|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
2.42e-80 |
|
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: 254.11 E-value: 2.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 882939013 83 QRLSRGSEESPPCEILSGDIIQFGVDVTENTRKVTHGCIVSTIKLFLP 130
Cdd:cd22679 79 QRLSKGSEESEPRELHSGDIVQFGVDVVENSRKVTHGCIVATVTLFLP 126
|
|
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
163-225 |
1.82e-26 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 102.76 E-value: 1.82e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939013 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-812 |
4.42e-19 |
|
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: 92.81 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSlrKELIA 242
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--EELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 243 LQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELA--------NKYNGAVNEI 314
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeaelKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 315 KDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA-DNDFTNERLTALQVRLEHLQEKTLKECS 393
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlQENLEGFSEGVKALLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 394 SLGIQVD------------DFLPKINGSTEK------EHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKEN 455
Cdd:TIGR02168 526 SELISVDegyeaaieaalgGRLQAVVVENLNaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 456 QAKAKESDLSDTLSP--SKEKSSDDTTDAQMDEQDLNEPLAKVSL-----------LKDDLQGTQSETEAKQDIQHLRKE 522
Cdd:TIGR02168 606 DLVKFDPKLRKALSYllGGVLVVDDLDNALELAKKLRPGYRIVTLdgdlvrpggviTGGSAKTNSSILERRREIEELEEK 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 523 LVEAQELARTSKQkcfELQALlEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQD 599
Cdd:TIGR02168 686 IEELEEKIAELEK---ALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEA 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 600 EILLLRQA---AAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL- 672
Cdd:TIGR02168 762 EIEELEERleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLe 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 673 ---------QGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK 743
Cdd:TIGR02168 842 dleeqieelSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 744 EQHlrdaADLKTLLSKAENQAKDVQkeyektQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:TIGR02168 922 EKL----AQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.34e-17 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438744 [Multi-domain] Cd Length: 139 Bit Score: 79.92 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 882939013 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
4.73e-15 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438747 [Multi-domain] Cd Length: 133 Bit Score: 72.72 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-812 |
1.74e-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: 74.71 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 334 KGQAEKKELQT---KIDEMEEKEQELQAKIEALQAdndftneRLTALQVRLEHLQEKTLKECSSLgiQVDDFLPKINGST 410
Cdd:TIGR02168 373 RLEELEEQLETlrsKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKL--EEAELKELQAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 411 EKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKL-SKENQAKAKESDLSDTLSPSKE-----KSSDDTTDAQM 484
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaQLQARLDSLERLQENLEGFSEGvkallKNQSGLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 485 DEQDLNEP-----LAKVSLLKDDLQG--TQSETEAKQDIQHLRK-----------------ELVEAQELARTSKQKCFEL 540
Cdd:TIGR02168 524 VLSELISVdegyeAAIEAALGGRLQAvvVENLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 541 QALLEEERKAYRNQVE------------ESAKQIQVLQVQLQKL-----------------HMDMENLQEEKDTEISSTR 591
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRREIEELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 592 DKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQRE---- 667
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEltel 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 668 -----------------------EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSD 724
Cdd:TIGR02168 760 eaeieeleerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 725 LSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 804
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
....*...
gi 882939013 805 NLKLLREK 812
Cdd:TIGR02168 916 ELEELREK 923
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.35e-13 |
|
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: 66.53 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 882939013 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
6.49e-13 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 64.13 E-value: 6.49e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939013 28 IKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRLSRgseesPPCEILSGDIIQF 105
Cdd:pfam00498 1 VTIGRS------PDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGP-----EPVRLKDGDVIRL 66
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
167-204 |
1.02e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.89 E-value: 1.02e-12
10 20 30
....*....|....*....|....*....|....*...
gi 882939013 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-804 |
2.14e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 228 SKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSlsnteDECTHLKEMneRTQEELRELANKY 307
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA-----DEAKKAEEK--KKADEAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 308 NGAvneiKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNErltalqvrlEHLQEK 387
Cdd:PTZ00121 1315 KKA----DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---------AKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 388 TLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGgdctfihqflECQKKlmvQGHLTKVVEESKLSKENQAKAKESDLSDT 467
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAA----------AAKKK---ADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 468 LspskEKSSDDTTDAQMDEQDLNEPlAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQElARTSKQKCFELQAlLEEE 547
Cdd:PTZ00121 1449 A----KKKAEEAKKAEEAKKKAEEA-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKK-AEEA 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 548 RKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE--KDTEISSTRDKLLSAQDEILLLRQA--AAEAVSERDTDFVSLQ 623
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 624 EELKKVRAE----LEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVL 699
Cdd:PTZ00121 1602 EEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 700 LSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE---KTQT 776
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIAH 1761
|
570 580
....*....|....*....|....*...
gi 882939013 777 VLSELKLKFEMTEQEKQSITDELKQCKD 804
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.47e-11 |
|
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: 61.53 E-value: 2.47e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 882939013 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
7.65e-11 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 59.20 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 882939013 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-679 |
1.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswQALIDEDRLLSRLEVMGNQLQAcsKNQTEDSLRKELIA 242
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEE--LEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 243 LQEDkhsyETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:COG1196 349 AEEE----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 323 VAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEcsSLGIQVDDF 402
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL--LLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 403 LPKINGSTEKEHLLSKSGGDCTFIHQFLECQKKL-------MVQGHLTKVVEESKLSKENQAKAKESDLS--DTLSPSKE 473
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaleaaLAAALQNIVVEDDEVAAAAIEYLKAAKAGraTFLPLDKI 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 474 KSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQkcfELQALLEEERKAYRN 553
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG---RLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 554 QVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAEL 633
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 882939013 634 EGWRKAASEYENEIRSLQSSFQlrcqqcEDQQREEATRLQGELEKL 679
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPD------LEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
516-812 |
9.60e-10 |
|
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: 62.39 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 516 IQHLRKELVEAQELARTSKQKCFELQALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLL 595
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 596 SAQDEIL-LLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsfQLRCQQCE-DQQREEATRLQ 673
Cdd:TIGR02169 265 KRLEEIEqLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 674 GELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR----- 748
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseel 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 749 -----DAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:TIGR02169 423 adlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-782 |
1.09e-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: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 241 IALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDK 320
Cdd:COG1196 298 ARLEQD-----------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 321 LKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLKEcsslgiqvd 400
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE--------- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 401 dflpkingSTEKEHLLSKsggdctfihqflecQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTT 480
Cdd:COG1196 438 --------EEEEEALEEA--------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 481 DAQMDEQDlnEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAqelartskqkcfeLQALLEEERKAYRNQVEESAK 560
Cdd:COG1196 496 LLEAEADY--EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 561 QIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAA 640
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA-DARYYVLGDTLLGRTLVAARLEAALRRA 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 641 SEYENEIRSLqssfqlrcqqcedqqREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFE 720
Cdd:COG1196 640 VTLAGRLREV---------------TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939013 721 LTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 782
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-748 |
2.30e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 228 SKNQTEDSLRKELIALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 302 ELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTK---IDEMEEKEQELQAKIEALQADNDfTNERLT 375
Cdd:PRK03918 290 EKAEEYiklSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHE-LYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 376 ALQVRLEHLQ-----------EKTLKECSSLGIQVDDFLPKINGstEKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLtk 444
Cdd:PRK03918 369 AKKEELERLKkrltgltpeklEKELEELEKAKEEIEEEISKITA--RIGELKKEIKELKKAIEELKKAKGKCPVCGRE-- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 445 VVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEP--LAKVSLLKDDLQGTQSETEaKQDIQHLRKE 522
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLK-KYNLEELEKK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 523 LVEAQELARTSKQKCFELQALLEE--ERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDE 600
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 601 ILLLRQAAAEaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcQQCEDQQREEATRLQGELEKLK 680
Cdd:PRK03918 604 YLELKDAEKE-LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS---EEEYEELREEYLELSRELAGLR 679
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939013 681 KEWDVLEtechSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR 748
Cdd:PRK03918 680 AELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALS 743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-807 |
3.50e-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: 60.85 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETTAKESLRRV--LQEKIE-V 268
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyAELKEELEDLRAELEEVDKEFAETRDELkdYREKLEkL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 269 VRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKE---LQTK 345
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEE 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 346 IDEMEEKEQELQAKIEALQADNDFTNER--------------------------------LTALQV----RLEHL---QE 386
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgvhgtvaqlgsvgeryATAIEVaagnRLNNVvveDD 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 387 KTLKECSSLGIQVD----DFLP--KINGSTEKEHLLSKSG-----------------------GDcTFIHQFLECQKKLM 437
Cdd:TIGR02169 558 AVAKEAIELLKRRKagraTFLPlnKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyvfGD-TLVVEDIEAARRLM 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 438 VQGHLT----KVVEESKLSKENQAKAKESDL-SDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQgtQSETEA 512
Cdd:TIGR02169 637 GKYRMVtlegELFEKSGAMTGGSRAPRGGILfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS--QELSDA 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 513 KQDIQHLRKELVEAQELARTSKQKCFELQA---LLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISS 589
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 590 TRDKLLSAQDEIlllrqaaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEA 669
Cdd:TIGR02169 795 EIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 670 tRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRD 749
Cdd:TIGR02169 865 -ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939013 750 AADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCkDNLK 807
Cdd:TIGR02169 944 EEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY-EKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-811 |
4.04e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 324 AEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQ------VRLEHLQEKTLKECSSLGI 397
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKekaeeyIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 398 QVDDFLPKINGSTEK-EHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKEN--QAKAKESDLSdtlspskek 474
Cdd:PRK03918 315 RLSRLEEEINGIEERiKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLT--------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 475 ssddttdaqmdEQDLNEPLAKVSLLKDDLQGTQSE-TEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKA--- 550
Cdd:PRK03918 386 -----------PEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKell 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 551 --YRNQVEESAKQIQVLQVQLQKLHMDMENLqeekdteisstrDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKK 628
Cdd:PRK03918 455 eeYTAELKRIEKELKEIEEKERKLRKELREL------------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 629 VRAELEGWRKAASEYENEIRSLQSSFqlrcqqcedqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLS----SEL 704
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 705 QRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhLRDAADLKTLLSKAENQAKDVQKEY-EKTQTVLSELKL 783
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELEELEKKYsEEEYEELREEYL 669
|
570 580 590
....*....|....*....|....*....|..
gi 882939013 784 KFEM----TEQEKQSITDELKQCKDNLKLLRE 811
Cdd:PRK03918 670 ELSRelagLRAELEELEKRREEIKKTLEKLKE 701
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
167-386 |
4.40e-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: 60.47 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTE-----DSLRKELI 241
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvkselKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 242 ALQEDKHSYETTAKESLRRVLQEKI-EVVRKLSEVERSLSNTEDECTHL-KEMNERTQE------ELRELANKYNGAVNE 313
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEkeylekEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 314 IKDLSDKLKVAEGKQEEIQQKGQ----------AEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEH 383
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeleaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
...
gi 882939013 384 LQE 386
Cdd:TIGR02169 929 LEE 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
482-791 |
4.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 482 AQMDEQDLNEPLAKVSLLKDDLQGTQSE-TEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEEsak 560
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAElEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE--- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 561 qiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAA 640
Cdd:COG1196 297 -------------------LARLEQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 641 SEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEwDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFE 720
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882939013 721 LTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 791
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
1.13e-08 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 1.13e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 882939013 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
580-812 |
1.24e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 580 QEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQL--- 656
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLELEELELELEEAQAEEYElla 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 657 ---RCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK 733
Cdd:COG1196 296 elaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 734 ELEKQVGSLKEQHL---RDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLR 810
Cdd:COG1196 376 EAEEELEELAEELLealRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
..
gi 882939013 811 EK 812
Cdd:COG1196 456 EE 457
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 882939013 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-812 |
1.97e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 378 QVRLEHlQEKTLKECSSLGIQVDDFLPKINGS-TEKEHLlsksggdctfihqflecqkKLMVQGHlTKVVEEskLSKENQ 456
Cdd:PRK02224 240 DEVLEE-HEERREELETLEAEIEDLRETIAETeREREEL-------------------AEEVRDL-RERLEE--LEEERD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 457 AKAKESDLSDtlspskekSSDDTTDAQMDEQDlneplAKVSLLKDDL-QGTQSETEAKQDIQHLRKELVEAQELARTSKQ 535
Cdd:PRK02224 297 DLLAEAGLDD--------ADAEAVEARREELE-----DRDEELRDRLeECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 536 KCFELQALLEEERKAYRNQVEEsakqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSER 615
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREE----------------------IEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 616 DtdfvSLQEELKKVRAELEGWRKAASEYEneiRSLQSSfqlRCQQCE------------DQQREEATRLQGELEKLKKEW 683
Cdd:PRK02224 422 D----ELREREAELEATLRTARERVEEAE---ALLEAG---KCPECGqpvegsphvetiEEDRERVEELEAELEDLEEEV 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 684 DVLETECHSLKkenvllssELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQ 763
Cdd:PRK02224 492 EEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER----AAELEAEAEEKREA 559
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 882939013 764 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKDNLKLLREK 812
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-807 |
2.79e-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: 57.72 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLGIQVDDFLPKINgstEKEHLLSKSG 420
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKyndLKKQKEELENELNLLEKEKL---NIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 421 gdctfiHQFLECQKKLMVqghLTKVVEESKL--SKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 498
Cdd:TIGR04523 194 ------NKLLKLELLLSN---LKKKIQKNKSleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 499 LKDDLQGTQSETE-AKQDIQHLRKELVEAQ-ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDM 576
Cdd:TIGR04523 265 IKKQLSEKQKELEqNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 577 ENLQEE---KDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSS 653
Cdd:TIGR04523 345 SQLKKEltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 654 FQLRCQQCED------QQREEATRLQGE-------LEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFE 720
Cdd:TIGR04523 421 KELLEKEIERlketiiKNNSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 721 LTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMteQEKQSITDELK 800
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELK 574
|
....*..
gi 882939013 801 QCKDNLK 807
Cdd:TIGR04523 575 QTQKSLK 581
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
5.11e-08 |
|
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.
Pssm-ID: 214578 [Multi-domain] Cd Length: 52 Bit Score: 49.87 E-value: 5.11e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 882939013 28 IKIGRSvarcrPAQNNATFDCKVLSRNHALVWFDhKTSKFYLQDTKSSNGTFINSQRL 85
Cdd:smart00240 1 VTIGRS-----SEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
|
|
| FHA_TCF19 |
cd22685 |
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ... |
29-119 |
6.21e-08 |
|
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.
Pssm-ID: 438737 [Multi-domain] Cd Length: 130 Bit Score: 52.03 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 882939013 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-387 |
1.10e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 160 MYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEV-MGNQLQACSKNQTEDSLRK 238
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 239 ELIALQEDK-------HSYETTAKESLRRVLQE-KIEVVRKLSEVERSLSNTEDECTHLKEMNERTqEELRELANKYNGA 310
Cdd:TIGR02168 782 AEIEELEAQieqlkeeLKALREALDELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 311 VNE----IKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNE---RLTALQVRLEH 383
Cdd:TIGR02168 861 IEEleelIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQlelRLEGLEVRIDN 940
|
....
gi 882939013 384 LQEK 387
Cdd:TIGR02168 941 LQER 944
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-793 |
1.22e-07 |
|
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: 55.51 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 239 ELIALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:pfam15921 279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAK-------IEALQADNDFTNERLTalqvRLEHL 384
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQ----RLEAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 385 QEKTLKECSSlgiQVDDFLPKINGSTEKEHLLSKsggdctfIHQFLECQKKLmvqghLTKVVEESKlSKENQAKAKESDL 464
Cdd:pfam15921 435 LKAMKSECQG---QMERQMAAIQGKNESLEKVSS-------LTAQLESTKEM-----LRKVVEELT-AKKMTLESSERTV 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 465 SDTLSPSKEKS-SDDTTDAQMDE--QDLNEPLAKVSLLK---DDLQGTQSETEA---------------KQDI------- 516
Cdd:pfam15921 499 SDLTASLQEKErAIEATNAEITKlrSRVDLKLQELQHLKnegDHLRNVQTECEAlklqmaekdkvieilRQQIenmtqlv 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 517 -QHLRKE---LVEAQELARTSKQKCFELQAL--LEEERKAYRNQVEesAKQIQVLQVQLQKLHMDMENLQEEKD------ 584
Cdd:pfam15921 579 gQHGRTAgamQVEKAQLEKEINDRRLELQEFkiLKDKKDAKIRELE--ARVSDLELEKVKLVNAGSERLRAVKDikqerd 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 585 ---TEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRkaaseyeNEIRSLQSSFQLRCQQC 661
Cdd:pfam15921 657 qllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR-------NTLKSMEGSDGHAMKVA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 662 EDQQReEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVgs 741
Cdd:pfam15921 730 MGMQK-QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV-- 806
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 882939013 742 lkeqhlrdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 793
Cdd:pfam15921 807 ---------ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
275-688 |
2.72e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 275 VERSLSNTEDECTHLKEMNERTQEelRELANKYNGAVNEIKDLSDKLKVAEGKQEE-IQQKGQA-----EKKELQTKIDE 348
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQaRETRDEAdevleEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 349 MEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGDC-T 424
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 425 FIHQFLECQKKLMVQghlTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDE-----QDLNEPLAKVSL 498
Cdd:PRK02224 336 AAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEiEELEEEIEElrerfGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 499 LKDDLQGT-----QSETEAKQDIQHLRKELVEAQELarTSKQKCFELQALLEEERKA-----YRNQVEESAKQIQVLQVQ 568
Cdd:PRK02224 413 FLEELREErdelrEREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVEGSPHVetieeDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 569 LQKLHMDMENLQEEKDTEisSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIr 648
Cdd:PRK02224 491 VEEVEERLERAEDLVEAE--DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA- 567
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 882939013 649 slqssfqlrcqqceDQQREEATRLQGELEKLKKEWDVLET 688
Cdd:PRK02224 568 --------------EEAREEVAELNSKLAELKERIESLER 593
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
256-786 |
3.04e-07 |
|
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: 54.41 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQE---ELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVR---LEHLQEKTLKECSSLGIQVDDFLPKINGS 409
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 410 TEKEHLLSKsggdctfihqflecqkklmvqghlTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDL 489
Cdd:pfam01576 172 EEKAKSLSK------------------------LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 490 NEPLA--KVSLLK--DDLQGTQS--ETEAKQDIQHLRK---------ELVEAQELARTSKQKCFELQALLEEERKAYRNQ 554
Cdd:pfam01576 228 QAQIAelRAQLAKkeEELQAALArlEEETAQKNNALKKireleaqisELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 555 VEESAKQIQVLQVQLQKLHMDMENLQ----EEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELK 627
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKkaleEETrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 628 KVRAELEGWRKAASEYENEIRSLQSS---FQLRCQQCEDQQREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLS 701
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQlqeLQARLSESERQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 702 SELQRQEKELHNSQKQSFELTSDLsilqmtrKELEKQVGSLKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSEL 781
Cdd:pfam01576 468 SQLQDTQELLQEETRQKLNLSTRL-------RQLEDERNSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDM 529
|
....*
gi 882939013 782 KLKFE 786
Cdd:pfam01576 530 KKKLE 534
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
8.27e-07 |
|
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: 48.00 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 882939013 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-684 |
1.43e-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: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 263 QEKIEVVRKLSEVERSLSNTEDEcthLKEMnERTQEELR---ELANKYNGAVNEIKDLSDKLKVAEGKQEEiqqkgqAEK 339
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDI---LNEL-ERQLKSLErqaEKAERYKELKAELRELELALLVLRLEELR------EEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 340 KELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKTLkecsSLGIQVDDFlpkingSTEKEHLlsks 419
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRL------EQQKQIL---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 420 ggdctfihqflecqkklmvqghltkvvEESKLSKENQAKAKESDLsdtlspskekssddttdaQMDEQDLNEPLAKVSLL 499
Cdd:TIGR02168 308 ---------------------------RERLANLERQLEELEAQL------------------EELESKLDELAEELAEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 500 KDDLQgtqsetEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAY---RNQVEESAKQIQVLQVQLQKLHMDM 576
Cdd:TIGR02168 343 EEKLE------ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 577 ENLQEEKDTEISS-TRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSsfq 655
Cdd:TIGR02168 417 ERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQA--- 489
|
410 420
....*....|....*....|....*....
gi 882939013 656 lRCQQCEDQQREEATRLQGELEKLKKEWD 684
Cdd:TIGR02168 490 -RLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
1.97e-06 |
|
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: 47.35 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 882939013 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.99e-06 |
|
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: 46.64 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 882939013 106 G 106
Cdd:cd22698 86 G 86
|
|
| FHA_PP2C70-like |
cd22678 |
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ... |
27-117 |
2.18e-06 |
|
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: 46.97 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 882939013 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
233-801 |
2.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 233 EDSLRKELIALQ-EDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:COG1196 222 LKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 312 NEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQEKTLKE 391
Cdd:COG1196 302 QDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAE-------EELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 392 CSSLGIQVDDFlpkingSTEKEHLLSKsggdctfihqflecqkklmvqghltkvvEESKLSKENQAKAKESDLSDTLsps 471
Cdd:COG1196 371 EAELAEAEEEL------EELAEELLEA----------------------------LRAAAELAAQLEELEEAEEALL--- 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 472 KEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKcfELQALLEEERKAY 551
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 552 RNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRA 631
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 632 E-----LEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQR 706
Cdd:COG1196 572 GratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 707 QEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFE 786
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570
....*....|....*
gi 882939013 787 MTEQEKQSITDELKQ 801
Cdd:COG1196 732 AEREELLEELLEEEE 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-812 |
2.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 539 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTd 618
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 619 fvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLKKEWDVLETEchslKKENV 698
Cdd:COG1196 300 ---LEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEEAEAELAEAEEA----LLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 699 LLSSELQRQEKELhnsQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVL 778
Cdd:COG1196 372 AELAEAEEELEEL---AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270
....*....|....*....|....*....|....
gi 882939013 779 SELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.72e-06 |
|
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: 46.16 E-value: 3.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 882939013 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-804 |
4.21e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 235 SLRKELIALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQT---KIDEMEEKEQELQAKIEALQadndftnerltalqvrlehlqektl 389
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN------------------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 390 kecsslgiqvddflpkingsTEKEHLLSKSggdctfIHQFLECQKKlmvqghlTKVVEESKLSKENQakaKESDLSDTLS 469
Cdd:TIGR04523 302 --------------------NQKEQDWNKE------LKSELKNQEK-------KLEEIQNQISQNNK---IISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 470 PSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEA-KQDIQHLRKELVEAQELARTSKQKCFELQA---LLE 545
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQQekeLLE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 546 EERKAYRNQVEESAKQIQvlqvqlqklhmDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAaaeaVSERDTDFVSLQEE 625
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIK-----------DLTNQDSVKELIIKNLDNTRESLETQLKVLSRS----INKIKQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 626 LKKVRAELEGWRKAASEYENEIRSL---QSSFQLRCQQCEdqqrEEATRLQGELEKLKKEWDVLETECHSLKKENVLLss 702
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLtkkISSLKEKIEKLE----SEKKEKESKISDLEDELNKDDFELKKENLEKEID-- 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 703 ELQRQEKELHNSQKqsfELTSDLSILQMTRKELEKQVGSLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 782
Cdd:TIGR04523 565 EKNKEIEELKQTQK---SLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
570 580
....*....|....*....|..
gi 882939013 783 LKFEMTEQEKQSITDELKQCKD 804
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRN 659
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-387 |
9.06e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 882939013 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-811 |
1.06e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 161 YSQELFQLSQYLQEA--LHREQ--MLEQKLATLQRLLAITQEASDtswqALIDedrlLSRLEvmgNQLQACSKNQTEDSL 236
Cdd:pfam15921 83 YSHQVKDLQRRLNESneLHEKQkfYLRQSVIDLQTKLQEMQMERD----AMAD----IRRRE---SQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 237 RKELIA--LQEDKHSYETTAKESLRR-------VLQEKIEVVRKLSEVERSLSNTEDECT--HLKEMNERTQEELRELAN 305
Cdd:pfam15921 152 HELEAAkcLKEDMLEDSNTQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMStmHFRSLGSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 306 kyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKEL-QTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL 384
Cdd:pfam15921 232 -------EISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 385 QEKTLKECSSLGIQVDDFlpkinGSTEKEHLLSKSGGDCTFIHQFLECQKKL-MVQGHLTKV-VEESKLSKE--NQAKAK 460
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDL-----ESTVSQLRSELREAKRMYEDKIEELEKQLvLANSELTEArTERDQFSQEsgNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 461 ESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAkvsllkddlqgtqseteakqdIQHLRKEL----VEAQELARTSKQK 536
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT---------------------IDHLRRELddrnMEVQRLEALLKAM 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 537 CFELQALLEEERKAYRNQVEESAKqiqvlqvqlqklhmdmenlqeekdteISSTRDKLLSAQDeilLLRQAAAEAVSERD 616
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEK--------------------------VSSLTAQLESTKE---MLRKVVEELTAKKM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 617 TdFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQqcedqqreeatrlqgELEKLKKEWDVL---ETECHSL 693
Cdd:pfam15921 490 T-LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQ---------------ELQHLKNEGDHLrnvQTECEAL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 694 KKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG----SLKE-QHLRDAADLKtlLSKAENQAKDVQ 768
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdrrlELQEfKILKDKKDAK--IRELEARVSDLE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 882939013 769 KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 811
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
622-806 |
1.74e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 622 LQEELKKVRAELEGWRKAASEY---ENEIRSLQSSFQL----RCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLK 694
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYrelKEELKELEAELLLlklrELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 695 KENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTL---LSKAENQAKDVQKEY 771
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEEL 353
|
170 180 190
....*....|....*....|....*....|....*
gi 882939013 772 EKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNL 806
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.25e-05 |
|
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: 44.18 E-value: 2.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 882939013 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-688 |
2.28e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 234 DSLRKELIALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTK-------IDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHL 384
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 385 QEKTLKECSSLGIQVDDFLPKINGStekehLLSKSGGDCTFIHQFLECQKKLMVQGHLTkVVEESKLSKENQAKAKESDL 464
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 465 SDTLsPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLkddlqgtqsetEAKQDIQHLRKELVEAQELARTSKQKCF--ELQA 542
Cdd:COG4717 307 LQAL-PALEELEEEELEELLAALGLPPDLSPEELL-----------ELLDRIEELQELLREAEELEEELQLEELeqEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 543 LLE----EERKAYRNQVEESAKqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvsERDTD 618
Cdd:COG4717 375 LLAeagvEDEEELRAALEQAEE-------------------YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 619 FVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLrcqqceDQQREEATRLQGELEKLKKEWDVLET 688
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.58e-05 |
|
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: 44.08 E-value: 2.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939013 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
2.96e-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: 43.48 E-value: 2.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
3.30e-05 |
|
second 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 second one. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438742 [Multi-domain] Cd Length: 105 Bit Score: 43.43 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 882939013 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.48e-05 |
|
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: 43.29 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 882939013 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
210-812 |
3.53e-05 |
|
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: 47.76 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 210 EDRLLSRLEVMGNQLQacsKNQTEDSLRKELIALQEDKHSYETTAK--------ESLRRVLQEKIEVVRKLSEVERSLSN 281
Cdd:TIGR02169 186 IERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELlkekealeRQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 282 TEDECTH----LKEMNER----TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ---QKGQAEKKELQTKIDEME 350
Cdd:TIGR02169 263 LEKRLEEieqlLEELNKKikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 351 EKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK---TLKECSSLGIQVDDFLPKINGS----TEKEHLLSKSGGDC 423
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaeTRDELKDYREKLEKLKREINELkrelDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 424 TFIHQFLEC--QKKLMVQGHLTKVVEESKLSKEN----------------QAKAKESDLSDTLSPSKEKSSDDTTDAQMD 485
Cdd:TIGR02169 423 ADLNAAIAGieAKINELEEEKEDKALEIKKQEWKleqlaadlskyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 486 EQDLNEPLAKVSLLKDDLQG-------------------------------TQSETEAKQDIQHLRKE------------ 522
Cdd:TIGR02169 503 EERVRGGRAVEEVLKASIQGvhgtvaqlgsvgeryataievaagnrlnnvvVEDDAVAKEAIELLKRRkagratflplnk 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 523 ------------------------------------------LVEAQELAR---------TSKQKCFELQALL----EEE 547
Cdd:TIGR02169 583 mrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAARrlmgkyrmvTLEGELFEKSGAMtggsRAP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 548 RKAYRNQVEESAKqiqvlqvqLQKLHMDMENLQEEKDTeISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELK 627
Cdd:TIGR02169 663 RGGILFSRSEPAE--------LQRLRERLEGLKRELSS-LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 628 KVRAELEGWRKAASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQGELEKLKKE-----WDVLETECHSLKKENVLLSS 702
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 703 ELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL-KEQHLRDA--ADLKTLLSKAENQAKDVQKEYEKTQTVLS 779
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIeKEIENLNGkkEELEEELEELEAALRDLESRLGDLKKERD 892
|
730 740 750
....*....|....*....|....*....|...
gi 882939013 780 ELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
3.72e-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: 47.07 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 153 VAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQT 232
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE---QELAA--LEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 233 EDSLRKELIALQEDKHSYETTAKESLRRV----LQEKIEVV---RKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 306 KyngaVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQ 385
Cdd:COG4942 165 L----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 882939013 386 EKT 388
Cdd:COG4942 241 ERT 243
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-557 |
4.95e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 369 ftNERLTALQVRLEHlQEKTLKECSSLGIQVDDFLPKINgsteKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEE 448
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 449 SKLSKENQAKAKEsdlsdtlspskEKSSDDTTDAQMDEQDLNeplAKVSLLKDDLQGTQSET-EAKQDIQHLRKELV-EA 526
Cdd:PHA02562 313 HSLEKLDTAIDEL-----------EEIMDEFNEQSKKLLELK---NKISTNKQSLITLVDKAkKVKAAIEELQAEFVdNA 378
|
250 260 270
....*....|....*....|....*....|.
gi 882939013 527 QELArtskqkcfELQALLEEERKAYRNQVEE 557
Cdd:PHA02562 379 EELA--------KLQDELDKIVKTKSELVKE 401
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
7.13e-05 |
|
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: 42.22 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 882939013 92 SPPC--EILSGDIIQFGvDVT 110
Cdd:cd22665 74 KPNVryELIDGDLLLFG-DVK 93
|
|
| FHA_NBN |
cd22667 |
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ... |
52-107 |
7.56e-05 |
|
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: 42.70 E-value: 7.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 882939013 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-387 |
8.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 8.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939013 310 AVNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEK 387
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
585-817 |
9.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 585 TEISSTRDKLLSAQDEILLLRQAAAEAvserdTDFVSLQEELKKVRAELEGWR-----KAASEYENEIRSLQSsfQLrcq 659
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA-----ERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRA--EL--- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 660 qceDQQREEATRLQGELEKLKKEWDVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsfeltsdlsiLQMTRKELEKQ 738
Cdd:COG4913 305 ---ARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEAL 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 739 VGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQckdnlklLREKGNNKP 817
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-------LERRKSNIP 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
299-812 |
1.03e-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: 46.17 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 299 ELRELANKYNGAVNEIKDLSDKLKVAEG---KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLT 375
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKnlnKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 376 aLQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEH--LLSKSGGDCTFIHQFLECQKKLmvqgHLTKVVEESKLSK 453
Cdd:TIGR04523 114 -NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEkeLEKLNNKYNDLKKQKEELENEL----NLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 454 ENQAKAKESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKDDLQgtqsetEAKQDIQHLRKELVEAQELARTS 533
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIE------KKQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 534 KQKCFELQALLEEERKayrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISStrdkllsaqdeilllrqaaaeavs 613
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------------------------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 614 erdtdfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATrLQGELEKLKKEWDVLETECHSL 693
Cdd:TIGR04523 311 -------ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE-KQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 694 KKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAA-----------------DLKTL 756
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikdltnqdsvkeliikNLDNT 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 882939013 757 LSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-811 |
1.13e-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: 46.19 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftn 371
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 372 eRLTALQVRLEHLQEKTLKECSSlgiqvddfLPKINGSTEKEHLLSksggdctfihqflecQKKLMVQGHLTKVVEESKL 451
Cdd:TIGR00606 465 -QLEGSSDRILELDQELRKAERE--------LSKAEKNSLTETLKK---------------EVKSLQNEKADLDRKLRKL 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 452 SKENQAKAKESD-LSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQEla 530
Cdd:TIGR00606 521 DQEMEQLNHHTTtRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNK-- 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 531 rtskqkcfELQAlLEEERKAYRNQveesakqiqvlqvqlqklhmdmenlQEEKDTEISSTRDKLLSAQdeilllrqaaae 610
Cdd:TIGR00606 599 --------ELAS-LEQNKNHINNE-------------------------LESKEEQLSSYEDKLFDVC------------ 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 611 AVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQC------EDQQREEATRLQGELEKLKKEWD 684
Cdd:TIGR00606 633 GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQSKLRLAPDKLK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 685 VLETECHSLKKENVLL-------SSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL--KEQHLRDAADLKT 755
Cdd:TIGR00606 713 STESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEESAKVCLTDVT 792
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 882939013 756 LLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 811
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.46e-04 |
|
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: 41.54 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
501-711 |
1.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 501 DDLQGTQSETE-AKQDIQHLRkELVEAQELARTSKQKCFELQALLEEeRKAYRNQVEesakqiqvlqvqLQKLHMDMENL 579
Cdd:COG4913 235 DDLERAHEALEdAREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRR------------LELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 580 QEEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSS--- 653
Cdd:COG4913 301 RAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPlpa 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939013 654 --------------FQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKEL 711
Cdd:COG4913 378 saeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-350 |
1.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|...
gi 882939013 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
572-830 |
2.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 572 LHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQ 651
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 652 SSFQLRcqqcedQQREEATRLQGELEKLKKEWDvletechslkkenvllssELQRQEKELHNSQKQSFELTSDLSILQMT 731
Cdd:COG4717 123 KLLQLL------PLYQELEALEAELAELPERLE------------------ELEERLEELRELEEELEELEAELAELQEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 732 RKELEKQVGSLKEQHLRDAAdlktllskaenqakdvqKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 811
Cdd:COG4717 179 LEELLEQLSLATEEELQDLA-----------------EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
250
....*....|....*....
gi 882939013 812 KGNNKPWPWMPMLAALVAV 830
Cdd:COG4717 242 EERLKEARLLLLIAAALLA 260
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
2.05e-04 |
|
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438724 [Multi-domain] Cd Length: 108 Bit Score: 41.51 E-value: 2.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 882939013 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-816 |
3.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 326 GKQEEIQQKGQAEKKELQTKIDEMEEKEQElqAKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPK 405
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 406 INGSTEKEHLLSKSGGDCTFIHQFLECQKKLMVQgHLTKVVEESKLSKENQAKAKEsdlsdtlspSKEKSSDDTTDAQMD 485
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEE---------AKKKADAAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 486 EQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELARTSKQKCFELQALLEEERKAyRNQVEESAKQIQVL 565
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 566 QVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELegwRKAASEYEN 645
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA---KKKAEEAKK 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 646 EIRSLQSSFQLRcQQCEDQQREEATRLQGELEKL--KKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTS 723
Cdd:PTZ00121 1498 KADEAKKAAEAK-KKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 724 DLS-----ILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKlkfemTEQEKQSITDE 798
Cdd:PTZ00121 1577 NMAlrkaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEE 1651
|
570
....*....|....*...
gi 882939013 799 LKQCKDNLKLLREKGNNK 816
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKK 1669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
575-816 |
3.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 575 DMENLQEEKDTEISSTRDKLLSAQDEILLLRqAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsf 654
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 655 QLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK- 733
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 734 --ELEKQVGSLKEQHlRDAADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 811
Cdd:PRK03918 347 lkELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
....*
gi 882939013 812 KGNNK 816
Cdd:PRK03918 420 EIKEL 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
589-780 |
3.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 589 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcedQQREE 668
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 669 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEkQVGSLKEQHLR 748
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----------LDELQDRLE-AAEDLARLELR 748
|
170 180 190
....*....|....*....|....*....|..
gi 882939013 749 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSE 780
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
313-696 |
4.25e-04 |
|
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: 44.29 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 313 EIKDLSDKLKVAEGKQEEIQQkgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtLKEC 392
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQS----ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED-LSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 393 SSlgiqvddflpkingstEKEHLLSKsggdctfihqflecqkklmvQGHLTKVVEESKLSKeNQAKAKESDLSDTLSPSK 472
Cdd:TIGR02169 750 EQ----------------EIENVKSE--------------------LKELEARIEELEEDL-HKLEEALNDLEARLSHSR 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 473 EKSSDDTTDAQMDE--------QDLNEPLAKVSLLKDDLQGTQSETEAKQ-DIQHLRKELVEAQELARTSKQKcfelqal 543
Cdd:TIGR02169 793 IPEIQAELSKLEEEvsriearlREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIKSIEKEIENLNGKKEE------- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 544 LEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQ 623
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 624 EE------LKKVRAELEgwrkaasEYENEIRSLQSSFQLRCQQCEDQQREEaTRLQGELEKLKKEWDVLE---TECHSLK 694
Cdd:TIGR02169 945 EIpeeelsLEDVQAELQ-------RVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILeriEEYEKKK 1016
|
..
gi 882939013 695 KE 696
Cdd:TIGR02169 1017 RE 1018
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
5.06e-04 |
|
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: 39.93 E-value: 5.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 882939013 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
577-812 |
5.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 577 ENLQEEK--DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF 654
Cdd:PHA02562 178 ELNQQIQtlDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 655 QlrcqqcedQQREEATRLQGELEKLKKEWDVLE--TECHSLKkenvllsSELQRQEKELHNSQKQSFELTSDLSILQMTR 732
Cdd:PHA02562 258 N--------KLNTAAAKIKSKIEQFQKVIKMYEkgGVCPTCT-------QQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 733 KELEKQVGSLKEQHLR------DAADLKTLLSKAENQAKDVQKEYEKTQTvlselklkfemteqEKQSITDELKQCKDNL 806
Cdd:PHA02562 323 DELEEIMDEFNEQSKKllelknKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAKLQDEL 388
|
....*.
gi 882939013 807 KLLREK 812
Cdd:PHA02562 389 DKIVKT 394
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-790 |
5.13e-04 |
|
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: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 238 KELIALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 316 DLsdKLKVAEGKQEeiQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQektlKECSSL 395
Cdd:pfam10174 286 FM--KNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLK-------ESLTAKEQRAAILQ----TEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 396 GIQVDdflpkingstEKEHLLSKSggdctfihqflecQKKLmvqghltkvveeSKLSKENQAKAKE-SDLSDTLSPSKEK 474
Cdd:pfam10174 351 RLRLE----------EKESFLNKK-------------TKQL------------QDLTEEKSTLAGEiRDLKDMLDVKERK 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 475 SSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQdiqhlrkELVEAQELARTSKQKCFE-LQALLEEERKAYRN 553
Cdd:pfam10174 396 INVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD-------TALTTLEEALSEKERIIErLKEQREREDRERLE 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 554 QVEESAKQIQVLQVQLQKLHMDMenlqEEKDTEISSTRDKLLSAQDEILLLRQAAAE---AVSERDTDFVSLQEELKKVR 630
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPEL----TEKESSLIDLKEHASSLASSGLKKDSKLKSleiAVEQKKEECSKLENQLKKAH 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 631 aELEGWRKAASEYENEIRSLQSSFQLRcqqcedqqREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKE 710
Cdd:pfam10174 545 -NAEEAVRTNPEINDRIRLLEQEVARY--------KEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 711 LHNSQKQsfeltsdlsiLQMTRKELEKQVGSLKEQHLRDAADLKTllSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQ 790
Cdd:pfam10174 616 QNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
5.26e-04 |
|
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: 40.49 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 882939013 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
6.57e-04 |
|
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: 39.59 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 882939013 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-386 |
6.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 331 IQQKGQAEKKELQT---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE 386
Cdd:PRK02224 361 LREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.86e-04 |
|
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: 39.40 E-value: 7.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 882939013 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
506-745 |
8.77e-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: 42.44 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 506 TQSETEAKQDIQHLRKELVEAQELARTSKQKcfelQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEekdt 585
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 586 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQssfqlrcqqcedQQ 665
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR------------AD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 666 REEATRLQGELEKLKKEWDVLETEchsLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ 745
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
527-729 |
8.90e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 527 QELARTSKQKcfelqaLLEEERKayRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQ 606
Cdd:pfam17380 396 QELEAARKVK------ILEEERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 607 AAAE-----AVSERDTDFVSLQEELKK--VRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR----EEATRLQGE 675
Cdd:pfam17380 468 QEEErkrkkLELEKEKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 882939013 676 LEKLKK--EWDVLETECHSlKKENVLLSSELQRQEKELHNsQKQSFELTSDLSILQ 729
Cdd:pfam17380 548 MEERRRiqEQMRKATEERS-RLEAMEREREMMRQIVESEK-ARAEYEATTPITTIK 601
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
528-784 |
9.09e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 528 ELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQA 607
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 608 AAEAVSERDTdfVSLQEELKKVR-AELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEatrlQGELEKLKKEWDVL 686
Cdd:pfam07888 110 SEELSEEKDA--LLAQRAAHEARiRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 687 ETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELE---KQVGSLKEQ---HLRDAADLKTLLSKA 760
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQERlnaSERKVEGLGEELSSM 263
|
250 260
....*....|....*....|....
gi 882939013 761 ENQAKDVQKEYEKTQTVLSELKLK 784
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQ 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-820 |
1.32e-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: 42.06 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 601 ILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcEDQQREEATRLQGELEKLK 680
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 681 KEWDVLETECHSLKKE-----------------NVLLSSE--------LQRQEKELHNSQKQSFELTSDLSILQMTRKEL 735
Cdd:COG4942 90 KEIAELRAELEAQKEElaellralyrlgrqpplALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 736 EKQVGSLKE---QHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 812
Cdd:COG4942 170 EAERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 882939013 813 GNNKPWPW 820
Cdd:COG4942 250 ALKGKLPW 257
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
448-815 |
1.34e-03 |
|
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: 42.40 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 448 ESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDlqgTQSETEAKQDiqHLRKELveaq 527
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDE---NLKELIEKKD--HLTKEL---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 528 ELARTSKQKCFELQALLEEE-----------RKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstRDKLLS 596
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDlqiatkticqlTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 597 AQDEILLLRQAAAEAVSERD--TDFVSLQE----ELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedqqreeat 670
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ--------------- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 671 RLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL-------- 742
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhq 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 743 ------KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 815
Cdd:pfam05483 520 ediincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
668-791 |
1.43e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 668 EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNsQKQSFELTSDLSilqmtrkELEKQVGSLKeqhl 747
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 882939013 748 rdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 791
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.45e-03 |
|
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: 38.60 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-386 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 242 ALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIkdl 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGD--- 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 318 sdklKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQE 386
Cdd:COG4913 762 ----AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
466-689 |
1.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 466 DTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEakqDIQHLRKELVEAQELARTSKQKCFELQALLe 545
Cdd:PRK04863 890 ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPE---QFEQLKQDYQQAQQTQRDAKQQAFALTEVV- 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 546 eERKAYRNqVEESAKQIQVLQVQLQKLHMDMENLQEEKDTeissTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQE- 624
Cdd:PRK04863 966 -QRRAHFS-YEDAAEMLAKNSDLNEKLRQRLEQAEQERTR----AREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEl 1039
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939013 625 --ELKK--VRAElEGWRKAASEYENEIRSLQSSFQLRCQQCEDQ---QREEATRLQGELEKLKKEWDVLETE 689
Cdd:PRK04863 1040 kqELQDlgVPAD-SGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.68e-03 |
|
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.
Pssm-ID: 438733 [Multi-domain] Cd Length: 129 Bit Score: 39.34 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882939013 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
451-773 |
1.72e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 451 LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQdLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRKELVEAQELA 530
Cdd:TIGR00606 760 IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 531 RTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHM--DMENLQEEKDTEISSTRDKLLSAQDEILLLRQAA 608
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 609 AEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLET 688
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 689 ECHSLKKenvllSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG-----SLKEQHLRDAADLKtLLSKAENQ 763
Cdd:TIGR00606 999 DMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGqmqvlQMKQEHQKLEENID-LIKRNHVL 1072
|
330
....*....|
gi 882939013 764 AKDVQKEYEK 773
Cdd:TIGR00606 1073 ALGRQKGYEK 1082
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-634 |
1.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTaKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE 291
Cdd:COG4717 92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 292 MNERTQEELRELANKYNGAV-NEIKDLSDKLKVAegkqeeiqqkgQAEKKELQTKIDEMEEKEQELQAKIEALQADndft 370
Cdd:COG4717 171 ELAELQEELEELLEQLSLATeEELQDLAEELEEL-----------QQRLAELEEELEEAQEELEELEEELEQLENE---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 371 nERLTALQVRLEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGdctFIHQFLECQKKLMVQGHLTKVVEESK 450
Cdd:COG4717 236 -LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 451 LSKENQAKAKESDLSDtLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHL----RKELVEA 526
Cdd:COG4717 312 ALEELEEEELEELLAA-LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 527 QELARTSKQkcfelqalLEEERKAYRNQVEESAKQIQVLQVQLQKlhMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQ 606
Cdd:COG4717 391 LEQAEEYQE--------LKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420
....*....|....*....|....*...
gi 882939013 607 AAAEAvsERDTDFVSLQEELKKVRAELE 634
Cdd:COG4717 461 ELEQL--EEDGELAELLQELEELKAELR 486
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
2.15e-03 |
|
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: 41.29 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 882939013 76 NGTFIN--SQRLSRGSEEsppcEILSGDIIQFG 106
Cdd:COG3456 69 NGTFLNgsDHPLGPGRPV----RLRDGDRLRIG 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
539-770 |
2.15e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 539 ELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEkdteISSTRDKLLSAQDEILLLRQAAAEavserdtd 618
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 619 fvsLQEELKKVRAELEGWRKaasEYENEIRSLQSS-------FQLRCQQCEDQQREeATRLQGELEKLKKEWDVLETECH 691
Cdd:COG4942 88 ---LEKEIAELRAELEAQKE---ELAELLRALYRLgrqpplaLLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 692 SLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ---HLRDAADLKTLLSKAENQAKDVQ 768
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAA 240
|
..
gi 882939013 769 KE 770
Cdd:COG4942 241 ER 242
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-812 |
2.18e-03 |
|
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: 41.88 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 327 KQEEIQQKGQ---AEKKELQTKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQVRLEHLQEKTLKECSSL 395
Cdd:pfam02463 251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 396 giqvddflpkingSTEKEHLLSKSGGDCTFIHQFLECQKKlmvqghltkvvEESKLSKENQAKAKESDLSDTLSPSKEKS 475
Cdd:pfam02463 331 -------------KKEKEEIEELEKELKELEIKREAEEEE-----------EEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 476 SDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQhlrKELVEAQELARTSKQKCFELQALLEEERKAYRNQV 555
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 556 EESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEG 635
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 636 WRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDvletecHSLKKENVLLSSELQRQEKELHNSQ 715
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK------SIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 716 KQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSI 795
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570
....*....|....*..
gi 882939013 796 TDELKQCKDNLKLLREK 812
Cdd:pfam02463 698 QLEIKKKEQREKEELKK 714
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
339-794 |
2.24e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 339 KKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRLEHLQEKtlkecsslgiqvddflpkingSTEKEhllsk 418
Cdd:pfam05557 15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKR---------------------EAEAE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 419 sggdctfihqflECQKKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSL 498
Cdd:pfam05557 69 ------------EALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 499 LKDDLQgtqsETEAK-QDIQHLRKELVEAQELARTSKQKCFELQalleeerkaYRNQVEESAKQIQVLQVQLQKLHMDME 577
Cdd:pfam05557 137 LQERLD----LLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKELE---------FEIQSQEQDSEIVKNSKSELARIPELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 578 NLQEEKDTEISstrdKLLSAQDEILLLR------QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRS-- 649
Cdd:pfam05557 204 KELERLREHNK----HLNENIENKLLLKeevedlKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 650 LQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDL---- 725
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyr 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 726 SILQMTRKEL-EKQVGSLKEQHLRDAADlktLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 794
Cdd:pfam05557 360 AILESYDKELtMSNYSPQLLERIEEAED---MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
300-387 |
2.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQV 379
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
....*...
gi 882939013 380 RLEHLQEK 387
Cdd:COG3883 204 ELAAAEAA 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
147-782 |
2.44e-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: 41.96 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 147 PSPVDKVAANTPSMYSQELFQLSQYLQEALHreqmleqklATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQa 226
Cdd:TIGR01612 644 PYQVPEHLKNKDKIYSTIKSELSKIYEDDID---------ALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 227 cskNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEVVRKLSE----VERSLSNTEDECTHLKEMNERTQEELRE 302
Cdd:TIGR01612 714 ---NMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEdfknKEKELSNKINDYAKEKDELNKYKSKISE 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 303 LANKYNGAVNeikdlSDKLKVAEGKQEEIQQKG-----QAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:TIGR01612 791 IKNHYNDQIN-----IDNIKDEDAKQNYDKSKEyiktiSIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 378 QVRLEHLQEKTLKECSSlgIQVDDFLPKINGStekEHLLSKSGGDCTFIHQFLECQKKlmVQGHLtKVVEESKLSKEN-- 455
Cdd:TIGR01612 866 HEQFAELTNKIKAEISD--DKLNDYEKKFNDS---KSLINEINKSIEEEYQNINTLKK--VDEYI-KICENTKESIEKfh 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 456 --QAKAKESdLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKDDLQGTQSETEAKQDIQHLRkelvEAQELARTS 533
Cdd:TIGR01612 938 nkQNILKEI-LNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFN----DLKANLGKN 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 534 KQKCFELQalLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTrdkllsaqdeILLLRQAAAEAVS 613
Cdd:TIGR01612 1013 KENMLYHQ--FDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKN----------IELLNKEILEEAE 1080
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 614 ERDTDFVSLQEELKKVRAELEGwRKAASEYENEIRSLQSSFQLRCQQCEDQQReeatrlqgELEKLKKewdvletechsl 693
Cdd:TIGR01612 1081 INITNFNEIKEKLKHYNFDDFG-KEENIKYADEINKIKDDIKNLDQKIDHHIK--------ALEEIKK------------ 1139
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 694 KKENVLlsSELQRQEKELhnsqkqsfELTSDLSILQMTRKELEKqvgslKEQHLRDAADLKTLLSKAENQAKDVQKEYEK 773
Cdd:TIGR01612 1140 KSENYI--DEIKAQINDL--------EDVADKAISNDDPEEIEK-----KIENIVTKIDKKKNIYDEIKKLLNEIAEIEK 1204
|
....*....
gi 882939013 774 TQTVLSELK 782
Cdd:TIGR01612 1205 DKTSLEEVK 1213
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-365 |
2.59e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 882939013 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA 365
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ 121
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-381 |
2.70e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 882939013 341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQVRL 381
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
544-717 |
2.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 544 LEEERKAYRNQVEESAKQIQVLQVQLQKLhMDMENLQEEKDTEISSTRdKLLSAQDEILLLRQAAAEAvserdTDFVSLQ 623
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL-----AELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 624 EELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSE 703
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170
....*....|....
gi 882939013 704 LQRQEKELHNSQKQ 717
Cdd:COG4717 229 LEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
236-386 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 236 LRKELIALQEDKHSYETTAK--ESLRRVLQEKIEVVRKLSEVERSLSNTEDecthlkemnerTQEELRELANKYNgavnE 313
Cdd:COG4913 615 LEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVAS-----------AEREIAELEAELE----R 679
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939013 314 IKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQadndftnERLTALQVRLEHLQE 386
Cdd:COG4913 680 LDASSDDLAALEEQLEELE----AELEELEEELDELKGEIGRLEKELEQAE-------EELDELQDRLEAAED 741
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
593-770 |
3.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 593 KLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIrslqssfqlrcqqceDQQREEATRL 672
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 673 QGELEKLK--KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQmtrKELEKQVGSLKEQHLRDA 750
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|
gi 882939013 751 ADLKTLLSKAENQAKDVQKE 770
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-359 |
3.92e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100
....*....|....*....|....*
gi 882939013 335 GQAEkKELQTKIDEMEEKEQELQAK 359
Cdd:PRK00409 603 SVKA-HELIEARKRLNKANEKKEKK 626
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
4.17e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.59 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQTKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 882939013 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
4.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 882939013 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-804 |
4.89e-03 |
|
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: 40.48 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 229 KNQTEDSLRKELIALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEAlQADNDFTNERLTALQV 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK-EINDKEKQVSLLLIQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 380 R--------LEHLQEKTLKECSSLGIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKL 451
Cdd:pfam05483 250 TekenkmkdLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 452 SKENQAKAKESDLSDTLSPSKEKSSDDTTDA-----QMDEQDLNEPLAKVSLLKDDLQGTQSETE--------AKQDIQH 518
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSleellRTEQQRLEKNEDQLKIITMELQKKSSELEemtkfknnKEVELEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 519 LRKELVEAQELARTSKQ----------KCFELQALLEEERKAYRN---QVEESAKQIQVLQVQLQKLHMDMENlQEEKDT 585
Cdd:pfam05483 410 LKKILAEDEKLLDEKKQfekiaeelkgKEQELIFLLQAREKEIHDleiQLTAIKTSEEHYLKEVEDLKTELEK-EKLKNI 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 586 EISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCE--- 662
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckl 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 663 DQQREEATRLQGELEKLKKEWDVLETECHSLKKEnvllsselqrqekeLHNSQKQSFELTSDLSILQMTRKELEKQVGSL 742
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--------------IENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939013 743 KEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQtvLSELKLkFEMTEQEKQSITDELKQCKD 804
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKK--ISEEKL-LEEVEKAKAIADEAVKLQKE 693
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-795 |
5.10e-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: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 327 KQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQA------------DNDFTNERLTALQVRLEHLQEKTLKECSS 394
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAqeavleetqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 395 LGIQVDDfLPKINGSTEKEHLLSKSGGDCTFIHQFLECQKKLMVQGHLTKVVEESKLSKE--------NQAKAKESDLSD 466
Cdd:TIGR00618 316 LQSKMRS-RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtltqhihTLQQQKTTLTQK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 467 TLSPSKEKSSDDTTDAQMDEQDLNEplakvsllkDDLQGTQSETEAKQDIQHLRKELVE--AQELARTSKQKcfelQALL 544
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYAELCAaaITCTAQCEKLE----KIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 545 EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVS-LQ 623
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAqLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 624 EELKKVRAELEGWRKAASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSE 703
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 704 LQRQEKELHNSQ-KQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 782
Cdd:TIGR00618 621 LQPEQDLQDVRLhLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
490
....*....|...
gi 882939013 783 LKFEMTEQEKQSI 795
Cdd:TIGR00618 701 QCQTLLRELETHI 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-798 |
5.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 369 F---------TNERLTALQVRLEHLQEKtlkecsslgiqvddflpkingstekehllsksggdctfIHQFLECQKKLmvq 439
Cdd:COG4717 127 LlplyqeleaLEAELAELPERLEELEER--------------------------------------LEELRELEEEL--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 440 ghltkvveESKLSKENQAKAKESDLSDTLSPSKEKssddttDAQMDEQDLNEPLAKVSLLKDDLQGTQSETE-AKQDIQH 518
Cdd:COG4717 166 --------EELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEeLEEELEQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 519 LRKELVEAQELARTSKQKCFELQALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQ 598
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 599 DEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRslqssfQLRCQQCEDQQREEATRLQGELEK 678
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE------ELQLEELEQEIAALLAEAGVEDEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 679 LKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSF--ELTSDLSILQMTRKELEKQVgslkEQHLRDAADLKTL 756
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEEL----EELREELAELEAE 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 882939013 757 LSKAENQAKdvqkeyektqtvLSELKLKFEMTEQEKQSITDE 798
Cdd:COG4717 462 LEQLEEDGE------------LAELLQELEELKAELRELAEE 491
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
5.68e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.73 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHSYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 882939013 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
666-792 |
5.78e-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: 39.62 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 666 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 741
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 882939013 742 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 792
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
234-387 |
6.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 234 DSLRKELIALQEdkhsyETTAKESLRRVLQEKIEVVR-KLSEVERSLSNTEDECTHLKEMNERTQEELRELAN--KYNGA 310
Cdd:COG1579 20 DRLEHRLKELPA-----ELAELEDELAALEARLEAAKtELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 882939013 311 VNEIKDLSDKLKVAEGKQEEIQqkgqAEKKELQTKIDEMEEKEQELQAKIEALQADNDftnERLTALQVRLEHLQEK 387
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELM----ERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAE 164
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-387 |
6.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 172 LQEALHREQMLEQKLATLQRLLAITQEAsdtswqalIDEDRL-LSRLEVMGNQLQACSKNQTEDSLRKELIAlqeDKHSY 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRET--------IEEKRErAEELRERAAELEAEAEEKREAAAEAEEEA---EEARE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECthlkemnERTQEELRELANKYNGAVNEIKDLSDKLKVAEGK-QE 329
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDEI-------ERLREKREALAELNDERRERLAEKRERKRELEAEfDE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882939013 330 EIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTN---ERLTALQVRLEHLQEK 387
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENR 706
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
609-771 |
9.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 609 AEAVSERDTDfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedQQREEATRLQGELEKLKKEWDVLET 688
Cdd:COG2433 379 EEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE--------RLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939013 689 ECHSLKKE---NVLLSSELQRQEKELHNsqkqsfeLTSDLSILQMTRKELEKQVGSLKE----QHLRDAADLKTLLSKAE 761
Cdd:COG2433 449 ELSEARSEerrEIRKDREISRLDREIER-------LERELEEERERIEELKRKLERLKElwklEHSGELVPVKVVEKFTK 521
|
170
....*....|
gi 882939013 762 NQAKDVQKEY 771
Cdd:COG2433 522 EAIRRLEEEY 531
|
|
| |
