|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
19-114 |
5.12e-51 |
|
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438752 [Multi-domain] Cd Length: 96 Bit Score: 174.75 E-value: 5.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 19 KAYLKSAEGFFVLN-KSTTIGRHeNSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGD 97
Cdd:cd22700 1 KGYLKSSDGIFQLDpKVTTIGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAPGD 79
|
90
....*....|....*..
gi 1034555165 98 ILRFGSAGLTYELVIEN 114
Cdd:cd22700 80 VLRFGFGGLPYELVVDN 96
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
35-101 |
1.56e-18 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 81.08 E-value: 1.56e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555165 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRF 101
Cdd:pfam00498 1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDG-GGRFYLEDLGSTNGTFVNGQRLGPEPVRLKDGDVIRL 66
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
627-1169 |
3.89e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 627 EHYKKLMSQAQELQIKFNSSQ----ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER- 701
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKlrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 702 -NRAKETLEEERKRMQELESLLAQQKKALAksitQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL 780
Cdd:COG1196 293 lLAELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 781 ESEKRKVQDLENHLTQQKEisESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEE 860
Cdd:COG1196 369 EAEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 861 TQKTKATESLKAESLALKLNETLAELETTKTKMImVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH----- 935
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglaga 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 936 -------------AQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERP----QDPLVAPMTESSAKDMAYEHLID 998
Cdd:COG1196 526 vavligveaayeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 999 DLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQS-------KELSVLKEKMAQMSSLV 1071
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSltggsrrELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1072 EKKDRELKALEEALRASQEKHRLQLntEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQ 1151
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*...
gi 1034555165 1152 RQKKALSELRARIKELEK 1169
Cdd:COG1196 764 ELERELERLEREIEALGP 781
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
28-109 |
1.24e-17 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 79.24 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd00060 14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITP-PVPLQDGDVIRLGDTTFR 90
|
..
gi 1034555165 108 YE 109
Cdd:cd00060 91 FE 92
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
29-110 |
4.74e-17 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 77.69 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 29 FVLNKS-TTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:COG1716 16 FPLDGGpLTIGRAPDNDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVTE-PAPLRDGDVIRLGKTELR 92
|
...
gi 1034555165 108 YEL 110
Cdd:COG1716 93 FRL 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-1044 |
9.57e-14 |
|
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: 76.65 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 292 RQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSL-KNEGENLKRDNAITSGMVSSLQ 370
Cdd:TIGR02169 233 EALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 371 KDILAK-------DEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQ----EKELKLCKTQI 439
Cdd:TIGR02169 308 RSIAEKereledaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 440 QDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKIT----QVTEDNINF 515
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleQLAADLSKY 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 516 QQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKE-----VDLLQHL-QVSPPVSG-------- 581
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvHGTVAQLgSVGERYATaievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 582 -LQKVVLD---VLRHALSWLEE-------------VEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFN 644
Cdd:TIGR02169 548 rLNNVVVEddaVAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 645 SSQETQQSLLQEK---LREHLAEKEKL-----NEERLEQ--EEKLKAKIRQLTEEKAALE---EYITQERNRAKETLEEE 711
Cdd:TIGR02169 628 DIEAARRLMGKYRmvtLEGELFEKSGAmtggsRAPRGGIlfSRSEPAELQRLRERLEGLKrelSSLQSELRRIENRLDEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 712 RKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLE 791
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA-RIEELEEDLHKLEEALNDLE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 792 NHLTQQKeISESNIAYEKrkakeamekEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLK 871
Cdd:TIGR02169 786 ARLSHSR-IPEIQAELSK---------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 872 AESLALKLNETLAELETTKTKMIMVEERLIlqqkmvkalqdeqesqrhGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 951
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLG------------------DLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 952 HHKKIEGEIATLKDndpapkEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDL 1031
Cdd:TIGR02169 918 RLSELKAKLEALEE------ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
810
....*....|...
gi 1034555165 1032 RGelnEKQKMELE 1044
Cdd:TIGR02169 992 KE---KRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
239-966 |
1.34e-13 |
|
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: 76.25 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 239 AQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELsQKVSETTTSRQNEKE-----ISQKCQVLDEDIDAKQ 313
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL-QKELYALANEISRLEqqkqiLRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 314 KEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQ 393
Cdd:TIGR02168 323 AQLEELESKLDELAE--------ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 394 NKDKDHQLEALGSRCSVLKEELKQEDAHRE--LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKS 471
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 472 KLEHFRSQVIKATYGRAKPFRD------------KPVTDQQL-IEKITQVTEDNINFqQKKWTLQKETQLSNSKQEETTE 538
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERlqenlegfsegvKALLKNQSgLSGILGVLSELISV-DEGYEAAIEAALGGRLQAVVVE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 539 NIEKLRTSLDScqacmkisccshdLKKEVDLLQHLQVSPPVSGLQKVVLDvlRHALSWLEEVEQLLRDLGILPSSPNKGF 618
Cdd:TIGR02168 554 NLNAAKKAIAF-------------LKQNELGRVTFLPLDSIKGTEIQGND--REILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 619 S--LYLIYLLEHYKKLMSQAQELQIKFN-----------------SSQETQQSLLQEKlrehlAEKEKLNEERLEQEEkl 679
Cdd:TIGR02168 619 SylLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILERR-----REIEELEEKIEELEE-- 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 680 kaKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQELESLLAQQKKALAKsITQEKNRVKEALEEEQTRVQELEERLA 759
Cdd:TIGR02168 692 --KIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 760 RQKEVLESSIAHEKRkAKEALESEKRKVQDLENHLTQQKEISESniayekrkakeamekekkkvqdLENRLTKQKEELEL 839
Cdd:TIGR02168 765 ELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDE----------------------LRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 840 KEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESqrh 919
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE--- 898
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1034555165 920 gFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 966
Cdd:TIGR02168 899 -LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
37-110 |
3.83e-13 |
|
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438756 [Multi-domain] Cd Length: 102 Bit Score: 66.96 E-value: 3.83e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555165 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22704 21 VGR-EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIpEQTYITLKLGDSIRFGYDTNVYRF 94
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
29-109 |
3.60e-12 |
|
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438717 [Multi-domain] Cd Length: 97 Bit Score: 63.79 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 29 FVLNK-STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHI--QNVAVKLIPGDILRFGSAG 105
Cdd:cd22665 16 FPLYEgENVIGRDPSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRlkPNVRYELIDGDLLLFGDVK 93
|
....
gi 1034555165 106 LTYE 109
Cdd:cd22665 94 CQYV 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-934 |
4.33e-12 |
|
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: 71.24 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 271 IANLQNEVAELSQKVSETTTSRQNEKeisQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKN 350
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEE-LEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKD-----KDHQLEALGSRCSVLKEELKQEDAHRELR 425
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 426 EAQEKELKlckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQVIKAtygrakpfrdkpvtdQQLIEKI 505
Cdd:TIGR02168 460 EEALEELR---EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN---------------QSGLSGI 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 506 TQVTEDNINFQqKKWTLQKETQLSNSKQEETTEN-------IEKLRTSLDSCQACMKISCCSHDlKKEVDLLQHLQVSPP 578
Cdd:TIGR02168 522 LGVLSELISVD-EGYEAAIEAALGGRLQAVVVENlnaakkaIAFLKQNELGRVTFLPLDSIKGT-EIQGNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 579 VSG-----------LQKVVLDVLRHaLSWLEEVEQLLRDLGILPSSPN----------KGFSLY---------------- 621
Cdd:TIGR02168 600 FLGvakdlvkfdpkLRKALSYLLGG-VLVVDDLDNALELAKKLRPGYRivtldgdlvrPGGVITggsaktnssilerrre 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 622 LIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKLNEERLEQEEKLKAKIRQLTE-------EKAA 692
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEEleQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTE 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 693 LEEYITQERNR------AKETLEEERkrmQELESLLAQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLE 766
Cdd:TIGR02168 759 LEAEIEELEERleeaeeELAEAEAEI---EELEAQIEQLKEELKAL--------REALDELRAELTLLNEEAANLRERLE 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 767 SSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 846
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE--LESELEALLNERASLEEALALLRSELEELSEELRE 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 847 LNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELettktkmimvEERLILQQKMVKALQDEQESQRHGFEEEIM 926
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL----------SEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
....*...
gi 1034555165 927 EYKEQIKQ 934
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
626-1373 |
4.48e-12 |
|
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: 71.24 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 626 LEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqLTEEKAALEEyitqernrak 705
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEE---------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 706 eTLEEERKRMQELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKR 785
Cdd:TIGR02168 268 -KLEELRLEVSELEEEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 786 KVQDLENHLTQQKEISESNIAYEkrkakeameKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTK 865
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELE---------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 866 ATESLKAESLALKLNET-LAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 944
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 945 KLQK----------VTQHHKKIEGEIATLKDNDPAPKE----------ERPQDPLVApmTESSAKDmAYEHL-------- 996
Cdd:TIGR02168 497 LQENlegfsegvkaLLKNQSGLSGILGVLSELISVDEGyeaaieaalgGRLQAVVVE--NLNAAKK-AIAFLkqnelgrv 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 997 ---------IDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMS--------------DLRGELNEKQKMELEQNVV----- 1048
Cdd:TIGR02168 574 tflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYRIVtldgd 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1049 -----------------LVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRlQLNTEKEQKPRKKTQTc 1111
Cdd:TIGR02168 654 lvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISAL- 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1112 DTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEkARSPDHKDHQNESFLDLKNLRM 1191
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1192 ENNVQKILLDAKpdlptLSRIEILAPQNGLCNARFGSAMEKSGKM-----DVAEALELSEKLYLDMSKTLGSLMNIKnMS 1266
Cdd:TIGR02168 811 ELTLLNEEAANL-----RERLESLERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNER-AS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1267 GHVSMKYLSRQEREKVNQLRQRDldlvfDKITQLKNQLGRKEELLRGYEKDVEQLrrsKVSIEMYQSQVAKLEDDIYKEA 1346
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELE-----SKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEA 956
|
810 820
....*....|....*....|....*...
gi 1034555165 1347 EEKALLKEA-LERMEHQLcqeKRINRAI 1373
Cdd:TIGR02168 957 EALENKIEDdEEEARRRL---KRLENKI 981
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
29-103 |
7.18e-12 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438745 [Multi-domain] Cd Length: 91 Bit Score: 62.71 E-value: 7.18e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIqNVAVKLIPGDILRFGS 103
Cdd:cd22693 13 FPIDKSGiTIGRADDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRV-TQPVVVQPGDTIRIGA 85
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
656-1114 |
3.67e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEEKLKA-KIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQELESLLAQQKKALAKSIT 734
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 735 QEknrVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 814
Cdd:PTZ00121 1486 DE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 815 AMEKEKKKVQDLENRLTKQKEELELKEQKEdvlnnKLSDALAMVEETQKTKATESLKAESLALKLNETLAELEttktkmi 894
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE------- 1630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 895 mvEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKieGEIATLKDNDPAPKEER 974
Cdd:PTZ00121 1631 --EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 975 PQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQqs 1054
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-- 1784
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1055 kelsvLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTS 1114
Cdd:PTZ00121 1785 -----LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK 1839
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
648-951 |
8.52e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLlqEKLREHLAEKEKlNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQK 726
Cdd:COG1196 183 ATEENL--ERLEDILGELER-QLEPLERQAEKAERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 727 KALAKsITQEKNRVKEALEEEQTRVQEL---EERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISEs 803
Cdd:COG1196 260 AELAE-LEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 804 niayEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETL 883
Cdd:COG1196 338 ----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555165 884 AELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQ 951
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
34-102 |
1.31e-10 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438735 [Multi-domain] Cd Length: 96 Bit Score: 59.43 E-value: 1.31e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 34 STTIGRHENSDLVLQSPDIDNHHALIEYnEAECSFVLqDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22683 22 VTTIGRSRSCDLVLSDPSISRFHAELRL-EQNGINVI-DNNSANGTFINGKRIKGKTYILKNGDIIVFG 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
684-1090 |
1.11e-09 |
|
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: 63.55 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 684 RQLTEEKAALEEYiTQERNRAKETLEEERKRMQELESLLAqqkkalaksitqEKNRVKEALEEEQTRVQELEERLARQKE 763
Cdd:TIGR02169 156 RKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIID------------EKRQQLERLRREREKAERYQALLKEKRE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 764 VLESSIAHEKRKAKEALESEKRKVQDLENHLTQ-QKEISESNIAYEKRKAKeamekekkkVQDLENRLTKQKEELELKeq 842
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQL---------LEELNKKIKDLGEEEQLR-- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 843 kedvLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFE 922
Cdd:TIGR02169 292 ----VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 923 EEIMEYKEQIKQHAQT---IVSLEEKLQKVTQHHKKIEGEIatlkdndpapkeerpqdplvapmtessakdmayEHLIDD 999
Cdd:TIGR02169 368 DLRAELEEVDKEFAETrdeLKDYREKLEKLKREINELKREL---------------------------------DRLQEE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1000 LLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELnEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELK 1079
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410
....*....|.
gi 1034555165 1080 ALEEALRASQE 1090
Cdd:TIGR02169 494 EAEAQARASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-830 |
1.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 254 VSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQnekEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGySKV 333
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAELARLEQD-IAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 334 LCQTLSERNSEITSLKNEGENLKRDNAitsgmvsSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRcsvLKE 413
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELE-------ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE---LAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 414 ELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQVIKATYGRAKPFRD 493
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 494 KPVTDQQLIEKITQVTEDninfQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkisccshDLKKEVDLLQHL 573
Cdd:COG1196 457 EEEALLELLAELLEEAAL----LEAALAELLEELAEAAARLLLLLEAEADYEGFLE------------GVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 574 QVSPPVSGLQKVVLDVLRHALSWLEEVEQ--LLRDLGILpsspnkgfSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQ 651
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVA--------AAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 652 SLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAK 731
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 732 SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEkrK 811
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE--E 750
|
570
....*....|....*....
gi 1034555165 812 AKEAMEKEKKKVQDLENRL 830
Cdd:COG1196 751 EALEELPEPPDLEELEREL 769
|
|
| FHA_PS1-like |
cd22691 |
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ... |
36-110 |
1.39e-09 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438743 [Multi-domain] Cd Length: 113 Bit Score: 57.04 E-value: 1.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22691 32 VVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEpGVPVELEEGDTVRLGASTRVYRL 107
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
36-102 |
2.36e-09 |
|
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438729 [Multi-domain] Cd Length: 106 Bit Score: 56.03 E-value: 2.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555165 36 TIGRHENSDLVLQSPDIDNHHALIEYN----EAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22677 25 VFGRLPGCDVVLEHPSISRYHAVLQYRgdadDHDGGFYLYDLGSTHGTFLNKQRIPpKQYYRLRVGHVLKFG 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-1102 |
2.61e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 667 KLNEERLEQEEKLKAkirqlTEEKAALEEYITQERNRAKETLEEER---KRMQELESLLAQQKKALAKSITQEKNRVKEA 743
Cdd:COG1196 169 KYKERKEEAERKLEA-----TEENLERLEDILGELERQLEPLERQAekaERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 744 LEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAkeamekekkkv 823
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 824 QDLENRLTKQKEELelkeqkedvlnnklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQ 903
Cdd:COG1196 312 RELEERLEELEEEL---------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 904 QKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERpqdplvapm 983
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE--------- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 984 tessakdMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEK 1063
Cdd:COG1196 442 -------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034555165 1064 MAQMSSLVEKKDREL----KALEEALRASQEKHRLQLNTEKEQ 1102
Cdd:COG1196 515 LLAGLRGLAGAVAVLigveAAYEAALEAALAAALQNIVVEDDE 557
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
35-82 |
3.87e-09 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 53.72 E-value: 3.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034555165 35 TTIGRHENS-DLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVN 82
Cdd:smart00240 1 VTIGRSSEDcDIQLDGPSISRRHAVIVYDGGGR-FYLIDLGSTNGTFVN 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
656-1093 |
4.01e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKE--TLEEERKRMQELESLLAQQKKALAKsI 733
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELRE-I 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 734 TQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISEsniaYEKRKAK 813
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKK-----KLKELEKRLEELEERHELYEEAKAKKEELER----LKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 814 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKA---------TESLKAESLA---LKLNE 881
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEeytAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 882 TLAELETTKT-------------KMIMVEERLILQQKMVKALQD-EQESQRHGFEEEIMEYKE----------------- 930
Cdd:PRK03918 464 IEKELKEIEEkerklrkelreleKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEyeklkekliklkgeiks 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 931 ------QIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliDDLLAAQ 1004
Cdd:PRK03918 544 lkkeleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-----KELEREE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1005 KEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKM----ELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKA 1080
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
490
....*....|...
gi 1034555165 1081 LEEALRASQEKHR 1093
Cdd:PRK03918 699 LKEELEEREKAKK 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
656-1097 |
4.25e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKAL---- 729
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKAdelk 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 730 -----------AKSITQEKNRVKEALE--EEQTRVQELEERLARQKEVLESS-IAHEKRKAKEALE--SEKRKVQDLENH 793
Cdd:PTZ00121 1412 kaaaakkkadeAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKkaEEAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 794 LTQ-QKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVlnnKLSDALAMVEETQKT----KATE 868
Cdd:PTZ00121 1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADELKKAEELKKAeekkKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 869 SLKAE---SLALKLNETLAELETTKTKMIMveeRLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEK 945
Cdd:PTZ00121 1569 AKKAEedkNMALRKAEEAKKAEEARIEEVM---KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 946 LQKVTQHHKkiEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKeilsqqevIMKLRKDLTEAH 1025
Cdd:PTZ00121 1646 KKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEK 1715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1026 SRMSDLRG--ELNEKQKMELEQNVVLVQQQSKELSV---LKEKMAQMSSLVEKKDRELKA-----LEEALRASQEKHRLQ 1095
Cdd:PTZ00121 1716 KKAEELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRME 1795
|
..
gi 1034555165 1096 LN 1097
Cdd:PTZ00121 1796 VD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
631-991 |
6.48e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 631 KLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA----KIRQLTEEKAALEEYITQERNRAKE 706
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeakKKAEEAKKKADEAKKAAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 707 TLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQElEERLARQKEVLESSIAHEKRKAKEALESEKRK 786
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 787 VQDLENHLTQQKEI--SESNIAYEKRKAKEAMEKEKKKVQDLEN--RLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 862
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 863 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 942
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 943 EEKlQKVTQHHKKIEGEIATLKDNDPAPKEE--RPQDPLVAPMTESSAKDM 991
Cdd:PTZ00121 1754 EEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDI 1803
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
28-109 |
9.43e-09 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 54.14 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsFVLQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGSAGLT 107
Cdd:cd22673 16 FPLTKKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGK-AYLENLSTTNPTLVNGKAIEK-SAELKDGDVITIGGRSFR 93
|
..
gi 1034555165 108 YE 109
Cdd:cd22673 94 FE 95
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
314-964 |
1.26e-08 |
|
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: 59.65 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 314 KEIQSLKSQISALQKGYsKVLCQTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQ 393
Cdd:TIGR04523 40 KKLKTIKNELKNKEKEL-KNLDKNLNKDEEKINNSNNKIKILEQQ-------IKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 394 NKDKDHQLEALGSRCSVLKEELKQEDAH-------------------------RELREAQEKELKLCKTQIQDMEKEMKK 448
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNidkflteikkkekeleklnnkyndlKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 449 LRAELRKSCTEQSVISRTLREKSKLEhfrSQVIKatygrakpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQK-ETQ 527
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLE---SQISE--------------LKKQNNQLKDNIEKKQQEINEKTTEISNtQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 528 LSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQvsppvsglQKVVLDVLRHALSWLEEVEQLLRDL 607
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN--------NQKEQDWNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 608 GILPSSPNKGFSlyliyllehykKLMSQAQELQIKFNSSQETQQSllqekLREHLAEKEKLNEERLEQEEKLKAKIRQLT 687
Cdd:TIGR04523 327 QNQISQNNKIIS-----------QLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 688 EEKAALEEYITQERNRAKEtLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEaLEEEQTRVQELEERLARQKEVLES 767
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 768 SIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNiayekrkakeamekekkkvQDLENRLTKQKEELELKEQKEDVL 847
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------------------KELEEKVKDLTKKISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 848 NNklsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIME 927
Cdd:TIGR04523 530 ES---------EKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034555165 928 YKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 964
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-760 |
1.30e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 230 AEIYVEEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDI 309
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 310 DAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKNEGENLKRDNAitsgmvsSLQKDILAKDEQVQQLKEEVSH 389
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAE-AELAEAEEELEELAEELLEALRAAA-------ELAAQLEELEEAEEALLERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 390 LKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLRE 469
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 470 KSKLEHFRSQVIKATYGRAKPFR----------DKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTEN 539
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGlagavavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 540 IEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILpsspnkgfs 619
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--------- 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 620 lyliyllehyKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQ 699
Cdd:COG1196 650 ----------TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 700 ERNRAKETLEEERKRMQELESLLAQQKKALAksITQEKNRVKEALEEEQTRVQELEERLAR 760
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEE--EALEELPEPPDLEELERELERLEREIEA 778
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
36-174 |
1.41e-08 |
|
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442679 [Multi-domain] Cd Length: 402 Bit Score: 59.00 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 36 TIGRHENSDLVLQSPD--IDNHHALIEYneAECSFVLQDfNSRNGTFVNECHI---QNVAVKLIPGDILRFGSagltYEL 110
Cdd:COG3456 29 TIGRSADCDWVLPDPDrsVSRRHAEIRF--RDGAFCLTD-LSTNGTFLNGSDHplgPGRPVRLRDGDRLRIGD----YEI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 111 V--IENPPPVSFPWMRGPAPWPGPQPPRATQQPNqAPPPshiPFHQGVQPAPMQRSWSQAFPRPTV 174
Cdd:COG3456 102 RveISGEDEGADDPLAAAPEPAVSSPSNLSDTEA-APDA---ALAFSFSLDPLEALDEAATEAPAT 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
663-1198 |
1.83e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 663 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyiTQERNRAKETLEEERKRMQElesllAQQKKALAKSITQEKNRVKE 742
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 743 ALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALE--SEKRKVQDLENHLTQQK----EISESNIAYEKRKAKEAM 816
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKkkadELKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 817 EKEKKKVQDLENRLTKQKEELELKEQKEDvlNNKLSDALAMVEETQKT-----KATESLKAESLALKLNETLAELETTKT 891
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 892 KMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQ-----HAQTIVSLEEKlQKVTQHHKKIEGEIATLKDN 966
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkKAEELKKAEEK-KKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 967 DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDLRGELNEKQKMELEQN 1046
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1047 VVLVQQQSKElsvlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFS 1126
Cdd:PTZ00121 1661 IKAAEEAKKA----EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555165 1127 SSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKA--RSPDHKDHQNESFLDLKNLRMENNVQKI 1198
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| FHA_Cep170A |
cd22724 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ... |
37-102 |
2.36e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438776 [Multi-domain] Cd Length: 106 Bit Score: 53.44 E-value: 2.36e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555165 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHI-QNVAVKLIPGDILRFG 102
Cdd:cd22724 25 VGR-DDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIpEQTYITLKLDDKLRFG 90
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
599-1387 |
2.51e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.83 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 599 EVEQLLRDLGILPSSPN-------------------------KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSL 653
Cdd:pfam02463 120 EVAELLESQGISPEAYNflvqggkieiiammkperrleieeeAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 654 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSI 733
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 734 TQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAK 813
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 814 EAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMV-----------------EETQKTKATESLKAESLA 876
Cdd:pfam02463 360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEkeaqlllelarqledllKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 877 LKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE---QESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 953
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKEtqlVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 954 KKIEGEIATLKDNDPAP-KEERPQDPLVAPMTESSAK---DMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMS 1029
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATadeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1030 DLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQ 1109
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1110 TCDTSVQIEpVHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNL 1189
Cdd:pfam02463 680 ELQEKAESE-LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1190 RMENNVQKILLDAKPDLPTLSRIEILAPQNGLCNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHV 1269
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1270 SMKYLSRQEREKVNQLRQRDLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIE----MYQSQVAKLEDDIYKE 1345
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEkkelEEESQKLNLLEEKENE 918
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1034555165 1346 AEEKALLKEALERMEHQLCQEKRINRAIRQQKMRKLRLRELR 1387
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE 960
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
32-109 |
2.66e-08 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438722 [Multi-domain] Cd Length: 105 Bit Score: 53.00 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 32 NKSTTIGRHENSDLVLQSPDIDNHHALIE---YNEAECSFV-LQDfNSRNGTFVNECHI-QNVAVKLIPGDILRF-GSAG 105
Cdd:cd22670 21 NQVITIGRSPSCDIVINDPFVSRTHCRIYsvqFDESSAPLVyVED-LSSNGTYLNGKLIgRNNTVLLSDGDVIEIaHSAT 99
|
....
gi 1034555165 106 LTYE 109
Cdd:cd22670 100 FVYV 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-1377 |
2.93e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 642 KFNSSQETQQSLLQEKLREHLAEKeKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESL 721
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKK-KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 722 LAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEAL--ESEKRKVQDLENHLTQQKe 799
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKkdAEEAKKAEEERNNEEIRK- 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 800 ISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELElkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLALKL 879
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA-----------KKAEEKKKADEAKK-KAEEAKKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 880 NETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEyKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGE 959
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 960 IATLKDNDPAPKEERPQDPLVAPMTESSAKDMAyehliddllaaqKEILSQQEVIMKLRKDLTEAhSRMSDLRGELNEKQ 1039
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEA------------KKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1040 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1119
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1120 VHT-----EAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRMENN 1194
Cdd:PTZ00121 1551 LKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1195 VQKILLDAKPDLPTlsrieilapqnglcNARFGSAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYL 1274
Cdd:PTZ00121 1631 EKKKVEQLKKKEAE--------------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1275 SRQEREKVNQLRQRDLDLVfDKITQLKNQ----LGRKEELLRGYEKDVEQLRRSKVSiEMYQSQVAKLEDDIYKEAEEKA 1350
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEK-KKAEELKKAeeenKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIR 1774
|
730 740
....*....|....*....|....*..
gi 1034555165 1351 LLKEALERMEHQLCQEKRINRAIRQQK 1377
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
656-1167 |
3.00e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEEKLKA--KIRQLTEEKAALEEYITQERNRAKETLE--EERKRMQELESLLAQQKKALAK 731
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKadAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 732 SITQEKNRVKEA---LEEEQTRVQELEERLARQKEVLESSI-AHEKRKAKEALE--SEKRKVQDLENHLTQQKEISESNI 805
Cdd:PTZ00121 1385 KKAEEKKKADEAkkkAEEDKKKADELKKAAAAKKKADEAKKkAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 806 AYEkrkakeamekekkkvqdlENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT-----KATESLKAESlALKLN 880
Cdd:PTZ00121 1465 KAE------------------EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAaeakkKADEAKKAEE-AKKAD 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 881 ETLAELETTKTKMIMVEERLILQQKMVKAlqdeqESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQhhKKIEGEI 960
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKA-----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVM 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 961 ATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEvimKLRKDLTEAHSRMSDL-RGELNEKQ 1039
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEaKKAEEDKK 1675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1040 KMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEP 1119
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034555165 1120 VHTEAFSSSQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKEL 1167
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
656-1188 |
3.83e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQ 735
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE--LEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 736 EKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKakea 815
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIE-----ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL---- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 816 mekekkkvQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMIM 895
Cdd:PRK03918 310 --------REIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 896 VEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEER 974
Cdd:PRK03918 357 LEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 975 PQDPLV-APMTESSAKDMAYEHLIdDLLAAQKEILSQQEVIMKLRKDLTEAH---------SRMSDLRGELNEKQKMELE 1044
Cdd:PRK03918 436 GKCPVCgRELTEEHRKELLEEYTA-ELKRIEKELKEIEEKERKLRKELRELEkvlkkeselIKLKELAEQLKELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1045 QNVVLVQQQSKELSVLKEKMAQMS---SLVEKKDRELKALEEALRA------SQEKHRLQLNTEKEQKPRKKTQTCDTSV 1115
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKgeiKSLKKELEKLEELKKKLAElekkldELEEELAELLKELEELGFESVEELEERL 594
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 1116 Q-IEPVHTEAFSSSQEQQSFSDLGVRCKGSRHE-----EVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKN 1188
Cdd:PRK03918 595 KeLEPFYNEYLELKDAEKELEREEKELKKLEEEldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
|
| FHA_Cep170B |
cd22725 |
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ... |
37-110 |
4.24e-08 |
|
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438777 [Multi-domain] Cd Length: 106 Bit Score: 52.62 E-value: 4.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555165 37 IGRhENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQN---VAVKLipGDILRFGSAGLTYEL 110
Cdd:cd22725 25 VGR-EDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDqkyITLKL--NDVIRFGYDSNMYVL 98
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
34-102 |
5.22e-08 |
|
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438746 [Multi-domain] Cd Length: 93 Bit Score: 51.94 E-value: 5.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFG 102
Cdd:cd22694 17 SVRIGRDPDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ--QVKLSDGTRVRLG 81
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
30-103 |
6.25e-08 |
|
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438730 [Multi-domain] Cd Length: 102 Bit Score: 51.98 E-value: 6.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 30 VLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVN--ECHIQNVAVKLIPGDILRFGS 103
Cdd:cd22678 20 GTRLPLTIGRIQRGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNgeSISPNGRPVVLSSGDVITLGS 95
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
238-1103 |
9.56e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 238 LAQQDKDEIILLL-GKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKeisqkcQVLDEDIDAKQKEI 316
Cdd:pfam02463 138 LVQGGKIEIIAMMkPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL------QELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 317 QSLKSQISALQKGYSKV-----LCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEvsHLK 391
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 392 SQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRaelRKSCTEQSVISRTLREKS 471
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 472 KLEHfRSQVIKATYGRAKPFRDKPVTDQQLI-----EKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTS 546
Cdd:pfam02463 367 KLEQ-LEEELLAKKKLESERLSSAAKLKEEElelksEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 547 LDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEV--EQLLRDLGILPSSPNKGFSLYLIY 624
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkESKARSGLKVLLALIKDGVGGRII 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 625 LLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA 704
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 705 KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEK 784
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 785 RKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKT 864
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 865 KATESLKAESLALKLNETLAEL--ETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSL 942
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKveEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 943 EEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLT 1022
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1023 EAHSRMSDLR------------GELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1090
Cdd:pfam02463 926 EAEILLKYEEepeellleeadeKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1034555165 1091 KHRLQLNTEKEQK 1103
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
622-937 |
1.00e-07 |
|
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: 56.67 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 622 LIYLLEHYKKLMSQAQelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKA--ALEEYITQ 699
Cdd:pfam17380 274 LLHIVQHQKAVSERQQ---------QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 700 ERNRAKETL-EEERKR----------------MQELESLLA--QQKKALAKSITQEKNRVKEALEEEQTRVQELEERLAR 760
Cdd:pfam17380 345 ERERELERIrQEERKRelerirqeeiameisrMRELERLQMerQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 761 QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAmekekkkvqDLENRLTKQKEELELK 840
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL---------EKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 841 EQKEDVLNNKLsdalAMVEETQKTKATE-SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRH 919
Cdd:pfam17380 496 ILEKELEERKQ----AMIEEERKRKLLEkEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
330
....*....|....*....
gi 1034555165 920 GFEEEIM-EYKEQIKQHAQ 937
Cdd:pfam17380 572 EREREMMrQIVESEKARAE 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
654-964 |
1.06e-07 |
|
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: 57.00 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 654 LQEKLREHLAEKEKLNEERLE-------QEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELESLLAQQK 726
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKaeryqalLKEKREYEGYELLKEKEALERQKEAIERQL-ASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 727 KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISES--N 804
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREieE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 805 IAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLA 884
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 885 ELETTKTKMIMVEERLilqqkmvKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLK 964
Cdd:TIGR02169 428 AIAGIEAKINELEEEK-------EDKALEIKKQ----EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
663-1085 |
1.12e-07 |
|
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: 57.00 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 663 AEKEKLNEErLEQEEKLKAKIRQLTEEKAALEEYITQERNRAkETLEEERKRMQELE-SLLAQQKKALAKSITQEKNRVk 741
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEgYELLKEKEALERQKEAIERQL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 742 EALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRkakeamekekk 821
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER----------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 822 KVQDLENRLTKQKEELELKEQKEDVLNNKLsdalamvEETQKTKATESLKAESLALKLNETLAELETTKTKMimveerli 901
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF-------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 902 lqqkmvKALQDEQESQRhgfeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLva 981
Cdd:TIGR02169 381 ------AETRDELKDYR----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL-- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 982 pmtESSAKDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLrgelnEKQKMELEQNVVLVQQQSKEL-SVL 1060
Cdd:TIGR02169 449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-----EAQARASEERVRGGRAVEEVLkASI 520
|
410 420
....*....|....*....|....*
gi 1034555165 1061 KEKMAQMSSLVEKKDRELKALEEAL 1085
Cdd:TIGR02169 521 QGVHGTVAQLGSVGERYATAIEVAA 545
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
6-103 |
1.55e-07 |
|
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438738 [Multi-domain] Cd Length: 123 Bit Score: 51.51 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 6 PCRLFIYGKTERMKAylksaeG--FFVLNKSTTIGRHENSDLVLQSPD--IDNHHALIEYNEAECSFVLQDFNSRNGTFV 81
Cdd:cd22686 3 PCIRVIVVESPSLQV------GslFIVTATGATIGREKDHGHTIRIPElgVSKFHAEIYYDDDEQSYTIVDLGSQNGTYL 76
|
90 100
....*....|....*....|....*..
gi 1034555165 82 NECHIQNVAVKLIP-----GDILRFGS 103
Cdd:cd22686 77 NGVRISQPKEKSDPyplthGDELKIGE 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
235-949 |
1.63e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKC--------QVLD 306
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELeklqekleQLEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 307 EDIDAKQKEIQSLKSQISALQKGYSKVLcQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEE 386
Cdd:pfam02463 374 ELLAKKKLESERLSSAAKLKEEELELKS-EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 387 VSHLKSQNKDKDHQLEalgsrcsvlkeelKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRT 466
Cdd:pfam02463 453 LEKQELKLLKDELELK-------------KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 467 LREKSKLEH---FRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKL 543
Cdd:pfam02463 520 VGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 544 RTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVV-----LDVLRHALSWLEEVEQLLRDLGILPSSPNKGF 618
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKakesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 619 SLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKL---KAKIRQLTEEKAALEE 695
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKK 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 696 YITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRvKEALEEEQTRVQELEERLARQKEVLESSIAHEKRK 775
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 776 AKEALESEKRKVQDLEnHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDAL 855
Cdd:pfam02463 839 ALELKEEQKLEKLAEE-ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 856 AMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQH 935
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
730
....*....|....
gi 1034555165 936 AQTIVSLEEKLQKV 949
Cdd:pfam02463 998 ERLEEEKKKLIRAI 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
271-797 |
3.66e-07 |
|
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: 55.03 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 271 IANLQNEVAELSQKVSETTTSRQNEKEisqKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVlcQTLSERN----SEIT 346
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNL--KKKIQKNksleSQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 347 SLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELRE 426
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 427 AQEKE--LKLCKTQIQDMEKEMKKLRAELRKScteQSVISRTLREKSKLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEK 504
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQN---NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 505 ITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDScqacmkisccshdLKKEVDLLQHLQVSppvsglQK 584
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-------------LEKEIERLKETIIK------NN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 585 VVLDVLRHALSwleEVEQLLRDLGILPSSPNKGFSLYLIylleHYKKLMSQAQELQIKFNSSQETQQSLLQEK--LREHL 662
Cdd:TIGR04523 440 SEIKDLTNQDS---VKELIIKNLDNTRESLETQLKVLSR----SINKIKQNLEQKQKELKSKEKELKKLNEEKkeLEEKV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 663 AEKEKLNEERLEQEEKLKAKIRQLTEEKAALE-EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVK 741
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 742 EALEEEQTRVQELEErlarqKEVLESSIAHEKRKAK---EALESEKRKVQDLENHLTQQ 797
Cdd:TIGR04523 593 QKEKEKKDLIKEIEE-----KEKKISSLEKELEKAKkenEKLSSIIKNIKSKKNKLKQE 646
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
235-913 |
3.99e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAElsqKVSETTTSRQNEKEISQKCQVLDEDIDAKQK 314
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE---ILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 315 EIQSLKSQISALQKGYSKVLCQTlsERNSEITSLKNEGENLKRDNAITSGMVsslqKDILAKDEQVQQLKEEVSHLKSQN 394
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQE--QLELLLSRQKLEERSQKESKARSGLKV----LLALIKDGVGGRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 395 KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQI------------QDMEKEMKKLRAELRKSCTEQSV 462
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLrllipklklplkSIAVLEIDPILNLAQLDKATLEA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 463 ISRTLREKSKLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLqKETQLSNSKQEETTENIEK 542
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL-LEIQELQEKAESELAKEEI 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 543 LRTSLDSCQACMKISCCSHDLKKEVDLLQhLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYL 622
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELL-ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 623 IYLLEHYKKLMSQAQELQIKfnssqetQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERN 702
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 703 RAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarQKEVLESSIAHEKRKAKEALES 782
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK----ELEEESQKLNLLEEKENEIEER 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 783 EKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQ 862
Cdd:pfam02463 923 IKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 863 KTKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 913
Cdd:pfam02463 1003 EKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
|
|
| FHA_SNIP1_DDL-like |
cd22676 |
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ... |
37-102 |
4.44e-07 |
|
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438728 [Multi-domain] Cd Length: 111 Bit Score: 49.99 E-value: 4.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 37 IGRHE-NSDLVLQSPDIDNHHALIEY-----------NEAECSFVLqDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22676 25 IGRDRrVADIPLDHPSCSKQHAVIQFrevekrnegdvIENIRPYII-DLGSTNGTFLNGEKIEpRRYYELREKDVLKFG 102
|
|
| VI_FHA |
TIGR03354 |
type VI secretion system FHA domain protein; Members of this protein family are FHA ... |
36-202 |
4.60e-07 |
|
type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274537 [Multi-domain] Cd Length: 396 Bit Score: 53.91 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 36 TIGRHENSDLVLQSPD--IDNHHALIEYNEAecSFVLQDFnSRNGTFVNECH---IQNVAVKLIPGDILRFGSagltYEL 110
Cdd:TIGR03354 27 TIGRSEDCDWVLPDPErhVSGRHARIRYRDG--AYLLTDL-STNGVFLNGSGsplGRGNPVRLEQGDRLRLGD----YEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 111 VIENPPPVSFPWMRGPAPWPGPQPPRATQQPNQAPPPSHIPF----HQGVQPAPMQRSWSQAFPRPTVVLPAsHRRPVSA 186
Cdd:TIGR03354 100 RVSLGDPLVSRQASESRADTSLPTAGGPPTPDPAPLAQLDPLkaldQEPLSAADLDDLSAPLFPPLDARLPA-FAAPIDA 178
|
170
....*....|....*.
gi 1034555165 187 NKEMFSFVVDDARKPP 202
Cdd:TIGR03354 179 EPTMVPPFVPLPAPEP 194
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
8-109 |
6.85e-07 |
|
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438750 [Multi-domain] Cd Length: 93 Bit Score: 48.95 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 8 RLFIYGKTERMKAYLKSAEgffvlnksTTIGRHENSDLVLQSPDIDNHHALIEYNEAECsfVLQDFNSRNGTFVNECHIQ 87
Cdd:cd22698 4 LIEQKGSEEGKDYELDQDE--------FTIGRSSNNDIRLNDHSVSRHHARIVRQGDKC--NLTDLGSTNGTFLNGIRVG 73
|
90 100
....*....|....*....|..
gi 1034555165 88 NVAVKliPGDILRFGSAGLTYE 109
Cdd:cd22698 74 THELK--HGDRIQLGETIFRFI 93
|
|
| FHA_GarA_OdhI-like |
cd22684 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ... |
35-108 |
8.16e-07 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438736 [Multi-domain] Cd Length: 94 Bit Score: 48.53 E-value: 8.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555165 35 TTIGRHENSDLVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTY 108
Cdd:cd22684 23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGG--FVVRDVGSLNGTYVNRERID--SAVLRNGDEVQIGKFRLVF 92
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-480 |
1.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 235 EEDLAQQDKDEIILLLGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTT----SRQNEKEISQKCQVLDEDID 310
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 311 AKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHL 390
Cdd:TIGR02168 793 QLKEELKALREALDELRA--------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 391 KSQNKDKDHQLEALgsrcsvlkeeLKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLRE- 469
Cdd:TIGR02168 865 EELIEELESELEAL----------LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGl 934
|
250
....*....|.
gi 1034555165 470 KSKLEHFRSQV 480
Cdd:TIGR02168 935 EVRIDNLQERL 945
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
634-810 |
1.07e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 634 SQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA---KIRQLTEEKAALEEYI---TQERNRAKET 707
Cdd:COG4942 20 DAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELaelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 708 LEEERKRMQE-------------LESLLAQQ-------KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLES 767
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqppLALLLSPEdfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034555165 768 SIAhEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKR 810
Cdd:COG4942 179 LLA-ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-735 |
1.33e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 282 SQKVSETTTSRQNE-KEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqtlsernsEITSLKNEGENLKRDna 360
Cdd:TIGR02168 665 SAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEE---------------ELEQLRKELEELSRQ-- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 361 itsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAqekelklcktQIQ 440
Cdd:TIGR02168 728 -----ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA----------QIE 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 441 DMEKEMKKLRAELRKscteqsvisrtlreksklehFRSQVikatygrakpfrdkpvtdQQLIEKITQVTEDNINFQQKKW 520
Cdd:TIGR02168 793 QLKEELKALREALDE--------------------LRAEL------------------TLLNEEAANLRERLESLERRIA 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 521 TLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKisccshDLKKEVDLLQHLQVSppvsglQKVVLDVLRHAlswLEEV 600
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIE------ELESELEALLNERAS------LEEALALLRSE---LEEL 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 601 EQLLRDLGilpsspnkgfslyliyllEHYKKLMSQAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKLN-EERLEQEE 677
Cdd:TIGR02168 900 SEELRELE------------------SKRSELRRELEELREKLAQLELRLEGLEVRidNLQERLSEEYSLTlEEAEALEN 961
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 678 KLKAKIRQLTEEKAALEEYITQERN---RAKETLEEERKRMQELEsllaQQKKALAKSITQ 735
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPvnlAAIEEYEELKERYDFLT----AQKEDLTEAKET 1018
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
647-805 |
1.41e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 647 QETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQ----ELESLL 722
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEreleERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 723 AQQKKALAkSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSiAHEKRKAKEALESEKRKVQDLENHLTQQKeise 802
Cdd:COG4913 362 ARLEALLA-ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-LAEAEAALRDLRRELRELEAEIASLERRK---- 435
|
...
gi 1034555165 803 SNI 805
Cdd:COG4913 436 SNI 438
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
376-966 |
1.44e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 376 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK-------EELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKK 448
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaeearkaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 449 LRaELRKSCTEQSVISRTLREKSKLEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQL 528
Cdd:PTZ00121 1317 AD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 529 SNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVlRHALSWLEEVEQLLRDLG 608
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAKKADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 609 ILPSSPNKGFSLYLIYLLEHYKKlmsQAQELQIKFNSSQETQQSLLQEklrehlaEKEKLNEERLEQEEKLKAKIRQLTE 688
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKK---KADEAKKAAEAKKKADEAKKAE-------EAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 689 EKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSItqEKNRVKEALEEEQTRVQELEERLARQKEvlESS 768
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEE--AKI 1620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 769 IAHEKRKAKEalesEKRKVQDLENHLTQQKEISES-NIAYEKRKAKEAMEKEKkkvQDLENRLTKQKEELELKEQKEDVL 847
Cdd:PTZ00121 1621 KAEELKKAEE----EKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEKKAAEA 1693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 848 NNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKmimVEERlilQQKMVKALQDEQESQRHGFEEEIME 927
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEED---KKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
570 580 590
....*....|....*....|....*....|....*....
gi 1034555165 928 YKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 966
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
665-1360 |
1.76e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 665 KEKLNEERLEQ-EEKLKAKIRQLTEEKAALEEYITQERNrAKETLEEERKRMQELESLLaqqkkalaKSITQEKNRVKEA 743
Cdd:PRK03918 152 RQILGLDDYENaYKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKEKEKELEEVLREI--------NEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 744 LEEEQTRVQELEER------LARQKEVLESSIAHEKRKAKE---ALESEKRKVQDLENHLTQQKEISESNIAYEKrkAKE 814
Cdd:PRK03918 223 LEKLEKEVKELEELkeeieeLEKELESLEGSKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIK--LSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 815 AMEKEKKKVQDLENRLTkqkeelelkeqkedvlnnKLSDALAMVEETQKtkateslKAESLALKLNETLAELETTKTKMI 894
Cdd:PRK03918 301 FYEEYLDELREIEKRLS------------------RLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 895 MVEERLILQQkMVKALQDEQESQRHGFE-EEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEE 973
Cdd:PRK03918 356 ELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 974 RPQDPLV-APMTESSAKDMAYEHLIDdllaaqkeilsqqevIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQnvvlvqq 1052
Cdd:PRK03918 435 KGKCPVCgRELTEEHRKELLEEYTAE---------------LKRIEKELKEIEEKERKLRKELRELEKVLKKE------- 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1053 qsKELSVLKEKMAQMSSLVEK-KDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQtcdtsvqiepvhteafsssqeq 1131
Cdd:PRK03918 493 --SELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL---------------------- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1132 qsfsdlgvrckgsrheEVIQRQKKALSELRARIKELEKARSPDHKDHQNESFLDLKNLRmennvqkilldakpdlptlSR 1211
Cdd:PRK03918 549 ----------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-------------------ER 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1212 IEILAPQNGLCNARFGSAMEKSGKMDVAEALELS-EKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQ--R 1288
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsR 673
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555165 1289 DLDLVFDKITQLKNQLGRKEELLRGYEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKE-ALERME 1360
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKErALSKVG 746
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-770 |
2.76e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 427 AQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQVIKATYGRAKPFRDKpvtDQQLIEKIT 506
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE---VEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 507 QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHD-LKKEVDLLQ--HLQVSPPVSGLQ 583
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDeLRAELTLLNeeAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 584 KVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQELQIKFNSSQE------TQQSLLQEK 657
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEE--------LEELIEELESELEALLNERASLEEalallrSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 658 LREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEK 737
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL-KRLENKI 981
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034555165 738 NRVK----EALEEeqtrVQELEER---LARQKEVLESSIA 770
Cdd:TIGR02168 982 KELGpvnlAAIEE----YEELKERydfLTAQKEDLTEAKE 1017
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
28-108 |
3.78e-06 |
|
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438719 [Multi-domain] Cd Length: 108 Bit Score: 46.94 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALI--EYNEAECSF-------VLQDFnSRNGTFVNECHIQNVA-VKLIPGD 97
Cdd:cd22667 15 YLLPGGEYTVGRKDCDIIIVDDSSISRKHATLtvLHPEANLSDpdtrpelTLKDL-SKYGTFVNGEKLKGGSeVTLKDGD 93
|
90
....*....|.
gi 1034555165 98 ILRFGSAGLTY 108
Cdd:cd22667 94 VITFGVLGSKF 104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-802 |
3.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKsCTEQSVISRTLREKSKLEHFRSQV---IKATYGR 487
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELperLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 488 AKPFRDKPVTDQQLIEKITQVTEDnINFQQKKWTLQKETQLSNSKQE---------ETTENIEKLRTSLDSCQACMKISC 558
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEE-LEELLEQLSLATEEELQDLAEEleelqqrlaELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 559 CSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILpsspnkgFSLYLIYLLEHYKKLMSQAQE 638
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL-------LALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 639 LQikfnsSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLteekaaleeyitQERNRAKETLEEERKRMQEL 718
Cdd:COG4717 307 LQ-----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL------------QELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 719 ESLLAQQKKALAKSITQ--EKNRVKEALEEEQTRVQELEERLARQ-KEVLESSIAHEKRKAKEALESEKRKVQDLENHLT 795
Cdd:COG4717 370 QEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELlGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
....*...
gi 1034555165 796 Q-QKEISE 802
Cdd:COG4717 450 ElREELAE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
660-1390 |
3.87e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 660 EHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 739
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 740 VKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKEAMEKE 819
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 820 KKKVQDLENRLTKQKEELELKEQKEdvlnnklsdalaMVEETQKTKATESLKAEslalklnetlaELETTKTKMIMVEER 899
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAH------------FARRQAAIKAEEARKAD-----------ELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 900 LILQQKMVKALQDEQESQRHGfeEEIMEYKEQIKQHAqtivsleEKLQKVTQHHKKiegeiatlKDNDPAPKEERPQDPL 979
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKA-------DAAKKKAEEAKK--------AAEAAKAEAEAAADEA 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 980 VAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSV 1059
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1060 lKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGV 1139
Cdd:PTZ00121 1439 -KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1140 RCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKIlldakpdlptlsrieilapqn 1219
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKKA--------------------- 1566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1220 glcnarfgsAMEKSGKMDVAEALELSEKLYLDMSKTLGSLMNIKNMSGHVSMKYLSRQEREKVNQLRQRDLDLVFDKITQ 1299
Cdd:PTZ00121 1567 ---------EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1300 LKNQlgRKEEllrgyEKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEKRINRAIRQqkMR 1379
Cdd:PTZ00121 1638 LKKK--EAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE--LK 1708
|
730
....*....|.
gi 1034555165 1380 KLRLRELRGAQ 1390
Cdd:PTZ00121 1709 KKEAEEKKKAE 1719
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
438-746 |
4.59e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 438 QIQDMEKEMKKLRaeLRKSCTEQSVISRTLrekSKLEHFRSqvikatYGRAKPFRDKPVTDQQLiEKITQVTEDNINfqq 517
Cdd:PRK05771 32 HIEDLKEELSNER--LRKLRSLLTKLSEAL---DKLRSYLP------KLNPLREEKKKVSVKSL-EELIKDVEEELE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 518 kkwTLQKETqlsnskqEETTENIEKLRTSLDSCQAcmkisccshdLKKEVDLLQHLqvSPPVSGLQ-----KVVLDVLRH 592
Cdd:PRK05771 97 ---KIEKEI-------KELEEEISELENEIKELEQ----------EIERLEPWGNF--DLDLSLLLgfkyvSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 593 ALswLEEVEQLLRDLGILPSSPNKGFSLY-LIYLLEHYKKLMSQAQELQIKFNSSQEtqQSLLQEKLREHLAEKEKLNEE 671
Cdd:PRK05771 155 DK--LEELKLESDVENVEYISTDKGYVYVvVVVLKELSDEVEEELKKLGFERLELEE--EGTPSELIREIKEELEEIEKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 672 RLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK---ETLEEER----------KRMQELESLLaqqKKALAKSITQEKN 738
Cdd:PRK05771 231 RESLLEELKELAKKYLEELLALYEYLEIELERAEalsKFLKTDKtfaiegwvpeDRVKKLKELI---DKATGGSAYVEFV 307
|
....*...
gi 1034555165 739 RVKEALEE 746
Cdd:PRK05771 308 EPDEEEEE 315
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
624-756 |
5.32e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 624 YLLEHYKKLMSQAQElqiKFN---SSQETQQSLLQEKLREH---LAEKEKLNEERLEQEEKLKAKIRQLteeKAALEEYI 697
Cdd:PRK00409 502 NIIEEAKKLIGEDKE---KLNeliASLEELERELEQKAEEAealLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEA 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 698 TQERNRAKETLEEERKRMQELESLLAQQKKalAKSITQEKNRVKEALEEEQTRVQELEE 756
Cdd:PRK00409 576 QQAIKEAKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
30-102 |
6.01e-06 |
|
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438731 [Multi-domain] Cd Length: 126 Bit Score: 46.88 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 30 VLNKSTTIGRHEN------SDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQ-----NVAVKLIPGDI 98
Cdd:cd22679 21 VLDEPVKIGRSVArarpaaNNAIFDCKVLSRNHALLWYDDG--KFYLQDTKSSNGTFVNNQRLSkgseeSEPRELHSGDI 98
|
....
gi 1034555165 99 LRFG 102
Cdd:cd22679 99 VQFG 102
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
635-807 |
6.94e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.46 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 635 QAQELQIKFnSSQETQQSllqEKLrehLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKR 714
Cdd:PRK11637 138 EHTGLQLIL-SGEESQRG---ERI---LAYFGYLNQARQETIAELKQTREELAAQKAELE----EKQSQQKTLLYEQQAQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 715 MQELESLLAQQKKALAKsitqeknrVKEALEEEQTRVQELeerlaRQKEV-LESSIAHEKRKAKEALESEKRKVQDLENh 793
Cdd:PRK11637 207 QQKLEQARNERKKTLTG--------LESSLQKDQQQLSEL-----RANESrLRDSIARAEREAKARAEREAREAARVRD- 272
|
170
....*....|....
gi 1034555165 794 ltQQKEISESNIAY 807
Cdd:PRK11637 273 --KQKQAKRKGSTY 284
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-802 |
8.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 252 KEVSRLSDYEIESKykdviiaNLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYS 331
Cdd:PRK03918 152 RQILGLDDYENAYK-------NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 332 KVlcqtlSERNSEITSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDhQLEALGSRCSVL 411
Cdd:PRK03918 225 KL-----EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 412 KEELKQ-EDAHRELreaqEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLE--HFRSQVIKATYGRA 488
Cdd:PRK03918 299 SEFYEEyLDELREI----EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 489 KPFRDK--PVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQAC------------- 553
Cdd:PRK03918 375 ERLKKRltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgrelteehrkell 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 554 ----MKISCCSHDLKKEVDLLQHLQV-----------SPPVSGLQKVV--LDVLRHALS--WLEEVEQLLRDLGILPSSP 614
Cdd:PRK03918 455 eeytAELKRIEKELKEIEEKERKLRKelrelekvlkkESELIKLKELAeqLKELEEKLKkyNLEELEKKAEEYEKLKEKL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 615 N--KGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQ----------EKLREHLAEKEKLNEERLE---QEEKL 679
Cdd:PRK03918 535 IklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesvEELEERLKELEPFYNEYLElkdAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 680 KAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELESLLAQQKKalaksitQEKNRVKEALEEEQTRVQELEERLA 759
Cdd:PRK03918 615 EREEKELKKLEEELDK-AFEELAETEKRLEELRKELEELEKKYSEEEY-------EELREEYLELSRELAGLRAELEELE 686
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1034555165 760 RQKEVLESSIAHEKRKaKEALESEKRKVQDLENHLTQQKEISE 802
Cdd:PRK03918 687 KRREEIKKTLEKLKEE-LEEREKAKKELEKLEKALERVEELRE 728
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
648-1108 |
1.21e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLLQEKLREHLAEKE------KLNEerLEQEEK-LKAKIRQLTEEKaaleEYITQERNRAKETLEEERKRMQELES 720
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEekdlheRLNG--LESELAeLDEEIERYEEQR----EQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 721 LLAQQKKALAKSITQEKNR--VKEALEEEQTRVQELEERL--ARQKEVLESSIAHEKRKAKEALESEKRKVQD-LENHLT 795
Cdd:PRK02224 256 LEAEIEDLRETIAETEREReeLAEEVRDLRERLEELEEERddLLAEAGLDDADAEAVEARREELEDRDEELRDrLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 796 QQKEISESNIAYEKRKAKEAM--EKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVE--ETQKTKATESLk 871
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEEraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFL- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 872 aESLALKLNETLAELETTKTKMIMVEERLilqqKMVKALQDE-------QESQRHGFEEEIMEYKEQIKQHAQTIVSLEE 944
Cdd:PRK02224 415 -EELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 945 KLQKVTQHH------KKIEGEIATLKDNdpapkeerpqdplvapmtessakdmayEHLIDDLLAAQKEIL-SQQEVIMKL 1017
Cdd:PRK02224 490 EVEEVEERLeraedlVEAEDRIERLEER---------------------------REDLEELIAERRETIeEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1018 RKDLTEAHSRMSDLRgELNEKQKMELEQNVVLVQQQSKELSVLKE------KMAQMSSLVEKKDRELKALEEALRASQEK 1091
Cdd:PRK02224 543 RERAAELEAEAEEKR-EAAAEAEEEAEEAREEVAELNSKLAELKEriesleRIRTLLAAIADAEDEIERLREKREALAEL 621
|
490
....*....|....*..
gi 1034555165 1092 HRLQLNTEKEQKPRKKT 1108
Cdd:PRK02224 622 NDERRERLAEKRERKRE 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-789 |
1.37e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 370 QKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEK--ELKLCKTQIQDMEKEMK 447
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 448 KLRAELRKsctEQSVISRTLREKSKLEHFRSQVIKATYGRAKpfrdkpvTDQQLIEKITQVTEDNINFQQKKWTLQKETQ 527
Cdd:COG4717 167 ELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQ-------QRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 528 LSNSKQEETTENIEKLR-------------TSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHAL 594
Cdd:COG4717 237 EAAALEERLKEARLLLLiaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 595 SwLEEVEQLLRDLGiLPSSPNKGFSLYLIYLLEHYKKLMSQAQELQikfnssQETQQSLLQEKLREHLAEKEKLNEERLE 674
Cdd:COG4717 317 E-EEELEELLAALG-LPPDLSPEELLELLDRIEELQELLREAEELE------EELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 675 QEEKLKAKIRQLTEEKAALEEYITQERNRA--------KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEAleE 746
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELeellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQL--E 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034555165 747 EQTRVQELEERLARQKEVLEsSIAHE---KRKAKEALESEKRKVQD 789
Cdd:COG4717 467 EDGELAELLQELEELKAELR-ELAEEwaaLKLALELLEEAREEYRE 511
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
29-102 |
1.45e-05 |
|
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438732 [Multi-domain] Cd Length: 96 Bit Score: 45.02 E-value: 1.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555165 29 FVLNKST-TIGRHENSDLVLQSPDIDNHHALIeYNEaECSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFG 102
Cdd:cd22680 16 FPFDFSSvSIGRDPENVIVIPDPFVSRNHARI-TVD-SNEIYIEDLGSTNGTFVNDFKRIKGPAKLHPNDIIKLG 88
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
36-103 |
1.55e-05 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 44.94 E-value: 1.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555165 36 TIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQNVAVKLIPGDILRFGS 103
Cdd:pfam16697 20 RIGSDPDCDIVLSDKEVSRVHLKLEVDDE--GWRLDDLGSGNGTLVNGQRVTELGIALRPGDRIELGQ 85
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
622-1090 |
1.75e-05 |
|
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: 49.63 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 622 LIYLLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYiTQER 701
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKK-QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 702 NRAKETLEEERKRMQELESLLAQQKKALAKSITQEknrVKEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALE 781
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQNQISQNNKIIS--------QLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 782 SEKRKVQDLEN-HLTQQKEISESNIAYEKrkAKEAMEKEKKKVQDLENRLTkqkeELELKEQKEDVLNNKLSDALAMVEE 860
Cdd:TIGR04523 346 QLKKELTNSESeNSEKQRELEEKQNEIEK--LKKENQSYKQEIKNLESQIN----DLESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 861 TQKTKATESLKAESLALKLNETLAELETTKTKmimveerLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIV 940
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 941 SLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDL----LAAQKEILSQQEVIMK 1016
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKEIDEKNKEIEE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1017 LRKDLTEAHSRMSDLRGELNEKQK------MELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKALEEALRASQE 1090
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKekkdliKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
32-104 |
2.05e-05 |
|
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438754 [Multi-domain] Cd Length: 123 Bit Score: 45.49 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 32 NKSTTIGR--HENSD---LVLQSPDIDNHHALIEYNEAEcsFVLQDFNSRNGTFVNECHIQ------NVAVKLIPGDILR 100
Cdd:cd22702 31 KQPCIIGSdpHQAISgisVVIPSPQVSELHARITCKNGA--FFLTDLGSEHGTWINDNEGRryrappNFPVRLHPSDVIE 108
|
....
gi 1034555165 101 FGSA 104
Cdd:cd22702 109 FGSD 112
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
666-953 |
2.33e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 666 EKLNEERLEQEEKLKAKiRQLTEEKaaLEEYITQERNRAKETLEEERKRMQELESL--LAQQKKALAKSITQEKNRVKEA 743
Cdd:PLN02939 106 EAIAAIDNEQQTNSKDG-EQLSDFQ--LEDLVGMIQNAEKNILLLNQARLQALEDLekILTEKEALQGKINILEMRLSET 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 744 LE------EEQTRVQELEERLAR------QKEVLESSIAHEKRKAKEALESE----KRKVQDLENHLTQQKEISESNIAY 807
Cdd:PLN02939 183 DAriklaaQEKIHVEILEEQLEKlrnellIRGATEGLCVHSLSKELDVLKEEnmllKDDIQFLKAELIEVAETEERVFKL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 808 EKrkakeAMEKEKKKVQDLENRLTKQKEelelkeqkeDVLnnKLS----DAL-AMVEETQKTKATESLKAESLAL----- 877
Cdd:PLN02939 263 EK-----ERSLLDASLRELESKFIVAQE---------DVS--KLSplqyDCWwEKVENLQDLLDRATNQVEKAALvldqn 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 878 --------KLNETLAELETTKTKMIMVEerlILQQKMvKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKV 949
Cdd:PLN02939 327 qdlrdkvdKLEASLKEANVSKFSSYKVE---LLQQKL-KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
....
gi 1034555165 950 TQHH 953
Cdd:PLN02939 403 SLEH 406
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
622-1109 |
2.39e-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: 48.95 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 622 LIYLLEHYKKLMSQAQElQIKFNSSQETQQSLLQEKLREHLA------EKEKLNEERLEQEEKLKAK-IRQLTEEKAALE 694
Cdd:pfam05483 259 LTFLLEESRDKANQLEE-KTKLQDENLKELIEKKDHLTKELEdikmslQRSMSTQKALEEDLQIATKtICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 695 EYITQERNRAKETLEEERKRMQELESLLAQQKKALAKS------ITQEKNRVKEALEEEQTRVQELEERLARQKEVL--E 766
Cdd:pfam05483 338 EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILaeD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 767 SSIAHEKRKAKEALESEKRKVQDLeNHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDV 846
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQEL-IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 847 L---NNKLS-DALAMVEETQKTKA--TESLKAESLALKLNETLAELETT-KTKMIMVEERLILQQKMVKALQDEQESQRH 919
Cdd:pfam05483 497 LlleNKELTqEASDMTLELKKHQEdiINCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 920 GFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDNDPAPKEERPQDPLVAPMTE---SSAKDmAYEHL 996
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElelASAKQ-KFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 997 IDDLlaaQKEILSQQEVIMKLRKDLTEAHSRMSD---LRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEK 1073
Cdd:pfam05483 656 IDNY---QKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034555165 1074 KDRELKALEEAL-------RASQEKHRLQLNTEKEQKPRKKTQ 1109
Cdd:pfam05483 733 KEQEQSSAKAALeielsniKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-806 |
2.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 645 SSQETQQSLLQEKLREHLAEKEKLNEERleqeEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQE---- 717
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAeaeAEIEERREELGERARALYRsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 718 ----------------------LESLLAQQKKALA--KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEK 773
Cdd:COG3883 102 vsyldvllgsesfsdfldrlsaLSKIADADADLLEelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQ 180
|
170 180 190
....*....|....*....|....*....|...
gi 1034555165 774 RKAKEALESEKRKVQDLENHLTQQKEISESNIA 806
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-830 |
2.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 655 QEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernrakETLEEERKRMQELESLLAQQKKALAksIT 734
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL--------EELEAELEELREELEKLEKLLQLLP--LY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 735 QEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESEKRKVQDLENHLTQQKEISESNIAYEKRKAKE 814
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170
....*....|....*.
gi 1034555165 815 AMEKEKKKVQDLENRL 830
Cdd:COG4717 207 RLAELEEELEEAQEEL 222
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-500 |
3.86e-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: 47.84 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 271 IANLQNEVAELSQKVSETttsRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLKN 350
Cdd:COG4942 29 LEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIRALEQELAALE--------AELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 351 EgenLKRDNAITSGMVSSLQK-------DILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRE 423
Cdd:COG4942 98 E---LEAQKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555165 424 LREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSK-LEHFRSQVIKATYGRAKPFRDKPVTDQQ 500
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEeLEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
274-799 |
4.59e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 274 LQNEVAELSQKVSETTTSRQNEK--EISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQTLS---ERNSEITSL 348
Cdd:TIGR00618 272 LRAQEAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 349 KNEGENLKRDNAITSgmvsslqkdilaKDEQVQQLKEEVSHLKSQNKDKDH---QLEALGSRCSVLKEELKQEDAHRELR 425
Cdd:TIGR00618 352 SQEIHIRDAHEVATS------------IREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAF 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLRE-----KSKLEHFRS-QVIKATYGRAKPFRDKPVTDQ 499
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslKEREQQLQTkEQIHLQETRKKAVVLARLLEL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 500 QLIEKitQVTEDNINFQQKKwTLQKETQLSNSKQEETTENIEKLRTSLDSCQA-CMKISCCSHDLKKEVDLLQH------ 572
Cdd:TIGR00618 500 QEEPC--PLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHqLTSERKQRASLKEQMQEIQQsfsilt 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 573 ---LQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKklmsqAQELQIKFNSSQET 649
Cdd:TIGR00618 577 qcdNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC-----SQELALKLTALHAL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 650 QQSLLQEKLREHLA----EKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRaKETLEEERKRMQELESLLAQQ 725
Cdd:TIGR00618 652 QLTLTQERVREHALsirvLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSL 730
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 726 KKALAKSITQEKNRVKEALEEEQTRVQELEERLAR--QKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQKE 799
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnnEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA 806
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
630-802 |
7.11e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 630 KKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkirqltEEKAAleeyitQERNRAKETLE 709
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA------EEAAA------KAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 710 EERKRMQELESLLAQQKKALAKSITQEKN------------RVKEALEEEQTRVQELEER---LARQKEVLESSIAHEKR 774
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeakkkaeaeaAAKAAAEAKKKAEAEAKKKaaaEAKKKAAAEAKAAAAKA 230
|
170 180
....*....|....*....|....*...
gi 1034555165 775 KAKEALESEKRKVQDLENHLTQQKEISE 802
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
656-778 |
7.29e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHLAEKEKLNEERLEQEE-----KLKAKIRQLTEEKAALEEYITqernRAKETLEEERKRMQELESLLAQQKKALA 730
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEereltEEEEEIRRLEEQVERLEAEVE----ELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555165 731 KSITQEK---------NRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKE 778
Cdd:COG2433 459 REIRKDReisrldreiERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
34-106 |
8.60e-05 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438720 [Multi-domain] Cd Length: 91 Bit Score: 42.84 E-value: 8.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555165 34 STTIGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnVAVKLIPGDILRFGSAGL 106
Cdd:cd22668 19 SNIIGRGSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPVT-PEWRLADGDVITLGHSEI 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
664-1380 |
8.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 664 EKEKLNEERLEQeeklKAKIRQLTEEKAALEE--YITQERNRAKETLEEERKRMQELESLLA-----QQKKALAKSITQE 736
Cdd:PTZ00121 1051 DIDGNHEGKAEA----KAHVGQDEGLKPSYKDfdFDAKEDNRADEATEEAFGKAEEAKKTETgkaeeARKAEEAKKKAED 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 737 KNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKvqdlenHLTQQKEISESNIAYEKRKAKEAM 816
Cdd:PTZ00121 1127 ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEVRKAEELRKAEDAR 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 817 EKEKKKVQDLENRLTKQKEELELkeqkedvlnnKLSDALAMVEETQKtKATESLKAESLalKLNETLAELETTKTKMIMV 896
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDA----------KKAEAVKKAEEAKK-DAEEAKKAEEE--RNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 897 EERLILQQKMVKALQDEQESQRHGFEE----EIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIE-----GEIATLKDND 967
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 968 PAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEILSQQEViMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNV 1047
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1048 VLVQQQSKELSVlKEKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSS 1127
Cdd:PTZ00121 1427 AEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1128 SQEQQSFSDLGVRCKGSRHEEVIQRQKKALSELRARIKELEKArspdhkdhqnESFLDLKNLRMENNVQKilldakpdlp 1207
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA----------DELKKAEELKKAEEKKK---------- 1565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1208 tlsrieilAPQNGLCNARFGSAMEKSGKMDVAEALELSEklyldmsktlgslmniknmsghvSMKYLSRQEREKVNQLRQ 1287
Cdd:PTZ00121 1566 --------AEEAKKAEEDKNMALRKAEEAKKAEEARIEE-----------------------VMKLYEEEKKMKAEEAKK 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1288 RDLDlvfdkitQLKNQLGRKEELLRgyeKDVEQLRRSKVSIEMYQSQVAKLEDDIYKEAEEKALLKEALERMEHQLCQEK 1367
Cdd:PTZ00121 1615 AEEA-------KIKAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
730
....*....|...
gi 1034555165 1368 RINRAIRQQKMRK 1380
Cdd:PTZ00121 1685 EDEKKAAEALKKE 1697
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
275-794 |
1.01e-04 |
|
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: 47.35 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 275 QNEVAELSQKVSETTTSRQNEKEISQKCQvldEDIDAKQKEIQSLKS---QISALQKGYSKVLCQ-TLSERNSEITSLKN 350
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKKEILEKKQ---EELKFVIKELQQLEGssdRILELDQELRKAERElSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 351 EGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVShLKSQNKDKDHQLEALGSRCSvlkEELKQEDAHRELREAQEK 430
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIRKIKSRHS---DELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 431 ELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLR---------------------EKSKLEHFRSQVIKATYGRAk 489
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEskeeqlssyedklfdvcgsqdEESDLERLKEEIEKSSKQRA- 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 490 PFRDKPVTDQQLIEKIT-----------QVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISC 558
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 559 CSHDLK-KEVDLLQH--LQVSPPVSGLQKVVLD---VLRHALSWLEEVEQLLRDLGILpsspnKGFSLYLIYLLEHYKKL 632
Cdd:TIGR00606 737 SIIDLKeKEIPELRNklQKVNRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDVTIM-----ERFQMELKDVERKIAQQ 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 633 MSQAQELQIKFNSSQETQQSL-LQEKLREHLAEKE---KLNEERLEQEEKLKAKIRQLTEEKAALEEYItQERNRAKETL 708
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIElnrKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL-QRRQQFEEQL 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 709 EEERKRMQELESLLAQQKK---ALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKR 785
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD 970
|
....*....
gi 1034555165 786 KVQDLENHL 794
Cdd:TIGR00606 971 YLKQKETEL 979
|
|
| FHA_Slr1951-like |
cd22697 |
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ... |
36-109 |
1.07e-04 |
|
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438749 [Multi-domain] Cd Length: 102 Bit Score: 42.84 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 36 TIGRHENSDLVLQSPDIDNHHALIEY----NEAECSFVLQDF----NSRNGTFVNECHIQNVAvkLIPGDILRFG-SAGL 106
Cdd:cd22697 21 TIGRHPGNDIQIPSQQISRRHATLRRkinpNLDISFWIIDGDlegaESLNGLWVNGERILQHE--LVNGDEIALGpKIVL 98
|
...
gi 1034555165 107 TYE 109
Cdd:cd22697 99 RYQ 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
647-783 |
1.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 647 QETQQSLLQEKLREHLAEKEKLNEERLE----QEEKLKAKIRQLTEEKAALEeyitQERNRAKETLEE-ERKRMQELESL 721
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERE----RRRARLEALLAAlGLPLPASAEEF 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 722 LAQQK--KALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLE------SSIAHEKRKAKEALESE 783
Cdd:COG4913 383 AALRAeaAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrkSNIPARLLALRDALAEA 452
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
690-802 |
1.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 690 KAALEEYITQERNRAKETLEEERKRMQEL--ESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERLARQKEVLEs 767
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEAKEEIH-----KLRNEFEKELRERRNELQKLEKRLLQKEENLD- 99
|
90 100 110
....*....|....*....|....*....|....*
gi 1034555165 768 siahekrKAKEALESEKRKVQDLENHLTQQKEISE 802
Cdd:PRK12704 100 -------RKLELLEKREEELEKKEKELEQKQQELE 127
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
261-805 |
1.61e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 261 EIESKYKDVIiANLQNEVAELsQKVSETTTSRQNEKEISQKCQVLDEDIDAKQ---KEIQSLKSQISALQKGYSkvlcqT 337
Cdd:TIGR01612 1136 EIKKKSENYI-DEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKT-----S 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 338 LSE-RNSEITSLKNEG----ENLKRDNAITSGMVSSLQKDILAKDEqVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR01612 1209 LEEvKGINLSYGKNLGklflEKIDEEKKKSEHMIKAMEAYIEDLDE-IKEKSPEIENEMGIEMDIKAEMETFNISHDDDK 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 413 EELKQEDAHRE-LREAQEKELKLC-----KTQIQDMEKEMKKLRAELRKSCTEqsvISRTLREKSKLEH-FRSQVIKATY 485
Cdd:TIGR01612 1288 DHHIISKKHDEnISDIREKSLKIIedfseESDINDIKKELQKNLLDAQKHNSD---INLYLNEIANIYNiLKLNKIKKII 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 486 GRAKPFRDKPVTDQQLI-------EKITQVTEDNINFQQKKWTLqkETQLSNSKQEETTENIEKLRTSLDSCQACMKISC 558
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIkdeldksEKLIKKIKDDINLEECKSKI--ESTLDDKDIDECIKKIKELKNHILSEESNIDTYF 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 559 CSHDLKKEVDLLQHLQVSPPVSGLQKVVLDVLRHALSWL-----EEVEQLLRDLGI-LPSSPNKGFSLYLIYLLEHYKK- 631
Cdd:TIGR01612 1443 KNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHdfninELKEHIDKSKGCkDEADKNAKAIEKNKELFEQYKKd 1522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 632 ---LMSQAQELQIKFNSSQETQQSllqeklREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQ--ERNRA-- 704
Cdd:TIGR01612 1523 vteLLNKYSALAIKNKFAKTKKDS------EIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKndKSNKAai 1596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 705 --KETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEK--RKAKEAL 780
Cdd:TIGR01612 1597 diQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKniEDKKKEL 1676
|
570 580
....*....|....*....|....*
gi 1034555165 781 ESEKRKVQDLENHLTQQKEISESNI 805
Cdd:TIGR01612 1677 DELDSEIEKIEIDVDQHKKNYEIGI 1701
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
271-725 |
1.79e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 271 IANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIdakqKEIQSLKSQISALQKGYSKVLCQTLSERNSEITSLKN 350
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH----ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 351 EGENLKrdnaitsgmvsslqkdilakdEQVQQLKEEVSHLKSQNKDKDHQLEALGS---RCSVLKEELKQEDaHRELREA 427
Cdd:PRK03918 399 AKEEIE---------------------EEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEH-RKELLEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 428 QEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHfrsqvIKATYGRAKPFRdkpvtdqqlIEKITQ 507
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYN---------LEELEK 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 508 VTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCCSHDLKKEVDLLQHLQVSPPVSGLQKVVL 587
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 588 DVLRhALSWLEEVEQLLRDLGILPSSPNKGFSlYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEK 667
Cdd:PRK03918 603 EYLE-LKDAEKELEREEKELKKLEEELDKAFE-ELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA 680
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 668 LNEERLEQEEKLKAKIRQLTEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQ 725
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
666-779 |
2.27e-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: 45.14 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 666 EKLNEERLEQEEKLKAKIRQLTEEKAALEEyITQERNRAKETLEEERKRMQELEsllaQQKKALAKSITQEKNRVKEALE 745
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALK----AERQKLLARLEKELAELAAELA 216
|
90 100 110
....*....|....*....|....*....|....
gi 1034555165 746 EEQTRVQELEERLARqkevLESSIAHEKRKAKEA 779
Cdd:COG4942 217 ELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
654-760 |
2.49e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 654 LQEKLREHLAEKEKLNEErleQEEKLKAKIRQLTEEKAALEEYITQERNR-------------AKETLEEERKRMQELES 720
Cdd:COG0542 416 LERRLEQLEIEKEALKKE---QDEASFERLAELRDELAELEEELEALKARweaekelieeiqeLKEELEQRYGKIPELEK 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034555165 721 LLAQQKKALAKSITQEKNRVKEA-----------------LEEEQTRVQELEERLAR 760
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEEdiaevvsrwtgipvgklLEGEREKLLNLEEELHE 549
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-783 |
2.56e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 250 LGKEVSRLSDYEIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQkg 329
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLE-- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 330 yskvlcQTLSERNSEITSLKNEGENLKRdnaitsgmvsslQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCS 409
Cdd:PRK03918 259 ------EKIRELEERIEELKKEIEELEE------------KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 410 VLKEELKqedahRELREAQEKELKLckTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHfrsqvikatygrak 489
Cdd:PRK03918 321 EEINGIE-----ERIKELEEKEERL--EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK-------------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 490 pfRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKIscCSHDLKKEVDL 569
Cdd:PRK03918 380 --RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE--LTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 570 LQHLQVSPPVSGLQKVVlDVLRHALSWLEEVEQLLRDLGILpsspnkgfsLYLIYLLEHYKKLMSQAQELQIKFNSSQET 649
Cdd:PRK03918 456 EYTAELKRIEKELKEIE-EKERKLRKELRELEKVLKKESEL---------IKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 650 QQSLLQEKLREHLAEKEKLNEErLEQEEKLKAKIRQLTEEKAALEE----YITQERNRAKETLEEERKRMQELESllAQQ 725
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKLDELEEelaeLLKELEELGFESVEELEERLKELEP--FYN 602
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555165 726 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLEssiahEKRKAKEALESE 783
Cdd:PRK03918 603 EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-----ELRKELEELEKK 655
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
304-442 |
2.59e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 304 VLDEDIDAKQKEIQSLKSQIS------ALQKGYSKVLCQTLSERNSEITSLKNEGENLKRDNAITSGMVSSLQKdilakd 377
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAeladllSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG------ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555165 378 eQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKqedAHRELREAQEKELKLCKTQIQDM 442
Cdd:PRK09039 117 -RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLA---ALEAALDASEKRDRESQAKIADL 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-967 |
2.99e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 270 IIANLQNEVAELSQKVSETTTSRQNEKeisQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLK 349
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIKNDKEQKNKLEVELNK-LEKQKKENKKNIDKFL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 350 NEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQedaHRELreaqE 429
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQK---NKSL----E 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 430 KELKLCKTQIQDMEKEMKKLRAELRKsctEQSVISRTlreKSKLEHFRSQVIKatygrakpfrdkpvTDQQLIEKITQVT 509
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINE---KTTEISNT---QTQLNQLKDEQNK--------------IKKQLSEKQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 510 EDNINFQQKKWTLQK-ETQLSNSKQEETTENIEKLRTSLDSCQAcmKISCCSHDLKKEVDLLQHLQVSppVSGLQKVVLD 588
Cdd:TIGR04523 278 QNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSELKNQEK--KLEEIQNQISQNNKIISQLNEQ--ISQLKKELTN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 589 VLRHALSWLEEVEQLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQELQIKFnSSQETQQSLLQEKLREHLAEKEKL 668
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQS--------YKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 669 NEER---LEQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLEEERKRMQELESLLAQQKKALaKSITQEKNRVKE 742
Cdd:TIGR04523 425 EKEIerlKETIIKNNSEIKDLTNQDSVKELIIKnldNTRESLETQLKVLSRSINKIKQNLEQKQKEL-KSKEKELKKLNE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 743 ALEEEQTRVQELEERLARQKE---VLESSIAHEKRKAKEaLESEKRKVQDLENHLTQQKEISESNIAYEK-RKAKEAMEK 818
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEkieKLESEKKEKESKISD-LEDELNKDDFELKKENLEKEIDEKNKEIEElKQTQKSLKK 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 819 EKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE 898
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 899 RLILQQKMVKALQDE-QESQRHGFEEEIMEYKEQIKQHAQTIvsleeKLQKVTQHHKKIEGEIATLKDND 967
Cdd:TIGR04523 663 EIIKKIKESKTKIDDiIELMKDWLKELSLHYKKYITRMIRIK-----DLPKLEEKYKEIEKELKKLDEFS 727
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
661-1011 |
3.37e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 661 HLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqernraketLEEERKRMQELESLLAQQKKA----LAKsiTQE 736
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVE------------MARELEELSARESDLEQDYQAasdhLNL--VQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 737 KNRVKEALEEEQTRVQELEERLARQKEVLESsiAHEKR-KAKEALESEKRKVQDLENHLT--QQ--KEISESNIAYE--- 808
Cdd:COG3096 342 ALRQQEKIERYQEDLEELTERLEEQEEVVEE--AAEQLaEAEARLEAAEEEVDSLKSQLAdyQQalDVQQTRAIQYQqav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 809 --KRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQK--------TKATESLKAESLALK 878
Cdd:COG3096 420 qaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 879 LNETLAEL-------ETTKTKMIMVEERLILQQKMVKALqdEQESQRHG--------FEEEIMEYKEQIKQHAQTIVSLE 943
Cdd:COG3096 500 LLRRYRSQqalaqrlQQLRAQLAELEQRLRQQQNAERLL--EEFCQRIGqqldaaeeLEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 944 EKLQKVTQHHKKIEGEIATLKDNDPA-----PKEERPQDPLVAPMTESSAKDMAYEHLID---------DLLAAQKEILS 1009
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAwlaaqDALERLREQSGEALADSQEVTAAMQQLLErereatverDELAARKQALE 657
|
..
gi 1034555165 1010 QQ 1011
Cdd:COG3096 658 SQ 659
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
28-110 |
3.62e-04 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438753 [Multi-domain] Cd Length: 106 Bit Score: 41.46 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 28 FFVLNKSTTIGR---------HENSDLVLQSPD-IDNHHALIEYNEAECSFVLQDFnSRNGTFVNE--CHIQNVAVKLIP 95
Cdd:cd22701 12 YYVQKLEVVLGRnsknssstaADSVDIDLGPSKkISRRHARIFYDFTTQCFELSVL-GRNGVKVDGilVKPGSPPVPLRS 90
|
90
....*....|....*
gi 1034555165 96 GDILRFGSAGLTYEL 110
Cdd:cd22701 91 GSLIQIGGVLFYFLL 105
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
278-954 |
3.86e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 278 VAELSQKVSETTTSRQNEKEIS---------QKCQVLDEDIDAKQKEIQSLKS---QISALQKGYSKVLCQTLSERNSEI 345
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEhwirdiqaiAGIMKIRPEFTKLQQEFNTLESaelRLSHLHFGYKSDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 346 TSLKNEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKdkdhqlEALGSRCSVLKEELKQEDAHRELR 425
Cdd:pfam12128 283 ETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG------AFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 426 EAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQ-VIKATY-GRAKPFRDkpvtdqQLIE 503
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLaVAEDDLqALESELRE------QLEA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 504 KITQVTED---------NINFQQKKWTLQKETQLsnsKQEETTENIEKLRTSLDSCqacmkisccshdlKKEVDLLQHLQ 574
Cdd:pfam12128 431 GKLEFNEEeyrlksrlgELKLRLNQATATPELLL---QLENFDERIERAREEQEAA-------------NAEVERLQSEL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 575 VSppVSGLQKVVLDVLRHALSWLEEVEQLLRDLGILPSSPnkgfSLYLIYLL--------EHYKKLMSQAQ----ELQIK 642
Cdd:pfam12128 495 RQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQ----AGTLLHFLrkeapdweQSIGKVISPELlhrtDLDPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 643 FNSSQETQQSLLQeklrehlaeKEKLNEERLEqeeklkakirqlTEEKAALEEYITQERNRAKETLEEERKRMQELESLL 722
Cdd:pfam12128 569 VWDGSVGGELNLY---------GVKLDLKRID------------VPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 723 AQQKKALAKSitqeknrvKEALEEEQTRVQELEERLARQKEVLESsiahEKRKAKEALESEKRKVQDLENHLTQQKEISE 802
Cdd:pfam12128 628 VQANGELEKA--------SREETFARTALKNARLDLRRLFDEKQS----EKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 803 SNIAYEKRKAKEamekekkkvQDLENRLTKQKEELelkeqkedVLNNKLSDALAMVEETqKTKATESLKAESLALK--LN 880
Cdd:pfam12128 696 KKHQAWLEEQKE---------QKREARTEKQAYWQ--------VVEGALDAQLALLKAA-IAARRSGAKAELKALEtwYK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 881 ETLAELETTKTKMIMVE-ERLILQQKMVKALQDEQES------QRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHH 953
Cdd:pfam12128 758 RDLASLGVDPDVIAKLKrEIRTLERKIERIAVRRQEVlryfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT 837
|
.
gi 1034555165 954 K 954
Cdd:pfam12128 838 K 838
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
635-779 |
3.88e-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: 44.75 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 635 QAQELQIKFNSSQETQQSLLQEKLREHLAE--------------KEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQE 700
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 701 RNR---AKETLEEERKRMQELESLLAQQKKALAKSItQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 777
Cdd:COG4942 159 LAElaaLRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 1034555165 778 EA 779
Cdd:COG4942 238 AA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
869-1107 |
4.02e-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: 44.37 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 869 SLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQrhgfEEEIMEYKEQIKQHAQTIVSLEEKLQK 948
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 949 VTQHHKKIEGEIATLKDN-----DPAPKEERPQDPLVAPMTESSAKDMAYEHLIDDLLAAQKEIlsqqevIMKLRKDLTE 1023
Cdd:COG4942 88 LEKEIAELRAELEAQKEElaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1024 AHSRMSDLRGELNEKQKMELEQnvvlvQQQSKELSVLK-EKMAQMSSLVEKKDRELKALEEALRASQEKHRLQLNTEKEQ 1102
Cdd:COG4942 162 LAALRAELEAERAELEALLAEL-----EEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 1034555165 1103 KPRKK 1107
Cdd:COG4942 237 AAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-956 |
4.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 371 KDILAKDEQVQQLKEEvshlksqnkdKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLR 450
Cdd:PRK03918 182 EKFIKRTENIEELIKE----------KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 451 AELRKSCTEQSVISRTLRE-KSKLEHFRSQV--------IKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWt 521
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEElKKEIEELEEKVkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 522 lqKETQLSNSKQEETTENIEKLRTSLDscqacmkisccshDLKKEVDLLQHLQVsppvsglQKVVLDVLRHALSwLEEVE 601
Cdd:PRK03918 331 --KELEEKEERLEELKKKLKELEKRLE-------------ELEERHELYEEAKA-------KKEELERLKKRLT-GLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 602 QLLRDLGILPSSPNKgfslyliyLLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKA 681
Cdd:PRK03918 388 KLEKELEELEKAKEE--------IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 682 KIRQLTEEKAALEEYITQERNRAKEtLEEERKRMQELESL--LAQQKKALAKSItqeKNRVKEALEEEQTRVQELEERLA 759
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLkeLAEQLKELEEKL---KKYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 760 RQKEvlESSIAHEKRKAKEALESEKRKvqdLENHLTQQKEISESNIAYEKRKAKEAMEKEKKKVQDLE------NRLTKQ 833
Cdd:PRK03918 536 KLKG--EIKSLKKELEKLEELKKKLAE---LEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 834 KEELELKEQKEDVLNNKLSDALAMVEETQktKATESLKAESLALKLNETLAELETTKTKMIMVEERLILQQKMVKALQDE 913
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1034555165 914 QESQRHGFeEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI 956
Cdd:PRK03918 689 REEIKKTL-EKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
261-810 |
4.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 261 EIESKYKDVIIANLQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSkvlcQTLSE 340
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIA----ETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 341 RNS---EITSLKNEGENLKRDNaitSGMVSSLQKDIlAKDEQVQQLKEEVShlksqnkDKDHQLEALGSRCSV-LKEELK 416
Cdd:PRK02224 274 REElaeEVRDLRERLEELEEER---DDLLAEAGLDD-ADAEAVEARREELE-------DRDEELRDRLEECRVaAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 417 QEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSklehfrsqvikatygraKPFRDKPV 496
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR-----------------ERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 497 TDQQLIEKITQVTEDninfqqKKWTLQKETQLSNSKQEEtTENIEKLRTSLDS--CQACMkisccshdlkkevdllQHLQ 574
Cdd:PRK02224 406 DLGNAEDFLEELREE------RDELREREAELEATLRTA-RERVEEAEALLEAgkCPECG----------------QPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 575 VSPPVsglqkvvlDVLRHALSWLEEVEQLLRDLGILPSSPNKGfslylIYLLEHYKKLMSQAQELQIKfnssQETQQSLL 654
Cdd:PRK02224 463 GSPHV--------ETIEEDRERVEELEAELEDLEEEVEEVEER-----LERAEDLVEAEDRIERLEER----REDLEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 655 QEKlREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQER------NRAKETLEEERKRMQELESLLA----- 723
Cdd:PRK02224 526 AER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevaelNSKLAELKERIESLERIRTLLAaiada 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 724 --------QQKKALAKSITQEKNRVKE------ALEEE--QTRVQELEERLARQKEVLE--SSIAHEKRKAKEALESEkr 785
Cdd:PRK02224 605 edeierlrEKREALAELNDERRERLAEkrerkrELEAEfdEARIEEAREDKERAEEYLEqvEEKLDELREERDDLQAE-- 682
|
570 580
....*....|....*....|....*
gi 1034555165 786 kVQDLENHLTQQKEISESNIAYEKR 810
Cdd:PRK02224 683 -IGAVENELEELEELRERREALENR 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
648-799 |
4.86e-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: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLLQEKLREHLAEKEKLNEERLEQEEK-------------------LKAKIRQLTEEKAALEeyitqERNRAKETL 708
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidvasAEREIAELEAELERLD-----ASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 709 EEERKRMQELESLLAQQKKALAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQ 788
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170
....*....|.
gi 1034555165 789 DLENHLTQQKE 799
Cdd:COG4913 770 NLEERIDALRA 780
|
|
| FHA_Par42-like |
cd22675 |
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ... |
37-117 |
5.25e-04 |
|
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438727 [Multi-domain] Cd Length: 113 Bit Score: 41.00 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 37 IGRHENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQnvAVKLIP---GDILRFGSAGLTYElVIE 113
Cdd:cd22675 33 FGRSPVCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIE--KGRPLPlpvGSVIQFGFSARKYK-VRK 109
|
....
gi 1034555165 114 NPPP 117
Cdd:cd22675 110 GPPS 113
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
28-103 |
5.88e-04 |
|
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.
Pssm-ID: 438734 [Multi-domain] Cd Length: 96 Bit Score: 40.59 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 28 FFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVN--------ECHIQNvavklipGDIL 99
Cdd:cd22682 15 FPITESTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVS--IIDLGSTNGTIVNgkkipklaSCDLQN-------GDQI 85
|
....
gi 1034555165 100 RFGS 103
Cdd:cd22682 86 KIGN 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
648-876 |
6.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLLQEKLREHLAEKEKLNEE--RLEQE-EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQ 724
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEldALQAElEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 725 QKKA-----------LAKSITQEKNRVkEALEEEQTRVQELEERLARQKEVLEssiahekrKAKEALESEKRKVQDLENH 793
Cdd:COG3883 95 LYRSggsvsyldvllGSESFSDFLDRL-SALSKIADADADLLEELKADKAELE--------AKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 794 LTQQKEISESNIAyEKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAE 873
Cdd:COG3883 166 LEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
...
gi 1034555165 874 SLA 876
Cdd:COG3883 245 SAA 247
|
|
| FHA_RAD53-like_rpt1 |
cd22689 |
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
3-82 |
7.72e-04 |
|
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438741 [Multi-domain] Cd Length: 132 Bit Score: 41.11 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 3 SLEPCRLFiYGKTERMKAYLKSAEGFFvlnkstTIGRHENSDLVLQSPDIDNHHALI---EYNEAECSFVLQDFNSrNGT 79
Cdd:cd22689 22 TQEPIRDL-SGDISQVLKEKRSIKKVW------TFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDISS-NGT 93
|
...
gi 1034555165 80 FVN 82
Cdd:cd22689 94 WLN 96
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
314-461 |
8.18e-04 |
|
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: 42.81 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 314 KEIQSLKSQISALQKGYS--KVLCQTLSERNS-----------EITSLKNEGENLkrdnaitSGMVSSLQKDILAKDEQV 380
Cdd:pfam17078 3 KVIESLHDQIDALTKTNLqlTVQSQNLLSKLEiaqqkeskfleNLASLKHENDNL-------SSMLNRKERRLKDLEDQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 381 QQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE--------DAHRELREAQEKELKLCKTQIQDMEKEMKKLRAE 452
Cdd:pfam17078 76 SELKNSYEELTESNKQLKKRLENSSASETTLEAELERLqiqydalvDSQNEYKDHYQQEINTLQESLEDLKLENEKQLEN 155
|
....*....
gi 1034555165 453 LRKSCTEQS 461
Cdd:pfam17078 156 YQQRISSND 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
671-802 |
8.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 671 ERLEQE-EKLKAKIRQLTEEKAALEEYItqernRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQT 749
Cdd:COG4913 238 ERAHEAlEDAREQIELLEPIRELAERYA-----AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034555165 750 RVQELEERLARQKEVLESSIAHEKRKAKEALESEkrkVQDLENHLTQQKEISE 802
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLERE---IERLERELEERERRRA 362
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
411-974 |
9.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 411 LKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKscteqsvisrTLREKSKLEHFRSQVIKATYGRAKP 490
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----------LEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 491 FRDKpvtdQQLIEKITQvTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDscqacmKISCCSHDLKKEVDLL 570
Cdd:PRK03918 251 EGSK----RKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE------EYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 571 QHLqvsppVSGLQKVV--LDVLRHALSWL-EEVEQLLRDLGILPSSpnkgfslylIYLLEHYKKLMSQAQELQIKFnssq 647
Cdd:PRK03918 320 EEE-----INGIEERIkeLEEKEERLEELkKKLKELEKRLEELEER---------HELYEEAKAKKEELERLKKRL---- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 etqQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItQERNRAK--------ETLEEERKRmqele 719
Cdd:PRK03918 382 ---TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKgkcpvcgrELTEEHRKE----- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 720 sLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVL-ESSIAHEKRKAKEALesEKRKVQDLENHLTQQK 798
Cdd:PRK03918 453 -LLEEYTAEL-KRIEKELKEIEEKERKLRKELRELEKVLKKESELIkLKELAEQLKELEEKL--KKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 799 EISESNIAYEKRKAKEAMEKEKKkvQDLENRLTKQKEELELKEQKEDVLNNKLSD-ALAMVEETQKT-KATESLKAESLA 876
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKL--EELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERlKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 877 LK-----LNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGF-EEEIMEYKEQIKQHAQTIVSLEEKLQKVT 950
Cdd:PRK03918 607 LKdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELE 686
|
570 580
....*....|....*....|....
gi 1034555165 951 QHHKKIEGEIATLKDNDPAPKEER 974
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAK 710
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
262-966 |
1.04e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 262 IESKYKDVIIANLQNEVAELSQKVSETTTS--RQNEKEISQ------------KCQVLDEDIDAKQKEIQSLKSQISALQ 327
Cdd:TIGR01612 960 IEKSYKDKFDNTLIDKINELDKAFKDASLNdyEAKNNELIKyfndlkanlgknKENMLYHQFDEKEKATNDIEQKIEDAN 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 328 KGYSKVLCQTlserNSEITSLKNEGENLKRDNaitsgmVSSLQKDILAKDE----QVQQLKEEVSHLKSQNKDKDHQLEa 403
Cdd:TIGR01612 1040 KNIPNIEIAI----HTSIYNIIDEIEKEIGKN------IELLNKEILEEAEinitNFNEIKEKLKHYNFDDFGKEENIK- 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 404 LGSRCSVLKEELK----QEDAH----RELREAQEKELKLCKTQIQDMEK--------------------------EMKKL 449
Cdd:TIGR01612 1109 YADEINKIKDDIKnldqKIDHHikalEEIKKKSENYIDEIKAQINDLEDvadkaisnddpeeiekkienivtkidKKKNI 1188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 450 RAELRKSCTEqsvISRTLREKSKLEHFRSqvIKATYGRA--KPFRDKPVTDQQLIEKITQVTE------DNINFQQKKWT 521
Cdd:TIGR01612 1189 YDEIKKLLNE---IAEIEKDKTSLEEVKG--INLSYGKNlgKLFLEKIDEEKKKSEHMIKAMEayiedlDEIKEKSPEIE 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 522 LQKETQLSNSKQEET------------------TENIEKLRT-SLDSCQACMKISCCShDLKKEvdllqhlqvsppvsgL 582
Cdd:TIGR01612 1264 NEMGIEMDIKAEMETfnishdddkdhhiiskkhDENISDIREkSLKIIEDFSEESDIN-DIKKE---------------L 1327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 583 QKVVLDVLRHAlswlEEVEQLLrdlgilpsspNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSSQETQQSLL--QEKLRE 660
Cdd:TIGR01612 1328 QKNLLDAQKHN----SDINLYL----------NEIANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELdkSEKLIK 1393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 661 HLAEKEKLNEERLEQEEKLKAK-IRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNR 739
Cdd:TIGR01612 1394 KIKDDINLEECKSKIESTLDDKdIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIK 1473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 740 VKEALEEEQTRVQELEERLARQKEVLESSIAHEKR--KAKEALESEKRKVQDLENHLTQQKeiSESNIAYEKRKAKEAME 817
Cdd:TIGR01612 1474 KDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAieKNKELFEQYKKDVTELLNKYSALA--IKNKFAKTKKDSEIIIK 1551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 818 KekkkVQDLENRLTKQKEELELKEQK---------EDVLNNKLSDALAM-VEETQKTKATESLKAESLALKLNETLAELE 887
Cdd:TIGR01612 1552 E----IKDAHKKFILEAEKSEQKIKEikkekfrieDDAAKNDKSNKAAIdIQLSLENFENKFLKISDIKKKINDCLKETE 1627
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034555165 888 TTKTKMimveerlilqQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKDN 966
Cdd:TIGR01612 1628 SIEKKI----------SSFSIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKN 1696
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
243-552 |
1.16e-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: 43.66 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 243 KDEIILLLGKEVSRLSDyeiESKYKDVIIANLQNEVAELSQKVSETTTSrqnekeisqkCQVLDEDIDAKQKEIQSLKSQ 322
Cdd:pfam10174 392 KERKINVLQKKIENLQE---QLRDKDKQLAGLKERVKSLQTDSSNTDTA----------LTTLEEALSEKERIIERLKEQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 323 ISALQKgyskvlcqtlsERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLE 402
Cdd:pfam10174 459 REREDR-----------ERLEELESLKKENKDLKEK-------VSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 403 ALGSRCSVLKEE-LKQEDAHRELREAQEKELKLCK--TQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLEHFRSQ 479
Cdd:pfam10174 521 SLEIAVEQKKEEcSKLENQLKKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDK 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 480 VIKATYGRA-KPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQ--EETTENIEKLRTSLDSCQA 552
Cdd:pfam10174 601 KIAELESLTlRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLqlEELMGALEKTRQELDATKA 676
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
630-800 |
1.19e-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: 43.63 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 630 KKLMSQAQELQIKFNSSqETQQSLLQEKLRE-------------------------------HLAEKEKLNEERLEQEEK 678
Cdd:pfam01576 408 KKLEGQLQELQARLSES-ERQRAELAEKLSKlqselesvssllneaegkniklskdvsslesQLQDTQELLQEETRQKLN 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 679 LKAKIRQLTEEKAALEEYItQERNRAKETLEeerKRMQELESLLAQQKKALaksitQEKNRVKEALEEEQTRVQELEERL 758
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQL-EEEEEAKRNVE---RQLSTLQAQLSDMKKKL-----EEDAGTLEALEEGKKRLQRELEAL 557
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034555165 759 ARQKEvlessiahEKRKAKEALESEKRKVQ----DLENHLTQQKEI 800
Cdd:pfam01576 558 TQQLE--------EKAAAYDKLEKTKNRLQqeldDLLVDLDHQRQL 595
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
627-780 |
1.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 627 EHYKKLMSQA-QELQIKFNSSQETQQSLLQ--EKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYItqernr 703
Cdd:PRK12704 64 EEIHKLRNEFeKELRERRNELQKLEKRLLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 704 aketlEEERKRMQELESLLAQQkkalAKSITQEKnrVKEALEEEQTR-VQELEERlarqkevlessiAHE--KRKAKEAL 780
Cdd:PRK12704 138 -----EEQLQELERISGLTAEE----AKEILLEK--VEEEARHEAAVlIKEIEEE------------AKEeaDKKAKEIL 194
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-797 |
1.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 658 LREHLAEKEklneERLEQEEKLKAKIRQLTEEKAALEEyitqernrAKETLEEERKRMQELESLLAQQKKALAKSITQEK 737
Cdd:COG4913 666 AEREIAELE----AELERLDASSDDLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 738 NRVKEALE-EEQTRVQELEERLARqkEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQQ 797
Cdd:COG4913 734 DRLEAAEDlARLELRALLEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
625-783 |
1.49e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 625 LLEHYKKLMSQAQELQIKFNSSQEtQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQL------------------ 686
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyldvllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 687 ---------------TEEKAALEEYITQER--NRAKETLEEERKRMQELESLLAQQKKALAKSITqEKNRVKEALEEEQT 749
Cdd:COG3883 114 fsdfldrlsalskiaDADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEA 192
|
170 180 190
....*....|....*....|....*....|....
gi 1034555165 750 RVQELEERLARQKEVLESSIAHEKRKAKEALESE 783
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
647-1170 |
1.58e-03 |
|
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: 43.13 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 647 QETQQSLLQEKLREHLAEKEKLNEERLEQE---EKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERKRMQE-LESLL 722
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 723 AQQkkALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAhEKRKAKEALESEKRKVQDLENHLTQQ-KEIS 801
Cdd:TIGR02169 301 AEI--ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAElEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 802 ESNIAY--EKRKAKEAMEKEKKKVQDLENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKL 879
Cdd:TIGR02169 378 KEFAETrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 880 NETLAELETTKTKMIMVEERLILQQKMVKALQ---DEQESQRHGFEEEIMEYK---EQIKQHAQTIVSLEEKLQKV-TQH 952
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRaveEVLKASIQGVHGTVAQLGSVgERY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 953 HKKIEGE-------------------IATLKDNDPAP------KEERPQDPLVAPMTESSAKDMAY-------------- 993
Cdd:TIGR02169 538 ATAIEVAagnrlnnvvveddavakeaIELLKRRKAGRatflplNKMRDERRDLSILSEDGVIGFAVdlvefdpkyepafk 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 994 ------------------------------------------------------------------EHLIDDLLAAQKEI 1007
Cdd:TIGR02169 618 yvfgdtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqrlrerlEGLKRELSSLQSEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1008 LSQQEVIMKLRKDLTEAHSRMSDLRGELN------EKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSLVEKKDRELKAL 1081
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEqleqeeEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 1082 EEAL---RASQEKHRLQ-----LNTEKEQKPRKKTQTCDTSVQIEPVHTEAFSSSQEQQSFSDLGVRCKgSRHEEVIQRQ 1153
Cdd:TIGR02169 778 EEALndlEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK-EQIKSIEKEI 856
|
650 660
....*....|....*....|
gi 1034555165 1154 ---KKALSELRARIKELEKA 1170
Cdd:TIGR02169 857 enlNGKKEELEEELEELEAA 876
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
33-110 |
1.67e-03 |
|
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438726 [Multi-domain] Cd Length: 108 Bit Score: 39.56 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 33 KSTTIGR-HENSDLVLQSPDIDNHHALIEYNEAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFGSAGLTYEL 110
Cdd:cd22674 27 KYYLFGRnSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEpHKPQQLPIDSTLRFGASTRRYIL 106
|
|
| FHA_EmbR-like |
cd22669 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ... |
22-109 |
1.72e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438721 [Multi-domain] Cd Length: 89 Bit Score: 38.94 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 22 LKSAEGFFVLNKSTTIGRHENSDLVLQSPDIDNHHALIEYNEAECSfvLQDFNSRNGTFVNECHIQNVAVkLIPGDILRF 101
Cdd:cd22669 5 IASGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYV--INDLRSSNGVHVQHERIRSAVT-LNDGDHIRI 81
|
....*...
gi 1034555165 102 GSAGLTYE 109
Cdd:cd22669 82 CDHEFTFQ 89
|
|
| FHA_Ct664-like |
cd22696 |
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ... |
25-103 |
1.86e-03 |
|
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438748 [Multi-domain] Cd Length: 97 Bit Score: 39.01 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 25 AEGFFVLNKSTTIGRHEN-SDLVLQSPDIDNHHALIEYNEAECSFVlQDFNSRNGTFVNECHIQNvAVKLIPGDILRFGS 103
Cdd:cd22696 13 AEFFLESGKTYFIGKDPTvCDIVLQDPSISRQHARLSIDQDNRVFI-EDLSSKNGVLVNGKPIEG-KEEISGSDVISLGT 90
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
701-783 |
1.92e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 701 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQE----LEERLARQKEVLESSIAHEKRKA 776
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEakaeAEAEAERIIAQAEAEIEQERAKA 112
|
....*..
gi 1034555165 777 KEALESE 783
Cdd:COG0711 113 LAELRAE 119
|
|
| FHA_Rv1747-like_rpt2 |
cd22737 |
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
37-109 |
2.18e-03 |
|
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.
Pssm-ID: 439356 [Multi-domain] Cd Length: 93 Bit Score: 39.01 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034555165 37 IGRHENSDLVLQSPDIDNHHALIEYNEAecSFVLQDFNSRNGTFVNECHIQnvAVKLIPGDILRFGSAGLTYE 109
Cdd:cd22737 25 IGRASDNDIVIPEGSVSRHHATLVPTPG--GTQIRDLRSTNGTFVNGLRVD--AALLHDGDVVTIGDIDFVFE 93
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
656-803 |
2.34e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 656 EKLREHL-AEKEKLNE--ERLEQEEK-LKAKIRQLTEEKaaleeyitQERNRAKETLEEERKRMQE-LESLLAQQKKALA 730
Cdd:PRK00409 505 EEAKKLIgEDKEKLNEliASLEELEReLEQKAEEAEALL--------KEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555165 731 KsitqeknRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKA-KEALESekrkvqdLENHLTQQKEISES 803
Cdd:PRK00409 577 Q-------AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRlNKANEK-------KEKKKKKQKEKQEE 636
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-456 |
2.62e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 261 EIESKYKDviIANLQNEVAELSQKVSETTtsrQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKGYSKVLCQT-LS 339
Cdd:TIGR04523 490 ELKSKEKE--LKKLNEEKKELEEKVKDLT---KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeID 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 340 ERNSEITSLKNEGENLKRDN-------AITSGMVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLK 412
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQeekqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034555165 413 EELKQ-EDAHRELREAQ---EKELKLCKTQIQDMEKEMKKLRAELRKS 456
Cdd:TIGR04523 645 QEVKQiKETIKEIRNKWpeiIKKIKESKTKIDDIIELMKDWLKELSLH 692
|
|
| FHA_GarA-like |
cd22720 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ... |
29-108 |
2.65e-03 |
|
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438772 [Multi-domain] Cd Length: 100 Bit Score: 38.83 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 29 FVLNKSTT-IGRHENSDLVLQSPDIDNHHAliEYNEAECSFVLQDFNSRNGTFVNECHIqNVAVkLIPGDILRFGSAGLT 107
Cdd:cd22720 19 FLLDQAITsAGRHPDSDIFLDDVTVSRRHA--EFRLENNEFNVVDVGSLNGTYVNREPV-DSAV-LANGDEVQIGKFRLV 94
|
.
gi 1034555165 108 Y 108
Cdd:cd22720 95 F 95
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
410-723 |
2.67e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 410 VLKEELKQ-EDAHRELREAQEKELKLCKTQIQDMEKEMKklRAELRKSCTEQSVISRTLREKSKLEHFRSQVIKATYGRA 488
Cdd:pfam09731 133 VLKEAISKaESATAVAKEAKDDAIQAVKAHTDSLKEASD--TAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 489 KPFRDKPV-TDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQACMKISCcSHDLKKEV 567
Cdd:pfam09731 211 PPLLDAAPeTPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLS-NDDLNSLI 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 568 DLLqHLQVSPPVSGLQKVVLDVLRHALSWLEEVEQLLRDLgilpsspnkgfSLYLIYLLEHykKLMSQAQELQIKFNSSQ 647
Cdd:pfam09731 290 AHA-HREIDQLSKKLAELKKREEKHIERALEKQKEELDKL-----------AEELSARLEE--VRAADEAQLRLEFERER 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 648 ETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAkIRQLTEEKAALEEYITQERNRAKETLEEERKRMQELESLLA 723
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE-IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATS 430
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
647-791 |
2.78e-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: 42.25 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 647 QETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEE-------YITQERNRAKETLEEERKRMQELE 719
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEeerkqrlQLQAAQERARQQQEEFRRKLQELQ 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034555165 720 SLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEErlarqKEVLESSIAHEKRKAKEALESEKRKVQDLE 791
Cdd:pfam15709 437 RKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-456 |
2.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 274 LQNEVAELSQKVSETTTSRQNEKEISQKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvlcqTLSERNSEITSLKNEGE 353
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------EIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 354 NLKRDNAITSGMVSSLQKDILAKD---------------EQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQE 418
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034555165 419 DAHRE-LREAQEKELKLCKTQIQDMEKEMKKLRAELRKS 456
Cdd:COG3883 170 KAELEaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
651-810 |
3.15e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 651 QSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEyitqERNRAKETLEEERKRMQELESllaqQKKALA 730
Cdd:pfam09787 17 ARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLRE----EIQKLRGQIQQLRTELQELEA----QQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 731 KSITQEKNRVKEALEEEQTRVQELEERLARQKEVLeSSIAHEKRKAKEALESEKRK----VQDLENHLTQQKEISESNIA 806
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEEL-RYLEEELRRSKATLQSRIKDreaeIEKLRNQLTSKSQSSSSQSE 167
|
....
gi 1034555165 807 YEKR 810
Cdd:pfam09787 168 LENR 171
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
705-800 |
3.28e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 39.66 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 705 KETLEEERKRMQELESLLAQQKKALAK-------SITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAK 777
Cdd:pfam05130 4 IELLEEELELLEELLELLEEEQEALKAgdiealeELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLSELLAKEEED 83
|
90 100
....*....|....*....|...
gi 1034555165 778 EALESEKRKVQDLENHLTQQKEI 800
Cdd:pfam05130 84 PELRELWQELLELLERLKELNEL 106
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
654-778 |
3.87e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 654 LQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKEtleeerkrMQEL-ESLLAQQKKALAKS 732
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE--------LEDCdPTELDRAKEKLKKL 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034555165 733 ITQEKNRVKEaLEEEQTRVQELE---ERLARQKEVLESSIAHEKRKAKE 778
Cdd:smart00787 217 LQEIMIKVKK-LEELEEELQELEskiEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-453 |
3.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 300 QKCQVLDEDIDAKQKEIQSLKSQISALQKgyskvLCQTLSERNSEITSLKNegenlkrdnaitsgmVSSLQKDILAKDEQ 379
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAE---------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034555165 380 VQQLKEEVSHLKSQNKDkdhqLEALGSRCSVLKEELkqeDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAEL 453
Cdd:COG4913 670 IAELEAELERLDASSDD----LAALEEQLEELEAEL---EELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
637-767 |
4.05e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 637 QELQIKFNSSQETQQSLLQEKLREHLAEkekLNEERLEQEEKLKAK---IRQLTEEKAALEEYITQERNRAKETLEEE-- 711
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEle 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034555165 712 --RKRMQELESLLAQQKKALAKsitqeknrvkeaLEEEQTRVQELEERLARQKEVLES 767
Cdd:COG3206 324 alQAREASLQAQLAQLEARLAE------------LPELEAELRRLEREVEVARELYES 369
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
635-747 |
4.19e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 635 QAQELQIKFNSSQE-TQQSLLQekLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAKETLEEERK 713
Cdd:pfam02841 173 KAEEVLQEFLQSKEaVEEAILQ--TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIE 250
|
90 100 110
....*....|....*....|....*....|....*
gi 1034555165 714 RM-QELESLLAQQKKALAKSITQEKNRVKEALEEE 747
Cdd:pfam02841 251 KMeAEREQLLAEQERMLEHKLQEQEELLKEGFKTE 285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
648-763 |
4.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLLQEKLREHLAEKEKLnEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRAK--ETLEEERKRMQELESLLAQQ 725
Cdd:COG3206 225 ESQLAEARAELAEAEARLAAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAAL 303
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034555165 726 KKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKE 763
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
648-751 |
4.71e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 648 ETQQSLLQEKLREHLAEKEKLNEERLEQEEkLKAKIRQLTEEKAALEEYitqernrAKETLEEERKRMQELESLLAQQKK 727
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQ-SQALAEAQQQELVALEGL-------AAELEEKQQELEAQLEQLQEKAAE 209
|
90 100
....*....|....*....|....*....
gi 1034555165 728 ALAKSITQEKNRVKEA-----LEEEQTRV 751
Cdd:PRK11448 210 TSQERKQKRKEITDQAakrleLSEEETRI 238
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
32-102 |
4.72e-03 |
|
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438715 [Multi-domain] Cd Length: 110 Bit Score: 38.49 E-value: 4.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555165 32 NKSTTIGRHENS--DLVLQ-SPDIDNHHALIEYNeAECSFVLQDFNSRNGTFVNECHIQ-NVAVKLIPGDILRFG 102
Cdd:cd22663 20 GKEVTVGRGLGVtyQLVSTcPLMISRNHCVLKKN-DEGQWTIKDNKSLNGVWVNGERIEpLKPYPLNEGDLIQLG 93
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
236-459 |
5.07e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 236 EDLAQQDKDEIILLLGK---EVSRLSDY-EIESKYKDVIIANLQnevaelSQKVSETTTSRQNEKEISQKcqvLDEDIDA 311
Cdd:PRK05771 34 EDLKEELSNERLRKLRSlltKLSEALDKlRSYLPKLNPLREEKK------KVSVKSLEELIKDVEEELEK---IEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 312 KQKEIQSLKSQISALQKgyskvlcqtlseRNSEITSLKNEGENLK--RDNAITSGMVSSLQKDIlaKDEQVQQLKEEVSH 389
Cdd:PRK05771 105 LEEEISELENEIKELEQ------------EIERLEPWGNFDLDLSllLGFKYVSVFVGTVPEDK--LEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 390 LKSQNKDKDhqlealgsRCSVLKEELKQEDAHRELREAQEKELKL------------CKTQIQDMEKEMKKLRAELRKSC 457
Cdd:PRK05771 171 YISTDKGYV--------YVVVVVLKELSDEVEEELKKLGFERLELeeegtpselireIKEELEEIEKERESLLEELKELA 242
|
..
gi 1034555165 458 TE 459
Cdd:PRK05771 243 KK 244
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
653-718 |
5.55e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.39 E-value: 5.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034555165 653 LLQEKLREhlaeKEKLNEERLEQEeKLKAKIRQLTEEKAALEeyitQERNRAKETLEEERKRMQEL 718
Cdd:PLN02316 250 LLEEKRRE----LEKLAKEEAERE-RQAEEQRRREEEKAAME----ADRAQAKAEVEKRREKLQNL 306
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
635-831 |
5.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 635 QAQELQIKFNSSQETQQSLLQE--KLREHLAEKEKlneeRLeQEEKLKAKIRQLTEEKAALEEYIT---QERNRAKETLE 709
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQlpELRKELEEAEA----AL-EEFRQKNGLVDLSEEAKLLLQQLSeleSQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 710 EERKRMQELESLLAQQKKALAK-SITQEKNRVKEALEEEQTRVQELEER----------LARQKEVLESSIAHEKRKAKE 778
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPElLQSPVIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034555165 779 ALESEKRKVQDLENHLTQQKEISESNIAyekrkakeamekekkKVQDLENRLT 831
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLA---------------ELPELEAELR 354
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
271-414 |
6.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 271 IANLQNEVAELS----------QKVSETTTSRQNEKEISQK----------CQVLDEDIDAKQKEIQSLKSQISALQKGY 330
Cdd:PHA02562 236 IEELTDELLNLVmdiedpsaalNKLNTAAAKIKSKIEQFQKvikmyekggvCPTCTQQISEGPDRITKIKDKLKELQHSL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 331 SKVLC--QTLSERNSEITSLKNEGENLKRDnaitsgmVSSLQKDILAKDEQVQQLKEEVSHLKSQNKDKD-------HQL 401
Cdd:PHA02562 316 EKLDTaiDELEEIMDEFNEQSKKLLELKNK-------ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAeelaklqDEL 388
|
170
....*....|...
gi 1034555165 402 EALGSRCSVLKEE 414
Cdd:PHA02562 389 DKIVKTKSELVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
655-810 |
6.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 655 QEKLREHLAEKEKLNEERLEQEE---KLKAKIRQLTEEKAA---LEEYITQERN-----RAKETLEEERKRM-------Q 716
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEErleALEAELDALQERREAlqrLAEYSWDEIDvasaeREIAELEAELERLdassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 717 ELESLLAQQKKALaKSITQEKNRVKEALEEEQTRVQELEERLARQKEVLESSIAHEKRKAKEALESEKRKVQDLENHLTQ 796
Cdd:COG4913 689 ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170
....*....|....
gi 1034555165 797 QKEISESNIAYEKR 810
Cdd:COG4913 768 RENLEERIDALRAR 781
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
366-947 |
6.30e-03 |
|
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: 41.26 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 366 VSSLQKDILAKDEQVQQLKEE----VSHLKSQNKDK------DHQLEALG--SRCSVLKEELKQEDAHRELREAQEK-EL 432
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSEsqnkIELLLQQHQDRieqlisEHEVEITGltEKASSARSQANSIQSQLEIIQEQARnQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 433 KLCKTQIQDMEKEMKKLRAELRKScteqsviSRTLREksKLEHFRSQVIKAT--YGRAKPFRDKPVTDQQLIEKITQVTE 510
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREA-------KRMYED--KIEELEKQLVLANseLTEARTERDQFSQESGNLDDQLQKLL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 511 DNINFQQKKWTLQKETQ-------------LSNSKQEETTENIEK------LRTSLDSCQACMK-----ISCCSHDLKKE 566
Cdd:pfam15921 384 ADLHKREKELSLEKEQNkrlwdrdtgnsitIDHLRRELDDRNMEVqrlealLKAMKSECQGQMErqmaaIQGKNESLEKV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 567 VDLLQHLQVSPPVsgLQKVVLDVLRHALSwLEEVEQLLRDLGILPSSPNKGFSLYLIYLLEHYKKLMSQAQELQIKFNSS 646
Cdd:pfam15921 464 SSLTAQLESTKEM--LRKVVEELTAKKMT-LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 647 QETQQSLLQ-EKLREHLAEKEKLNEERLEQEEKLKAKIRQ-------LTEEKAALEEYITQERNRAKE---TLEEERKRM 715
Cdd:pfam15921 541 DHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 716 QELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQELEERLARQKEVleSSIAHEKRKAKEALESEKRKVQDLENHLT 795
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL--NSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 796 QQKEISESNIAYEKRKAKEAMEKEKKKVQ---DLENRLTKQKEELELKEQKEDVLNNKLSDAlamveetqkTKATESLKA 872
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTNA---------NKEKHFLKE 769
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034555165 873 ESlaLKLNETLAELETTKTKMIMVEERLILQQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLeeKLQ 947
Cdd:pfam15921 770 EK--NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRL--KLQ 840
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
376-475 |
6.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 376 KDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRK 455
Cdd:COG2433 411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEE 490
|
90 100
....*....|....*....|
gi 1034555165 456 SCTEQsvisRTLREKSKLEH 475
Cdd:COG2433 491 LKRKL----ERLKELWKLEH 506
|
|
| FHA_CHK2 |
cd22666 |
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ... |
27-82 |
6.99e-03 |
|
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438718 [Multi-domain] Cd Length: 112 Bit Score: 37.99 E-value: 6.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034555165 27 GFFVL---NKSTTIGRHENSDLVLQSPDIDNH---------HALI--EYNEAECSFV-LQDFnSRNGTFVN 82
Cdd:cd22666 10 GFSSLdlvKDEYTFGRDKSCDYCFDSPALKKTsyyrtyskkHFRIfrEKGSKNTYPVfLEDH-SSNGTFVN 79
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-474 |
7.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 285 VSETTTSRQNEKEISQkcqvLDEDIDAKQKEIQSLKSQISALQKGYSKvLCQTLSERNSEITSLKNEGENLKRDNAITSG 364
Cdd:COG4942 16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 365 MVSSLQKDILAKDEQVQQL---------KEEVSHLKSQN--KDKDHQLEALGSRCSVLKEELKQEDAHRELREAQEKELK 433
Cdd:COG4942 91 EIAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034555165 434 LCKTQIQDMEKEMKKLRAELRKSCTEQSVISRTLREKSKLE 474
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
274-455 |
7.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 274 LQNEVAELSQKVSETTTS----RQNEKEISqkcqvLDEDIDAKQKEIQSLKSQISALQkgyskvlcqtlsernSEITSLK 349
Cdd:COG3206 180 LEEQLPELRKELEEAEAAleefRQKNGLVD-----LSEEAKLLLQQLSELESQLAEAR---------------AELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 350 NEGENLKRDNAITSGMVSSLQKD--ILAKDEQVQQLKEEVSHLKSQNKDKDHQLEALGSRCSVLKEELKQEDahRELREA 427
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA--QRILAS 317
|
170 180
....*....|....*....|....*...
gi 1034555165 428 QEKELKLCKTQIQDMEKEMKKLRAELRK 455
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
309-456 |
7.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 309 IDAKQKEIQSLKSQISALQKgyskvlcqtlsernsEITSLKNEGENL--KRDNAITSGMVSSLQKDILAKDEQVQQLKEE 386
Cdd:COG4913 612 LAALEAELAELEEELAEAEE---------------RLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 387 VSHLKSQNKDkdhqLEALGsrcsvlkeelKQEDAHRELREAQEKELKLCKTQIQDMEKEMKKLRAELRKS 456
Cdd:COG4913 677 LERLDASSDD----LAALE----------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
701-783 |
7.85e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 701 RNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRVKEALEEEQTRVQEL----EERLARQKEVLESSIAHEKRKA 776
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEIlaeaKEEAERILEQAKAEIEQEKEKA 111
|
....*..
gi 1034555165 777 KEALESE 783
Cdd:cd06503 112 LAELRKE 118
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-762 |
8.02e-03 |
|
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: 40.82 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 313 QKEIQSLKSQISALQkgyskvlcqtlsernSEITSLKNEGENLKRDNAITSGMVSSLQKDIlakdeqvQQLKEEVSHLKS 392
Cdd:TIGR02169 680 RERLEGLKRELSSLQ---------------SELRRIENRLDELSQELSDASRKIGEIEKEI-------EQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 393 QNKDKDHQLEAlgsrCSVLKEELKQEDAHRElREAQEKELKLCKtqiqdMEKEMKKLRAELRKSCTEQSVisrtlREKSK 472
Cdd:TIGR02169 738 RLEELEEDLSS----LEQEIENVKSELKELE-ARIEELEEDLHK-----LEEALNDLEARLSHSRIPEIQ-----AELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 473 LEHFRSQVIKATYGRAKPFRDKPVTDQQLIEKITQVTEDNINFQQKKWTLQKETQLSNSKQEETTENIEKLRTSLDSCQA 552
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 553 CMKisccshDLKKEVDLLQhlqvsppvsglqkvvldvlrhalSWLEEVEQLLRDLGIlpsspnkgfslyliyLLEHYKKL 632
Cdd:TIGR02169 883 RLG------DLKKERDELE-----------------------AQLRELERKIEELEA---------------QIEKKRKR 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 633 MSQaqelqikfnssQETQQSLLQEKLREHLAEKEKLNEERLEQ--EEKLKAKIRQLTEEKAALEEYitqeRNRAKETLEE 710
Cdd:TIGR02169 919 LSE-----------LKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRALEPV----NMLAIQEYEE 983
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034555165 711 ERKRMQELesllaqqkkalaksitQEKnrvKEALEEEQTRVQELEERLARQK 762
Cdd:TIGR02169 984 VLKRLDEL----------------KEK---RAKLEEERKAILERIEEYEKKK 1016
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
911-1105 |
8.31e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 911 QDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKIEGEIATLKdndpAPKEERPQDPLVapmtessaKD 990
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELK----EQNEELEKQYKV--------KK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 991 MAYEHLIDDllaaqkeilsqQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVLKEKMAQMSSL 1070
Cdd:pfam05667 391 KTLDLLPDA-----------EENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKEL 459
|
170 180 190
....*....|....*....|....*....|....*
gi 1034555165 1071 vekkDRELKALEEALRASQEKHRlQLNTEKEQKPR 1105
Cdd:pfam05667 460 ----REKIKEVAEEAKQKEELYK-QLVAEYERLPK 489
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
270-390 |
8.41e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 270 IIANLQNEVAELSQKVSETTTSRQNEKEIsqkcqvLDEdIDAKQKEIQSLKSQISALQkgyskvlcQTLSERNSEITSLK 349
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEI------MDE-FNEQSKKLLELKNKISTNK--------QSLITLVDKAKKVK 364
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034555165 350 NEGENLKRDNAITSGMVSSLQKDILAKDEQVQQLKEEVSHL 390
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
625-1093 |
8.61e-03 |
|
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: 40.72 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 625 LLEHYKKLMSQAQELQIKFNSSQETQQSLLQEKLREHLAEKEKLNEERLEQEEKLKAKIRQLTEEKAALEEYITQERNRA 704
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 705 KETLEEERKRMQELESLLaQQKKALAKSITQEKNRVKEALEEEQTR------------VQELEERLARQKEVLESSIAHE 772
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFrdlqgqlahakkQQELQQRYAELCAAAITCTAQC 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 773 K-------RKAKEALESEKRKVQDLENHLTQQKEIS------------------ESNIAYE-KRKAKEAMEKEKKKVQDL 826
Cdd:TIGR00618 454 EklekihlQESAQSLKEREQQLQTKEQIHLQETRKKavvlarllelqeepcplcGSCIHPNpARQDIDNPGPLTRRMQRG 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 827 ENRLTKQKEELELKEQKEDVLNNKLSDALAMVEETQKTKATESLKAESLALKLNETLAELETTKTKMIMVEE----RLIL 902
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEaedmLACE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 903 QQKMVKALQDEQESQRHGFEEEIMEYKEQIKQHAQTIVSLEEKLQKVTQHHKKI-EGEIATLKDNDPAPKEERPQDPLVA 981
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKMQSEKEQLT 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 982 PMTESSA-KDMAYEHLIDDLLAAQKEILSQQEVIMKLRKDLTEAHSRMSDLRGELNEKQKMELEQNVVLVQQQSKELSVL 1060
Cdd:TIGR00618 694 YWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034555165 1061 KEKMAQMSSL---VEKKDRELKALEEALRASQEKHR 1093
Cdd:TIGR00618 774 LQTGAELSHLaaeIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
694-783 |
8.76e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 38.06 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034555165 694 EEYITQERNRAKETLEEERKRMQELESLLAQQKKALAKSITQEKNRV----KEALEEEQTRVQELEERLARQkevlessI 769
Cdd:PRK07353 38 EDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAEAdklaAEALAEAQAEAQASKEKARRE-------I 110
|
90
....*....|....
gi 1034555165 770 AHEKRKAKEALESE 783
Cdd:PRK07353 111 EQQKQAALAQLEQQ 124
|
|
| |
