESRLRDSIARAER--EAKAR 259
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
806-934 |
6.85e-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: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 806 IAELRIELKKANNKLSNSES-VQQQMEFLNRQLLVLGEVNELYLEQLQnKHSDTTKEVEmmkaAYRKELEKNRSHVLQQT 884
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAqLQKLQEDLEKQAEIAREAQQNYERELV-LHAEDIKALQ----ALREELNELKAEIAELK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2240436797 885 QRLDTSQKRILELESHLAkkdhlllEQKKYLEDvklqargQLQAAESRYE 934
Cdd:pfam07926 78 AEAESAKAELEESEESWE-------EQKKELEK-------ELSELEKRIE 113
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
703-887 |
9.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 703 YERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKD----IQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQI 778
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelraALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 779 RQlqHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDT 858
Cdd:COG4717 423 EA--LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
170 180
....*....|....*....|....*....
gi 2240436797 859 TkeVEMMKAAYRKElekNRSHVLQQTQRL 887
Cdd:COG4717 501 L--LEEAREEYREE---RLPPVLERASEY 524
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
719-935 |
1.13e-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: 43.27 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 719 LRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQ-RDTMVTKlhsqirqlqHDREEfynqsqelqt 797
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlREVENEK---------NDKDK---------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 798 KLEDCRNMIAElriELKKANNKLSNSESVQQQMEFLNRQLLVLGEVNElylEQLQNKHSDTTKEvEMMKAayrkeLEKNR 877
Cdd:pfam10174 601 KIAELESLTLR---QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRE---DNLADNSQQLQLE-ELMGA-----LEKTR 668
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 878 SHVLQQTQRLDTSQKRILELESHLAKkdhLLLEQKKYLEDV---KLQArgqLQAAESRYEA 935
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEKDGHLTN---LRAERRKQLEEIlemKQEA---LLAAISEKDA 723
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
724-942 |
1.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 724 KAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYN--QLQEQRDTMVTK---LHSQIRQLQHDREEFYNQSQELQTK 798
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQlseLESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 799 LEDCRNMIAELrielkkannklSNSESVQQQMEFLNRQLLVLGEVNELYLE----------QLQNKHSDTTKEVEMMKAA 868
Cdd:COG3206 249 LGSGPDALPEL-----------LQSPVIQQLRAQLAELEAELAELSARYTPnhpdvialraQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2240436797 869 YRKELEKNRSHVLQQTQRLDTSQKRILELESHlakkdhllleQKKYLEdvkLQArgQLQAAESRYEA-QKRITQV 942
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPEL----------EAELRR---LER--EVEVARELYESlLQRLEEA 377
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
719-901 |
1.33e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 719 LRKVIKAAALEE-HNAAMKDQL-KLQEKDIQMWKvsLQKEQARYNQLQEQRDTMVTKLHSQIRQLQhDREEFYNQSQELQ 796
Cdd:PRK01156 269 LEKNNYYKELEErHMKIINDPVyKNRNYINDYFK--YKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 797 TKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQllvlgevnelyLEQLQNKHSDTTKEVEMMKAAYRKELEKN 876
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN-----------IERMSAFISEILKIQEIDPDAIKKELNEI 414
|
170 180
....*....|....*....|....*
gi 2240436797 877 RSHVLQQTQRLDTSQKRILELESHL 901
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENL 439
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
709-886 |
1.47e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 709 QQHALRNRRLLRKVIKaaaLEEHNAAMKDqLKLQEKDIQMWKVSLQKEQARYN---------QLQEQRDTMVTKLHSQIR 779
Cdd:PHA02562 234 AEIEELTDELLNLVMD---IEDPSAALNK-LNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 780 QLQHDREEFYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSesvQQQMEFLNRQLLVLgevnELYLEQLQNKHSDTT 859
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTN---KQSLITLVDKAKKV----KAAIEELQAEFVDNA 378
|
170 180
....*....|....*....|....*..
gi 2240436797 860 KEVEMMKAAYRKELEKNRSHVLQQTQR 886
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
705-937 |
1.59e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 705 RFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHD 784
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 785 REEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEFLNRQLlvlgevnelyLEQLQNKHSDTTKEVEM 864
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----------ENKIQDGKDDYLKQKET 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 865 MKAAYRKELEKNRSH-------VLQQTQRLDTS--QKRILELESHLAKKDHLLLEQKKYLEDvKLQARGQLQAAESRYEA 935
Cdd:TIGR00606 978 ELNTVNAQLEECEKHqekinedMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQ-HLKEMGQMQVLQMKQEH 1056
|
..
gi 2240436797 936 QK 937
Cdd:TIGR00606 1057 QK 1058
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
725-816 |
2.16e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.49 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 725 AAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNqlQEQRDTMVTKLHSQIRQLQHDREEFynqSQELQTKLedcRN 804
Cdd:smart00935 20 QKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS--EAAREKKEKELQKKVQEFQRKQQKL---QQDLQKRQ---QE 91
|
90
....*....|..
gi 2240436797 805 MIAELRIELKKA 816
Cdd:smart00935 92 ELQKILDKINKA 103
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
713-955 |
2.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 713 LRNRRLLRKVIkaaaleehnaamkDQLKLQEKDIQmwkvSLQKEQARYNQLQEQRDTMVTKLhSQIRQLQ---HDRE--- 786
Cdd:COG3206 90 LKSRPVLERVV-------------DKLNLDEDPLG----EEASREAAIERLRKNLTVEPVKG-SNVIEISytsPDPElaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 787 -------EFYNQSQeLQTKLEDCRNMIAELRIELKKANNKLSNSEsvQQQMEFLNRQLLV-LGEVNELYLEQ---LQNKH 855
Cdd:COG3206 152 avanalaEAYLEQN-LELRREEARKALEFLEEQLPELRKELEEAE--AALEEFRQKNGLVdLSEEAKLLLQQlseLESQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 856 SDTTKEVEMMKAAY---RKELEKNRSHV--LQQTQRLDTSQKRILELESHLAKkdhlllEQKKYLE---DVKlQARGQLQ 927
Cdd:COG3206 229 AEARAELAEAEARLaalRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAE------LSARYTPnhpDVI-ALRAQIA 301
|
250 260
....*....|....*....|....*....
gi 2240436797 928 AAESRYEAQ-KRITQVFELEILDLYGRLE 955
Cdd:COG3206 302 ALRAQLQQEaQRILASLEAELEALQAREA 330
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
735-956 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 735 MKDQLKLQEKDIQMW---KVSLQKEQARYNQLQEQRDTmvtklhsqirqlqhdreeFYNQSQELQTKLEDCRNMIAELRI 811
Cdd:pfam05622 150 LRRQVKLLEERNAEYmqrTLQLEEELKKANALRGQLET------------------YKRQVQELHGKLSEESKKADKLEF 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 812 ELKKANNKLsnsESVQQQMEFLNRQLLVLGEVN-ELYLEQLQNKH----------SDTTKEV---EMMKAAYRKELEK-- 875
Cdd:pfam05622 212 EYKKLEEKL---EALQKEKERLIIERDTLRETNeELRCAQLQQAElsqadallspSSDPGDNlaaEIMPAEIREKLIRlq 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 876 --NRSHVLQQT-----------QRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQV 942
Cdd:pfam05622 289 heNKMLRLGQEgsyrerltelqQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEH 368
|
250
....*....|....
gi 2240436797 943 FElEILDLYGRLEK 956
Cdd:pfam05622 369 LE-KLHEAQSELQK 381
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
751-938 |
2.69e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 751 VSLQKEQARYNQLQEQRDTMvtklhsqiRQLQ--HDREEFYNQSQELQTKLEDCRNMIAELRIELKKANN-----KLSNS 823
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEM--------RRLEveRKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEeirlrKQRLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 824 ESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHsdttkevemmkaayRKELEKNRSHVLQQTQRLDTSQKRILELESHLAK 903
Cdd:pfam15709 398 EERQRQEEEERKQRLQLQAAQERARQQQEEFR--------------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAE 463
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436797 904 KDHLLLEQKKYlEDVKLQARGQLQAAESRYEAQKR 938
Cdd:pfam15709 464 EQKRLMEMAEE-ERLEYQRQKQEAEEKARLEAEER 497
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
707-894 |
3.12e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 707 KRQQHALRNRRLlRKVIKAA-----ALEEHNAAMKDQLKLQEKDIqMWKVSLQKEQARYNQLQeqrdtmvtklhSQIRQL 781
Cdd:pfam12795 31 KIDASKQRAAAY-QKALDDApaelrELRQELAALQAKAEAAPKEI-LASLSLEELEQRLLQTS-----------AQLQEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 782 QHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQ------QQMEFLNRQLLVLGEVNELYLEQLQNkh 855
Cdd:pfam12795 98 QNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGeplseaQRWALQAELAALKAQIDMLEQELLSN-- 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2240436797 856 sdttkevEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRI 894
Cdd:pfam12795 176 -------NNRQDLLKARRDLLTLRIQRLEQQLQALQELL 207
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
704-946 |
3.25e-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: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRNRRLLRKVIKAAalEEHNaAMKDQLKLQEKDIQMWKVSLQKEQaRYNQLQEQRDTMVTKLHSQIRQLQH 783
Cdd:pfam05557 330 LNKKLKRHKALVRRLQRRVLLLT--KERD-GYRAILESYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLSV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 784 DREEFYNQSQELQTkledcrnmiAELRIELKKANNKLSNSESVQQQMEFLNRqllvlgEVNELYLEQLQNKHSDTTKEVE 863
Cdd:pfam05557 406 AEEELGGYKQQAQT---------LERELQALRQQESLADPSYSKEEVDSLRR------KLETLELERQRLREQKNELEME 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 864 MMKAAYRKELEKNRSHVLQ---------------QTQRLD---TSQKRILE-LESHLAKKDHLLLEQKKYLEDVKLQARG 924
Cdd:pfam05557 471 LERRCLQGDYDPKKTKVLHlsmnpaaeayqqrknQLEKLQaeiERLKRLLKkLEDDLEQVLRLPETTSTMNFKEVLDLRK 550
|
250 260
....*....|....*....|..
gi 2240436797 925 QLQAAESRYEAQKRITQVFELE 946
Cdd:pfam05557 551 ELESAELKNQRLKEVFQAKIQE 572
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
753-957 |
3.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 753 LQKEQARYNQLQEQRdTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKLSNSESVQQQMEF 832
Cdd:PRK03918 157 LDDYENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 833 LnRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVlQQTQRLDTSQKRILELESHLAKKDHLLLEQK 912
Cdd:PRK03918 236 L-KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2240436797 913 KYLEDVKLQARG---QLQAAESRYEAQKRITQVFElEILDLYGRLEKD 957
Cdd:PRK03918 314 KRLSRLEEEINGieeRIKELEEKEERLEELKKKLK-ELEKRLEELEER 360
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
738-912 |
4.35e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 738 QLKLQEKDIQMWKVSLQK---EQARYNQLQEQRDtmVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELK 814
Cdd:COG5022 922 NLEFKTELIARLKKLLNNidlEEGPSIEYVKLPE--LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 815 KANNKLSNSESVQ---QQMEFLNRQLLVLGEVNELYLEQ---------LQNKHSDTTKEVEMMKA-----AYRKELEKNR 877
Cdd:COG5022 1000 ELAELSKQYGALQestKQLKELPVEVAELQSASKIISSEstelsilkpLQKLKGLLLLENNQLQArykalKLRRENSLLD 1079
|
170 180 190
....*....|....*....|....*....|....*
gi 2240436797 878 SHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQK 912
Cdd:COG5022 1080 DKQLYQLESTENLLKTINVKDLEVTNRNLVKPANV 1114
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
757-922 |
4.61e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 757 QARYNQLQEQRDTMVTKLHSqirqLQHDREEFYNQSQELQTKLEDCRNMIAEL--RIE--LKKANNKLSNSESVQQQMef 832
Cdd:pfam10168 560 QKRVKLLKLQKEQQLQELQS----LEEERKSLSERAEKLAEKYEEIKDKQEKLmrRCKkvLQRLNSQLPVLSDAEREM-- 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 833 lNRQLLVLGEVnelyLEQLQNkhsdTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRIL-ELESHLAKKdhlLLEQ 911
Cdd:pfam10168 634 -KKELETINEQ----LKHLAN----AIKQAKKKMNYQRYQIAKSQSIRKKSSLSLSEKQRKTIkEILKQLGSE---IDEL 701
|
170
....*....|.
gi 2240436797 912 KKYLEDVKLQA 922
Cdd:pfam10168 702 IKQVKDINKHV 712
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
728-918 |
4.64e-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: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 728 LEEHNAAMKDQLKLQEKDIQMwkvSLQKE----QARYNQLQEQrdtmvTKLHSQ-IRQLQHDREEFYNQSQELQTKLEDC 802
Cdd:pfam05622 287 LQHENKMLRLGQEGSYRERLT---ELQQLledaNRRKNELETQ-----NRLANQrILELQQQVEELQKALQEQGSKAEDS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 803 RNMIAELRIELKKANNKLSNSESVQQQMEflnrqllvlgevnELYLEQLQNKHSDTT--------KEVEM--MKAAYRKE 872
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIE-------------ELEPKQDSNLAQKIDelqealrkKDEDMkaMEERYKKY 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2240436797 873 LEKNRSHVlqqtQRLDTSQKRILELESHLAKKDhlLLEQKKYLEDV 918
Cdd:pfam05622 426 VEKAKSVI----KTLDPKQNPASPPEIQALKNQ--LLEKDKKIEHL 465
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
774-926 |
5.79e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 39.72 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 774 LHSQIRQLQHDREEFYNQSQELQTKLEDCRnmiaelrielKKANNKLSNSESVQQQMEFLN-------RQLLVLgevnEL 846
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQ----------QKESKFLENLASLKHENDNLSsmlnrkeRRLKDL----ED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 847 YLEQLQNKHsdttKEVEMMKAAYRKELEKNRSH---VLQQTQRLDTSQKRIleLESHLAKKDHLLLE---QKKYLEDVKL 920
Cdd:pfam17078 74 QLSELKNSY----EELTESNKQLKKRLENSSASettLEAELERLQIQYDAL--VDSQNEYKDHYQQEintLQESLEDLKL 147
|
....*.
gi 2240436797 921 QARGQL 926
Cdd:pfam17078 148 ENEKQL 153
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
821-938 |
6.96e-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: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 821 SNSESVQQQMEFLNRQLLVLGEVNELYLEQLQN--KHSDTTKEVEMMKAAYRKELEKNRSHVLQQ----TQRLDTSQKRI 894
Cdd:pfam10473 17 RKADSLKDKVENLERELEMSEENQELAILEAENskAEVETLKAEIEEMAQNLRDLELDLVTLRSEkenlTKELQKKQERV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2240436797 895 LELESHLAKKDHLLLEqkkyLEDVKLQARGQLQAAESRYEAQKR 938
Cdd:pfam10473 97 SELESLNSSLENLLEE----KEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
725-956 |
7.60e-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: 40.54 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 725 AAALEEHNAAMkDQLKLQEKDIQMWKVSLQKEQaryNQLQEQRDTMvtklhSQIRQ-LQHDREEFYNQSQELQTKLEDC- 802
Cdd:pfam01576 355 TQALEELTEQL-EQAKRNKANLEKAKQALESEN---AELQAELRTL-----QQAKQdSEHKRKKLEGQLQELQARLSESe 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 803 --RNMIAE----LRIELKKANNKLSNSES----VQQQMEFLNRQllvLGEVNELYLEQLQNKHSDTTKevemmkaayRKE 872
Cdd:pfam01576 426 rqRAELAEklskLQSELESVSSLLNEAEGknikLSKDVSSLESQ---LQDTQELLQEETRQKLNLSTR---------LRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 873 LEKNRSHVLQQTQRLDTSQKRileLESHLAKKDHLLLEQKKYLEDVKlqarGQLQAAEsryEAQKRITQVFELEILDL-- 950
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRN---VERQLSTLQAQLSDMKKKLEEDA----GTLEALE---EGKKRLQRELEALTQQLee 563
|
250
....*....|
gi 2240436797 951 ----YGRLEK 956
Cdd:pfam01576 564 kaaaYDKLEK 573
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
729-958 |
8.78e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 729 EEHNAAMKDQLKLQEKDIQMwKVSLQKEQARYNQLQEQRDTMVTKLHSQiRQLQHDREE----FYNQSQELQTKLEDcrn 804
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAE-TELCAEAEEmrarLAARKQELEEILHE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 805 MIAELRIELKKANNKLSNSESVQQQMEFLN---------RQLLVLGEVNE-----------LYLEQLQNKHSDTTKEVEM 864
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEeqldeeeaaRQKLQLEKVTTeakikkleediLLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 865 MKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYL-----EDVKLQ---ARGQLQAAESRYEAQ 936
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKrklegESTDLQeqiAELQAQIAELRAQLA 239
|
250 260
....*....|....*....|..
gi 2240436797 937 KRitqvfELEILDLYGRLEKDG 958
Cdd:pfam01576 240 KK-----EEELQAALARLEEET 256
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
683-956 |
9.23e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 683 PSDEIRTLRDQLLLLHNQLLYERFKRQQH-----ALRNR-RLLRKVIKAAAL--EEHNAAMKDQLKLQEKDIQMWKVSLQ 754
Cdd:PRK04863 835 PEAELRQLNRRRVELERALADHESQEQQQrsqleQAKEGlSALNRLLPRLNLlaDETLADRVEEIREQLDEAEEAKRFVQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 755 KEQARYNQLqeqrDTMVTKLHS---QIRQLQHDreefYNQSQELQTKLedcrNMIAELRIELKKANNKLSNSESVQqqme 831
Cdd:PRK04863 915 QHGNALAQL----EPIVSVLQSdpeQFEQLKQD----YQQAQQTQRDA----KQQAFALTEVVQRRAHFSYEDAAE---- 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 832 flnrqllVLGEVNELyLEQLQNKHsdttKEVEMMKAAYRKELEknrshvlQQTQRLDTSQKRILELESHLAKKDHLLLEQ 911
Cdd:PRK04863 979 -------MLAKNSDL-NEKLRQRL----EQAEQERTRAREQLR-------QAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2240436797 912 KKYLEDVKLQA-----------RGQLQAAES-----RYEAQKRITqVFELEILDLYGRLEK 956
Cdd:PRK04863 1040 KQELQDLGVPAdsgaeerararRDELHARLSanrsrRNQLEKQLT-FCEAEMDNLTKKLRK 1099
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
704-875 |
9.93e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 704 ERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQH 783
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2240436797 784 DREEFYNQSQELQTKLEdcrnmIAELRIELKKANNKLSNsesvqqqmeflnrqllvLGEVNELYLE---QLQNKHSDTTK 860
Cdd:COG1196 745 EELLEEEALEELPEPPD-----LEELERELERLEREIEA-----------------LGPVNLLAIEeyeELEERYDFLSE 802
|
170
....*....|....*
gi 2240436797 861 EVEMMKAAyRKELEK 875
Cdd:COG1196 803 QREDLEEA-RETLEE 816
|
|
| |
