|
Name |
Accession |
Description |
Interval |
E-value |
| FHA_SLMAP |
cd22679 |
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ... |
3-130 |
5.92e-81 |
|
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: 5.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 3 SALAIFTCRPNSHPFQERHVYLDEPIKIGRSVARCRPAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINS 82
Cdd:cd22679 1 SALAILTPRPNSHPFQERHIVLDEPVKIGRSVARARPAANNAIFDCKVLSRNHALLWYDD--GKFYLQDTKSSNGTFVNN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907106177 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 |
7.18e-27 |
|
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: 103.53 E-value: 7.18e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106177 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQ 225
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| FHA_DMA-like |
cd22692 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ... |
27-108 |
1.19e-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: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 27 PIKIGRSVARCRPAQNNAT-FDCKVLSRNHALVWfdHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQF 105
Cdd:cd22692 38 QIHIGRYTERVRQAIYHPVvFKSKVVSRTHGCIK--VDEGNWYIKDVKSSSGTFLNHQRLSPASRTSKPYPLRDGDILQL 115
|
...
gi 1907106177 106 GVD 108
Cdd:cd22692 116 GMD 118
|
|
| FHA_VPS64-like |
cd22695 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ... |
6-126 |
4.56e-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: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 6 AIFTCRPNSHPFQERHV---YLDEPIKIGRSVARCRPAQN---------------NATFDCKVLSRNHALVWFDHKTSKF 67
Cdd:cd22695 2 HILVLKSLNATFETKFLvvpFKPDGLKLGRPVTNSVNKNNsgskrdlfsqqvrpdNGNFDSRVLSRNHACLSCDPTTGKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 68 YLQDTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFGVDVTEntrKVTHGCIVSTIK 126
Cdd:cd22695 82 YIRDLKSSNGTFVNGQKIRQND-----VELKVGDEVDLGTDIDS---KIEHRKISAYVE 132
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
13-106 |
2.11e-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: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 13 NSHPFQERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKtsKFYLQDTKSSNGTFINSQRLsrgseeS 92
Cdd:cd00060 6 DGDGGGREFPLTKGVVTIGRS------PDCDIVLDDPSVSRRHARIEVDGG--GVYLEDLGSTNGTFVNGKRI------T 71
|
90
....*....|....
gi 1907106177 93 PPCEILSGDIIQFG 106
Cdd:cd00060 72 PPVPLQDGDVIRLG 85
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
28-105 |
5.85e-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: 5.85e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106177 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 |
6.26e-13 |
|
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: 63.27 E-value: 6.26e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1907106177 167 QLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-733 |
1.39e-11 |
|
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: 68.16 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 156 NTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQA--CSKNQTE 233
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 234 DSLRKELIALQEDKHSYE------TTAKESLRRVLQE--KIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELAN 305
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEdrrerlQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 306 KYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKidemEEKEQELQAKIEALQADNDFTNERLTALQG----IQ 381
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGrlqaVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 382 VDD--------------------FLP-------KINGSTEKEKLMVQGHLTKVVEESKLSKE------------------ 416
Cdd:TIGR02168 552 VENlnaakkaiaflkqnelgrvtFLPldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddl 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 417 ----NQAKAKESDLS------DTLSP--------SKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL---EEERKAYR 473
Cdd:TIGR02168 632 dnalELAKKLRPGYRivtldgDLVRPggvitggsAKTNSSILERRREIEEleEKIEELEEKIAELEKALaelRKELEELE 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 474 NQVEESAKQIQVLQVQLQKLHMDMENLQEEKDT---EISSTRDKLLSAQDEILLLRQA---AAEAVSERDTDFVSLQEEL 547
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEELEAQI 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 548 KKVRAELEGWRKAASEYENEIRSLQSSF---QLRCQQCEDQQREEATRL----------QGELEKLKKEWDVLETECHSL 614
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLedleeqieelSEDIESLAAEIEELEELIEEL 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 615 KKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHlrdaADLKTLLSKAENQAKDVQkeyek 694
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQ----- 942
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907106177 695 tQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:TIGR02168 943 -ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
244-725 |
2.07e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 244 QEDKHSYETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK 322
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEkKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 323 VAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMVQG 402
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 403 -------HLTKVVEESKLSKENQAKAKESDLSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR 473
Cdd:PTZ00121 1441 eeakkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 474 -------NQVEESAKQIQVLQVQLQKLHMDMENLQE-EKDTEISSTRDKLLSAQDEILLLRQA--AAEAVSERDTDFVSL 543
Cdd:PTZ00121 1521 akkadeaKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 544 QEELKKVRAE----LEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENV 619
Cdd:PTZ00121 1601 YEEEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 620 LLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE---KTQ 696
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkKIA 1760
|
490 500
....*....|....*....|....*....
gi 1907106177 697 TVLSELKLKFEMTEQEKQSITDELKQCKD 725
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-733 |
2.12e-11 |
|
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: 67.77 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 190 QRLLAITQEASDTSWQALIDE--------DRLLSRLEVMGNQLQACSKNQTE-----DSLRKELIALQEDKHSYETT--- 253
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 254 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 334 KGQAEKKELQT---KIDEMEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDFLPKIngsTEKEKLMVQGHLTKVVEE 410
Cdd:TIGR02168 373 RLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ-EIEELLKKL---EEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 411 sklskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYR---NQVEESAKQIQVLQ 487
Cdd:TIGR02168 449 -----LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 488 VQLQKLHMDmENLQEEKDTEISSTRDKLL-----SAQDEILLLRQAAA------EAVSERDTDFVSLQEELKKVRAELEG 556
Cdd:TIGR02168 524 VLSELISVD-EGYEAAIEAALGGRLQAVVvenlnAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 557 WRKAASEYENEIRSLQSSFQLRCQQCEDQQreEATRLQG--------------------------------------ELE 598
Cdd:TIGR02168 603 VAKDLVKFDPKLRKALSYLLGGVLVVDDLD--NALELAKklrpgyrivtldgdlvrpggvitggsaktnssilerrrEIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 599 KLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVgslkEQHLRDAADLKTLL 678
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV----EQLEERIAQLSKEL 756
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907106177 679 SKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
|
| FHA_AGGF1 |
cd22686 |
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ... |
52-106 |
2.21e-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: 2.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907106177 52 SRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPCEILSGDIIQFG 106
Cdd:cd22686 48 SKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSDPYPLTHGDELKIG 102
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
14-106 |
6.87e-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: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 14 SHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHktSKFYLQDTKSSNGTFINSQRLSRgsees 92
Cdd:COG1716 8 EGPLAGRRFPLDGgPLTIGRA------PDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTE----- 74
|
90
....*....|....
gi 1907106177 93 pPCEILSGDIIQFG 106
Cdd:COG1716 75 -PAPLRDGDVIRLG 87
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-732 |
1.50e-10 |
|
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: 65.07 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 212 RLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYETTAKESLRRVLQEKIEvvrkLSEVERSlSNTEDECTHLKE 291
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE----LDGFERG-PFSERQIKNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 292 MNERTQEELRELANKyngavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQ---ADND 368
Cdd:TIGR00606 398 LVIERQEDEAKTAAQ------LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQqleGSSD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 369 FTNERLTALQGIQVDDFLPKINGSTE----KEKLMVQGHLTKVVEESKLSKENQAKAKESD-LSDTLSPSKEKSSDDTTD 443
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSLTEtlkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTtRTQMEMLTKDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 444 AQMDEQDLNEPLAKVSLL--KALLEEERKAYRNQVEESAKQIQVLQVQLQKLhmdmENLQEEKDTEISSTRDKLLSAQDE 521
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 522 ILLLRQAAAEavserDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQC------EDQQREEATRLQG 595
Cdd:TIGR00606 628 LFDVCGSQDE-----ESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrvfqtEAELQEFISDLQS 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 596 ELEKLKKEWDVLETECHSLKKENVLL-------SSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL--KEQ 666
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpEEE 782
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106177 667 HLRDAADLKTLLSKAENQAKDVQKEYEKTQTVL--SELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 732
Cdd:TIGR00606 783 SAKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
298-733 |
5.50e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 298 EELRELANKYNGAVNEIkdLSDKLKVAEGKQEEIQQKgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTAL 377
Cdd:PRK02224 165 EEYRERASDARLGVERV--LSDQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 378 QGIQvddflpkingSTEKEKLMVQGHLTKVVEESKLSKENQAKAKEsDLSDTLSPSKEKSSD--DTTDAQMDEQDLNEPL 455
Cdd:PRK02224 240 DEVL----------EEHEERREELETLEAEIEDLRETIAETERERE-ELAEEVRDLRERLEEleEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 456 AK-VSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEK----------DTEISSTRDKLLSAQDEILL 524
Cdd:PRK02224 309 AEaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelreeaaelESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 525 LR---QAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSF----QLR----CQQCE---------- 583
Cdd:PRK02224 389 LEeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaeALLeagkCPECGqpvegsphve 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 584 --DQQREEATRLQGELEKLKKEWDVLETECHSLKkenvllssELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG 661
Cdd:PRK02224 469 tiEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106177 662 SLKEQhlrdAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQS------ITDELKQCKDNLKLLREK 733
Cdd:PRK02224 541 ELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREK 614
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-703 |
7.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 161 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKEL 240
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 241 IALQEDKHSYETT---AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG1196 298 ARLEQDIARLEERrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 318 SDKLKVAEGKQEEIQQkgqaEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEK 397
Cdd:COG1196 378 EEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 398 LMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVE 477
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 478 ESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKL-------LSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKV 550
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 551 RAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEK 630
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106177 631 ELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELK 703
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-707 |
3.23e-09 |
|
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: 60.57 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 271 KLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAvneIKDLSDKLKvaegKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM---ISDLEERLK----KEEKGRQELEKAKRKLEGESTDLQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 351 EKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLmvQGHLTKVVE--ESKLSKENQAKAKESDLSD 428
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL--EAQISELQEdlESERAARNKAEKQRRDLGE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 429 TLSPSKEKSSD--DTTDAQMDEQDLNEplAKVSLLKALLEEERKAYRNQVEESAKqiqvlqvqlqKLHMDMENLQEEkdt 506
Cdd:pfam01576 300 ELEALKTELEDtlDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQLQEMRQ----------KHTQALEELTEQ--- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 507 eisstrdkllsaqdeillLRQAAAEAVSERDTDfVSLQEELKKVRAELEGWRKAASEYENEIRSLQSS---FQLRCQQCE 583
Cdd:pfam01576 365 ------------------LEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQlqeLQARLSESE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 584 DQQREEA---TRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLsilqmtrKELEKQV 660
Cdd:pfam01576 426 RQRAELAeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRL-------RQLEDER 498
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907106177 661 GSLKEQhlrdaadlktlLSKAENQAKDVQKEYEKTQTVLSELKLKFE 707
Cdd:pfam01576 499 NSLQEQ-----------LEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
235-725 |
3.32e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 235 SLRKELIALQEDKHSYETTAKE--SLRRVLQEKIEVVRKLSEVERSLsntEDECTHLKEMNERTQEELRELANKYNGAVN 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKikNKLLKLELLLSNLKKKIQKNKSL---ESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQT---KIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQGIQVDdflp 387
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKK---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 388 kingstekeklmvqghltKVVEESKLSKENQakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKalleE 467
Cdd:TIGR04523 323 ------------------LEEIQNQISQNNK---IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK----K 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 468 ERKAYRNQVEESAKQIQVLQVQLQKlhmdMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSE------RDTDFV 541
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQN----QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEikdltnQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 542 SLQEELKKVRAELEgwrKAASEYENEIRSLQSSFQLRCQQCEDQQRE------EATRLQGELEKLKKEWDVL-------- 607
Cdd:TIGR04523 454 LIIKNLDNTRESLE---TQLKVLSRSINKIKQNLEQKQKELKSKEKElkklneEKKELEEKVKDLTKKISSLkekiekle 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 608 ------ETECHSLKKENVLLSSELQRQ--EKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHL---RDAADLKT 676
Cdd:TIGR04523 531 sekkekESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdliKEIEEKEK 610
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1907106177 677 LLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKD 725
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
164-204 |
6.68e-09 |
|
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: 51.96 E-value: 6.68e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907106177 164 ELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSW 204
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-733 |
6.97e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 228 SKNQTEDSLRKELIALQEDKHSYETTA------KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNERTQEELR 301
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKeeieelEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 302 ELANKYNgavnEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKE---QELQAKIEALQADNDFTNERLTALQ 378
Cdd:PRK03918 290 EKAEEYI----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 379 GIQVddFLPKINGSTEKEKLMVQGHLTKVVEESKLSKENQAKaKESDLSDTLSPSKEKSSDDTTDAQmdeqDLNEPLAKV 458
Cdd:PRK03918 366 EAKA--KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELKKAIE----ELKKAKGKC 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 459 SLLKALLEEERKA-----YRNQVEESAKQIQVLQVQLQKLHMDMENLqeekdteisstrDKLLSAQDEILLLRQAAAEAV 533
Cdd:PRK03918 439 PVCGRELTEEHRKelleeYTAELKRIEKELKEIEEKERKLRKELREL------------EKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 534 SERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFqlrcqqcedqqrEEATRLQGELEKLKKEWDVLETECHS 613
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL------------EKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 614 LKKENVLLS----SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQhLRDAADLKTLLSKAENQAKDVQ 689
Cdd:PRK03918 575 LLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-FEELAETEKRLEELRKELEELE 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106177 690 K------------EYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:PRK03918 654 KkyseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
462-733 |
8.60e-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: 59.31 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 462 KALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEIL-LLRQAAAEAVSERDTDF 540
Cdd:TIGR02169 214 QALLKEKREY---EGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELEKRLEEIEqLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 541 VSLQEELKKVRAELEGWRKAASEYENEIRSLQSsfQLRCQQCE-DQQREEATRLQGELEKLKKEWDVLETECHSLKKENV 619
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEE--RLAKLEAEiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 620 LLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLR----------DAADLKTLLSKAENQAKDVQ 689
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRlseeladlnaAIAGIEAKINELEEEKEDKA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907106177 690 KEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| FHA_MEK1-like |
cd22670 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ... |
14-110 |
1.61e-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: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 14 SHPFQERHV---YLDEPIKIGRSvARCRPAQNNATfdckvLSRNHALVW---FDHKT-SKFYLQDTkSSNGTFINSQRLS 86
Cdd:cd22670 7 SSPGSTDIVlpiYKNQVITIGRS-PSCDIVINDPF-----VSRTHCRIYsvqFDESSaPLVYVEDL-SSNGTYLNGKLIG 79
|
90 100
....*....|....*....|....*
gi 1907106177 87 RGseespPCEILS-GDIIQFGVDVT 110
Cdd:cd22670 80 RN-----NTVLLSdGDVIEIAHSAT 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-600 |
2.63e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 296 TQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQ---KGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNE 372
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 373 RLTALQGIqvddflpkingstekeklmvqghltKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTT-------DAQ 445
Cdd:TIGR02168 755 ELTELEAE-------------------------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 446 MDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLL 525
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 526 RQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEY-------ENEIRSLQSSF--------------QLRCQQCED 584
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLelrleglEVRIDNLQERLseeysltleeaealENKIEDDEE 968
|
330
....*....|....*.
gi 1907106177 585 QQREEATRLQGELEKL 600
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| FHA |
smart00240 |
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ... |
28-85 |
4.61e-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: 4.61e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106177 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 |
5.55e-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: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 29 KIGRSVARCRPAQNNATFDcKVLSRNHALVWFDHKTS---KFYLQDTkSSNGTFINSQRLSRGSEEsppcEILSGDIIQF 105
Cdd:cd22685 31 RIGRNPEVCDVFLCSSQHP-NLISREHAEIHAERDGNgnwKVLIEDR-STNGTYVNDVRLQDGQRR----ELSDGDTITF 104
|
90
....*....|....*.
gi 1907106177 106 G--VDVTENTRKVTHG 119
Cdd:cd22685 105 GhkNGRRVKQWPYQKS 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-715 |
1.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 250 YETTAKES--LRRVLQEKIEVVRKL----SEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsDKLKV 323
Cdd:PRK03918 160 YENAYKNLgeVIKEIKRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 324 AEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndfTNERLTALQG-----IQVDDFLPKIN---GSTEK 395
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEkaeeyIKLSEFYEEYLdelREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 396 EKLMVQGHLTKVVE-----ESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDE-QDLNEPLAKVSL--LKALLE 466
Cdd:PRK03918 315 RLSRLEEEINGIEErikelEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEElERLKKRLTGLTPekLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 467 EERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQE-EKDTEISSTRDKLLSAQDEILLLRQAAAE------AVSERDTD 539
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGKCPVCGRELTEEHRKELLEEYTAElkriekELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 540 FVSLQEELKKVRAELEGWRKAASEYE--NEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHS---L 614
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKleeL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 615 KKENVLLSSELQRQEKELHNSQKQSFELT-SDLSILQMTRKELE---------KQVGSLKEQHLRDAADLKTLLSKAENQ 684
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelKDAEKELEREEKELKKLEEELDKAFEE 634
|
490 500 510
....*....|....*....|....*....|.
gi 1907106177 685 AKDVQKEYEKTQTVLSELKLKFEMTEQEKQS 715
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
409-728 |
1.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 409 EESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQM---DEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQV 485
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 486 LQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEIlllrqaaaeaVSERDTDFVSLQEELKKVRAELEGWRKAASEYE 565
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE----------VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 566 NEIRSLQSSFQLRCQQCEDQQREEAtRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSD 645
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 646 LSILQMTRKELEKQVGSLKEQHLRDAADLKTLLS----KAENQAKDVQ------------KEYEKTQTVLSELKLKFEMT 709
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvQAELQRVEEEiralepvnmlaiQEYEEVLKRLDELKEKRAKL 998
|
330
....*....|....*....
gi 1907106177 710 EQEKQSITDELKQCkDNLK 728
Cdd:TIGR02169 999 EEERKAILERIEEY-EKKK 1016
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-617 |
2.10e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 255 KESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 335 GQAEKKELQTKIDEMEEKEQ---ELQAKIEALQADNDftnerltalqgiqvDDFLPKINGSTEKEKLMVQGHLTKVVE-E 410
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEdlhKLEEALNDLEARLS--------------HSRIPEIQAELSKLEEEVSRIEARLREiE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 411 SKLSKENQAKAKESDLSDTLspskeksSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQL 490
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQEL-------QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 491 QKLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEE------LKKVRAELEgwrkaasEY 564
Cdd:TIGR02169 892 DELEAQLRELERKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQ-------RV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106177 565 ENEIRSLQSSFQLRCQQCEDQQREEaTRLQGELEKLKKEWDVLE---TECHSLKKE 617
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-733 |
2.83e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 267 EVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKI 346
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 347 DEMEEKEQE---LQAKIEALQADNDFTNERLTALQGIQVDdfLPKINGSTEKEKLMVQGHLTKVVEE--SKLSKENQAKA 421
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEK--LNNKYNDLKKQKEELENELNLLEKEklNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 422 KESDLSDTLSPSKEKSSDDTTDaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQ 501
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSL----ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 502 EeKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVS-LQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQ 580
Cdd:TIGR04523 271 E-KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 581 QCEDQQREEATrLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQV 660
Cdd:TIGR04523 350 ELTNSESENSE-KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 661 GSLKEQHLRDAA-----------------DLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQC 723
Cdd:TIGR04523 429 ERLKETIIKNNSeikdltnqdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
490
....*....|
gi 1907106177 724 KDNLKLLREK 733
Cdd:TIGR04523 509 EEKVKDLTKK 518
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
229-736 |
3.06e-07 |
|
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: 53.96 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 229 KNQTEDSLRKELIALQEDKHSYETTAK---------ESLRRVLQEKIEVVRKLSEVERSlsnTEDECTHLKEMNERTQEE 299
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenEKVSLKLEEEIQENKDLIKENNA---TRHLCNLLKETCARSAEK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 300 LRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNdftnERLTALQG 379
Cdd:pfam05483 171 TKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 380 IQvddflpkingSTEKEKLMVQghLTKVVEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQ----------MDEQ 449
Cdd:pfam05483 247 IQ----------ITEKENKMKD--LTFLLEESR-DKANQLEEKTKLQDENLKELIEKKDHLTKELEdikmslqrsmSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 450 DLNEPLAKVSLLKALLEEERKAyrnQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEisstRDKLLSAQDEILLLRQAA 529
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEELLRTE----QQRLEKNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 530 AEAVSERD--TDFVSLQE----ELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedqqreeatRLQGELEKLKKE 603
Cdd:pfam05483 387 QKKSSELEemTKFKNNKEveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQ---------------ELIFLLQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 604 WDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL--------------KEQHLR 669
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMtlelkkhqediincKKQEER 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 670 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 736
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-555 |
3.27e-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: 53.91 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 256 ESLRRVLQEKIEVVRK-LSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:TIGR02168 683 EEKIEELEEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 335 ---GQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGI---QVDDFLPKING--STEKEKLMVQGHLTK 406
Cdd:TIGR02168 763 ieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRERleSLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 407 VVEESKLSKENQAKAKESdlSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVL 486
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAE--IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 487 QVQLQKLHMDMENLQEEKDTEISStrdklLSAQDEILLlrQAAAEAVSERDTDFVSLQEELKKVRAELE 555
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQER-----LSEEYSLTL--EEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| FHA_FKH1-like |
cd22701 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ... |
27-106 |
7.42e-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: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 27 PIKIGRSVARcRPAQNNATFDC-----KVLSRNHALVWFDHKTSKFYLQdTKSSNGTFINSQRLSRGseeSPPCEILSGD 101
Cdd:cd22701 18 EVVLGRNSKN-SSSTAADSVDIdlgpsKKISRRHARIFYDFTTQCFELS-VLGRNGVKVDGILVKPG---SPPVPLRSGS 92
|
....*
gi 1907106177 102 IIQFG 106
Cdd:cd22701 93 LIQIG 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
152-609 |
8.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 152 KVAANTPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDtswqaliDEDRLLSRLEVMGNQLQACSKNQ 231
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 232 TEDSLRKELIALQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKE-MNERTQEELRELANKYNGA 310
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 311 VNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAdndftnerLTALQGIQVDDFLPKIN 390
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALL--------ALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 391 GSTekeKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERK 470
Cdd:COG4717 277 GVL---FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 471 AYRNQVEESAKQIQVLQVQLQKLHM-DMENLQE-----EKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFV--- 541
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEaGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeee 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 542 --SLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLrcqqceDQQREEATRLQGELEKLKKEWDVLET 609
Cdd:COG4717 434 leELEEELEELEEELEELREELAELEAELEQLEEDGEL------AELLQELEELKAELRELAEEWAALKL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-600 |
1.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 162 SQELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgNQLQAcsKNQTEDSLRKELI 241
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAE--AEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 242 ALQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 322 KVAEGKQEEIQQ-KGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEKEKLMV 400
Cdd:COG1196 470 EEAALLEAALAElLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 401 QGHLTKVVEESK---LSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKA------LLEEERKA 471
Cdd:COG1196 550 NIVVEDDEVAAAaieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 472 YRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTR-DKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKV 550
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELlAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 551 RAELEGWRKAASEYENEIRSLQSSFQLRCQQCE--------------------DQQREEATRLQGELEKL 600
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLeeeelleeealeelpeppdlEELERELERLEREIEAL 779
|
|
| FHA_EspA-like |
cd22698 |
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ... |
26-106 |
1.93e-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: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 26 EPIKIGRSVArcrpaqNNATFDCKVLSRNHALVwfDHKTSKFYLQDTKSSNGTFINSQRLSRGseesppcEILSGDIIQF 105
Cdd:cd22698 21 DEFTIGRSSN------NDIRLNDHSVSRHHARI--VRQGDKCNLTDLGSTNGTFLNGIRVGTH-------ELKHGDRIQL 85
|
.
gi 1907106177 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 |
1.95e-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: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 27 PIKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLsrgSEESPPCEILSGDIIQFG 106
Cdd:cd22678 24 PLTIGRIQ------RGDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESI---SPNGRPVVLSSGDVITLG 94
|
90
....*....|.
gi 1907106177 107 vdvTENTRKVT 117
Cdd:cd22678 95 ---SETKILVR 102
|
|
| FHA_RNF8 |
cd22663 |
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ... |
25-114 |
2.19e-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: 46.97 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 25 DEPIKIGRSVArcrpAQNNATFDC-KVLSRNHALVWFDHKTSKFyLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDII 103
Cdd:cd22663 20 GKEVTVGRGLG----VTYQLVSTCpLMISRNHCVLKKNDEGQWT-IKDNKSLNGVWVNGERI----EPLKPYPLNEGDLI 90
|
90
....*....|.
gi 1907106177 104 QFGVDVTENTR 114
Cdd:cd22663 91 QLGVPPENKEP 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
163-366 |
3.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQAcSKNQTEDSLRKELIA 242
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-ELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 243 LQedKHSYETTAKESLR-RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKL 321
Cdd:COG4942 113 LY--RLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907106177 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| FHA_Cep170 |
cd22704 |
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ... |
55-108 |
3.57e-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: 3.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907106177 55 HALVWFDHKTSKFYLQDTKSSNGTFINSQRLSrgseESPPCEILSGDIIQFGVD 108
Cdd:cd22704 39 HAVITYDQIDNEFKIKDLGSLNGTFVNDSRIP----EQTYITLKLGDSIRFGYD 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
247-728 |
3.71e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 247 KHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE--DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVA 324
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 325 E--------GKQEEIQQKGQAEKK-ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvddflPKINGSTEK 395
Cdd:PTZ00121 1287 EekkkadeaKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA-----EAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 396 EKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKE---KSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAY 472
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEedkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 473 RNQVEESAKQIQVLQVQLQKLHMDMEnlqEEKDTEISSTRDKLLSAQDEillLRQAAAEAvsERDTDFVSLQEELKKVRA 552
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAE---EAKKADEAKKKAEEAKKADE---AKKKAEEA--KKKADEAKKAAEAKKKAD 1513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 553 ELegwRKA--ASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEK 630
Cdd:PTZ00121 1514 EA---KKAeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 631 ELHNSQKQSFELTSDLSILQMTRKELEKQVGSLK----EQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKf 706
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK- 1669
|
490 500
....*....|....*....|..
gi 1907106177 707 emtEQEKQSITDELKQCKDNLK 728
Cdd:PTZ00121 1670 ---AEEDKKKAEEAKKAEEDEK 1688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-733 |
4.12e-06 |
|
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: 50.45 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 197 QEASDTSWQALIDEDRLLSRLEVMGNQLQacsknqtedSLRKELIALQEDKHSYETTAKESLRRVLQEKI---EVVRKLS 273
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIE---------EERKRRDKLTEEYAELKEELEDLRAELEEVDKefaETRDELK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLK----VAEGKQEEIQQ-------------KGQ 336
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleeEKEDKALEIKKqewkleqlaadlsKYE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 337 AEKKELQTKIDEMEEKEQELQAKIEAL--QADNDFTNERLTALQGIQVDDFLPKINGST-------EKEKLMVQ----GH 403
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAeaQARASEERVRGGRAVEEVLKASIQGVHGTVaqlgsvgERYATAIEvaagNR 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 404 LTK-VVEESKLSKENQAKAKESDLS-----------DTLSPSKEKSSDDTTDAQMDEQDLNEPLAK-------------- 457
Cdd:TIGR02169 549 LNNvVVEDDAVAKEAIELLKRRKAGratflplnkmrDERRDLSILSEDGVIGFAVDLVEFDPKYEPafkyvfgdtlvved 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 458 -------------VSLLKALLE----------EERKAYRNQVEESAKqiqvlqvqLQKLHMDMENLQEEKDTeISSTRDK 514
Cdd:TIGR02169 629 ieaarrlmgkyrmVTLEGELFEksgamtggsrAPRGGILFSRSEPAE--------LQRLRERLEGLKRELSS-LQSELRR 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 515 LLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlRCQQCEDQQREEATRLQ 594
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLE 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 595 GELEKLKKE-----WDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSL-KEQHL 668
Cdd:TIGR02169 779 EALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIeKEIEN 858
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 669 RDA--ADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:TIGR02169 859 LNGkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
543-727 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 543 LQEELKKVRAELegwrkaaseYENEIRSLQSSfqlrcqqcEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLS 622
Cdd:COG1196 218 LKEELKELEAEL---------LLLKLRELEAE--------LEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 623 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTL---LSKAENQAKDVQKEYEKTQTVL 699
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAEL 360
|
170 180
....*....|....*....|....*...
gi 1907106177 700 SELKLKFEMTEQEKQSITDELKQCKDNL 727
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-711 |
1.48e-05 |
|
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: 48.66 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 162 SQELFQLSQYLQEALHR----EQMLEQKLATLQRLLAITQEASDTSWQALIDEDRllsRLEVMGNQLQACSKNQTEDSLR 237
Cdd:pfam10174 129 AKELFLLRKTLEEMELRietqKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWER---TRRIAEAEMQLGHLEVLLDQKE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 238 KELIALQEDKHS-YETTAKESLRRVLQEKIEVV-RKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKyngaVNEIK 315
Cdd:pfam10174 206 KENIHLREELHRrNQLQPDPAKTKALQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQ----MEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 316 DLSD--KLKVAEGKQEeiQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINgst 393
Cdd:pfam10174 282 SHSKfmKNKIDQLKQE--LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ-TEVDALRLRLE--- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 394 EKEKLMV--QGHLTKVVEES----------------KLSKENQAKAKESDLSDTLSpSKEKSSDDTTDA--QMDEQDLNE 453
Cdd:pfam10174 356 EKESFLNkkTKQLQDLTEEKstlageirdlkdmldvKERKINVLQKKIENLQEQLR-DKDKQLAGLKERvkSLQTDSSNT 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 454 PLAKVSLLKALLEEERKAYRNQvEESAKQIQVLQVQLQKLHMDMENLQEEKDteiSSTRDKLLSAQDEILLLRQAAAEAV 533
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLK-EQREREDRERLEELESLKKENKDLKEKVS---ALQPELTEKESSLIDLKEHASSLAS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 534 S--ERDTDFVSLQEELKKVRAE---LEGWRKAASEYENEIRSlQSSFQLRCQQCEDQ---QREEATRLQGELEKLKKEWD 605
Cdd:pfam10174 511 SglKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAVRT-NPEINDRIRLLEQEvarYKEESGKAQAEVERLLGILR 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 606 VLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEKQVGSLKEQHLRDAADLKTllSKAENQA 685
Cdd:pfam10174 590 EVENEKNDKDKKIAELESLTLRQMKEQNKKVAN----------IKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQL 657
|
570 580
....*....|....*....|....*.
gi 1907106177 686 KDVQKEYEKTQTVLSELKLKFEMTEQ 711
Cdd:pfam10174 658 EELMGALEKTRQELDATKARLSSTQQ 683
|
|
| FHA_PPP1R8 |
cd22674 |
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ... |
52-106 |
2.02e-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: 2.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 52 SRNH-ALVWfdHK-TSKFYLQDTKSSNGTFINSQRLsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22674 48 SRVHaALVY--HKhLNRVFLIDLGSTHGTFVGGIRL----EPHKPQQLPIDSTLRFG 98
|
|
| FHA_Kanadaptin |
cd22677 |
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ... |
51-106 |
2.32e-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: 2.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106177 51 LSRNHALVWF----DHKTSKFYLQDTKSSNGTFINSQRLsrgseesPP---CEILSGDIIQFG 106
Cdd:cd22677 41 ISRYHAVLQYrgdaDDHDGGFYLYDLGSTHGTFLNKQRI-------PPkqyYRLRVGHVLKFG 96
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-736 |
2.93e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 239 ELIALQEDKHSYETTAK--ESLRRVLQEKIE-----VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAV 311
Cdd:pfam15921 279 EITGLTEKASSARSQANsiQSQLEIIQEQARnqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAK-------IEALQADNDFTNERLTALQGIqVDD 384
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEAL-LKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 385 FLPKINGSTEKEKLMVQGhltkvveesklskENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKAL 464
Cdd:pfam15921 438 MKSECQGQMERQMAAIQG-------------KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 465 LEEERKAYRNQVEESAKQIQVLQVQLQKLhmdmENLQEEKD------TEISSTRDKLLSAQDEILLLRQAA--------- 529
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDhlrnvqTECEALKLQMAEKDKVIEILRQQIenmtqlvgq 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 530 -AEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQ-LRCQQCE----DQQREEATR-LQGELEKLKK 602
Cdd:pfam15921 581 hGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdLELEKVKlvnaGSERLRAVKdIKQERDQLLN 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 603 EWDVLETECHSLKKENVLLSSELQRQEKELH-NSQKQSFELTSDLSILQMTRKELEKQVGS----------LKEQHLRDA 671
Cdd:pfam15921 661 EVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvamgMQKQITAKR 740
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907106177 672 ADLKTLLSKA---ENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 736
Cdd:pfam15921 741 GQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| FHA_RAD53-like_rpt2 |
cd22690 |
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ... |
12-103 |
2.96e-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: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 12 PNSHPfqerHVYL-DEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSKF---YLQDTkSSNGTFINSQRLSR 87
Cdd:cd22690 8 NPSYP----DIELtQNTTFIGRS------KDCDEEITDPRISKHHCIITRKRSGKGLddvYVTDT-STNGTFINNNRLGK 76
|
90
....*....|....*.
gi 1907106177 88 GSEesppCEILSGDII 103
Cdd:cd22690 77 GSQ----SLLQDGDEI 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-572 |
3.16e-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: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 328 QEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpKINGSTEKEKLMVQGHLTKV 407
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 408 VEESKlSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKayrnQVEEsakqiqvlq 487
Cdd:COG4942 89 EKEIA-ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE----QAEE--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 488 vqlqkLHMDMENLQEEKDtEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENE 567
Cdd:COG4942 155 -----LRADLAELAALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*
gi 1907106177 568 IRSLQ 572
Cdd:COG4942 229 IARLE 233
|
|
| FHA_ArnA-like |
cd22680 |
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ... |
28-106 |
3.66e-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: 43.10 E-value: 3.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 28 IKIGRSVarcrpaQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRlsrgsEESPPCEILSGDIIQFG 106
Cdd:cd22680 23 VSIGRDP------ENVIVIPDPFVSRNHARITVD--SNEIYIEDLGSTNGTFVNDFK-----RIKGPAKLHPNDIIKLG 88
|
|
| FHA_DgcB-like |
cd22682 |
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ... |
14-106 |
3.69e-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: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 14 SHPFQERHvyldepIKIGRSVarcrpaQNNATFDCKVLSRNHALvwFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEesp 93
Cdd:cd22682 14 QFPITEST------IVIGRSV------ESQVQIDDDSVSRYHAK--LAVNPSAVSIIDLGSTNGTIVNGKKIPKLAS--- 76
|
90
....*....|...
gi 1907106177 94 pCEILSGDIIQFG 106
Cdd:cd22682 77 -CDLQNGDQIKIG 88
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
223-694 |
4.84e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 223 QLQACSKNQTEDSLRKELIALQEDKHSYE--------TTAKESLRRVLQEKIEVVRK-----------LSEVERSLSNTE 283
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDEN 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 284 DECTHLKEMNERTQEELRE----LANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAK 359
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 360 IEALQADNDFTNERLTALQGIQVDDFLPKIngsTEKEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSD 439
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKV---CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 440 DttdaqmdEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHM--DMENLQEEKDTEISSTRDKLLS 517
Cdd:TIGR00606 834 K-------QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqQFEEQLVELSTEVQSLIREIKD 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 518 AQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGEL 597
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQL 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 598 EKLKKEWDVLETECHSLKKenvllSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVG-----SLKEQHLRDAA 672
Cdd:TIGR00606 987 EECEKHQEKINEDMRLMRQ-----DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGqmqvlQMKQEHQKLEE 1061
|
490 500
....*....|....*....|..
gi 1907106177 673 DLKtLLSKAENQAKDVQKEYEK 694
Cdd:TIGR00606 1062 NID-LIKRNHVLALGRQKGYEK 1082
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
239-725 |
5.02e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 239 ELIALQEDKHSYETTAKES-LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKqVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQEL-QAKIEALQADNDFTNERLTALQGIQVDDflPKINGSTEKE 396
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQ--QRLEKNEDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 397 KLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQV 476
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 477 EESAKQIQVLQVQLQKLHMDMENlQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEG 556
Cdd:pfam05483 460 TAIKTSEEHYLKEVEDLKTELEK-EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 557 WRKAASEYENEIRSLQSSFQLRCQQCE---DQQREEATRLQGELEKLKKEWDVLETECHSLKKEnvllsselqrqekeLH 633
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--------------IE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 634 NSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQtvLSELKLkFEMTEQEK 713
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK--ISEEKL-LEEVEKAK 681
|
490
....*....|..
gi 1907106177 714 QSITDELKQCKD 725
Cdd:pfam05483 682 AIADEAVKLQKE 693
|
|
| FHA_MDC1 |
cd22665 |
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ... |
13-110 |
6.40e-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: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 13 NSHPFQERHVYLDE-PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTskFYLQDTKSSNGTFINSQRLSrgsee 91
Cdd:cd22665 7 SQAHGPEKDFPLYEgENVIGRD------PSCSVVLPDKSVSKQHACIEVDGGT--HLIEDLGSTNGTRIGNKVRL----- 73
|
90 100
....*....|....*....|.
gi 1907106177 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 |
6.78e-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: 6.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907106177 52 SRNHALVWFDH---------KTSKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQFGV 107
Cdd:cd22667 40 SRKHATLTVLHpeanlsdpdTRPELTLKDL-SKYGTFVNGEKLKGGSE----VTLKDGDVITFGV 99
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-722 |
6.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKgQAEKKELQTKIDEMEEKEQELQAKIEALQADND 368
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 369 F--TNERLTALQgIQVDDFLPKINGSTEKEKLMVQghltkvVEESKLSKENQAKAKESDLsdtlspsKEKSSDDTTDAQM 446
Cdd:COG4717 127 LlpLYQELEALE-AELAELPERLEELEERLEELRE------LEEELEELEAELAELQEEL-------EELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 447 DEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDmENLQEEKDT--------EISSTRDKLLSA 518
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLlliaaallALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 519 QDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRcqqcEDQQREEATRLQGELE 598
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP----PDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 599 KLKKEWDVLETECHSLKkenvlLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLL 678
Cdd:COG4717 348 ELQELLREAEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907106177 679 skAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 722
Cdd:COG4717 423 --EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-722 |
7.95e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 506 TEISSTRDKLLSAQDEILLLRQAAAEAvserdTDFVSLQEELKKVRAELEGWR-----KAASEYENEIRSLQSsfQLrcq 580
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA-----ERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRA--EL--- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 581 qceDQQREEATRLQGELEKLKKEWDVLETECHSLKKENV-LLSSELQRQEKELHNsqkqsfeltsdlsiLQMTRKELEKQ 659
Cdd:COG4913 305 ---ARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEE--------------RERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907106177 660 VGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDELKQ 722
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| FHA_Rv1747-like_rpt1 |
cd22694 |
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ... |
18-86 |
1.31e-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: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 18 QERHVYLDEPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDhkTSKFYLQDTKSSNGTFINSQRLS 86
Cdd:cd22694 8 GELRFDPGSSVRIGRD------PDADVRLDDPRVSRRHALLEFD--GDGWVYTDLGSRNGTYLNGRRVQ 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
178-350 |
1.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 178 REQML--EQKLATLQRLLAITQEAsDTSWQALIDEDRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYE---T 252
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 253 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|...
gi 1907106177 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDEME 350
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
260-712 |
1.41e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 260 RVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK 339
Cdd:COG5022 954 PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 340 KelQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddfLPKINGSTEKEKLMVQghltkvveESKLSKENQA 419
Cdd:COG5022 1034 I--ISSESTELSILKPLQKLKGLLLLENNQLQARYKALK-------LRRENSLLDDKQLYQL--------ESTENLLKTI 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 420 KAKESDLSDTLSpSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMEN 499
Cdd:COG5022 1097 NVKDLEVTNRNL-VKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFA 1175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 500 LQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKvrAELEGWRKAASEYE-NEIRSLQSSFQLR 578
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKK--LISEGWVPTEYSTSlKGFNNLNKKFDTP 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 579 CQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKE-NVLLSSELQRQEKELhnSQKQSFELTSDLSILQMTRKELE 657
Cdd:COG5022 1254 ASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYiNVGLFNALRTKASSL--RWKSATEVNYNSEELDDWCREFE 1331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106177 658 KQVGSLKEQHLRDAADLKTLLSKAENQAKDV-QKEYEKTQTVLSELKLKFEMTEQE 712
Cdd:COG5022 1332 ISDVDEELEELIQAVKVLQLLKDDLNKLDELlDACYSLNPAEIQNLKSRYDPADKE 1387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-493 |
1.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQkgqaEKKELQTKIDEMEEKEQELQAKIEALQADnd 368
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAELRAELEAQKEE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 369 fTNERLTALQGIQVDDFLPKINGSTEKEKLMVQGHLTKVVEESKLSKENQAKAKESDLSDT---LSPSKEKSSDDTTDAQ 445
Cdd:COG4942 106 -LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraeLEAERAELEALLAELE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907106177 446 MDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQVLQVQLQKL 493
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| FHA_CHFR |
cd22672 |
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ... |
49-105 |
1.82e-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: 1.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 49 KVLSRNHALVWFDHKTsKFYLQDTkSSNGTFINSQRLSRGSEesppCEILSGDIIQF 105
Cdd:cd22672 39 KLVSGDHCKIIRDEKG-QVWLEDT-STNGTLVNKVKVVKGQK----VELKHGDVIYL 89
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-478 |
1.83e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 294 ERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD------N 367
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 368 DFTNERLTALQGIQ-VDDFLPKINGSTekeklMVQGHLTKVVEESKLSKEnQAKAKESDLSDTlspsKEKSSDDTTDAQM 446
Cdd:COG3883 99 GGSVSYLDVLLGSEsFSDFLDRLSALS-----KIADADADLLEELKADKA-ELEAKKAELEAK----LAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|..
gi 1907106177 447 DEQDLNEPLAKVSLLKALLEEERKAYRNQVEE 478
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
257-555 |
2.19e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 257 SLRRVLQEKIEVVRKLSEVERslsnteDECTHLKEmNERTqEELRELANKYNGAVNEIKDLSDKLKVAEGKQ-------- 328
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHI------EDLKEELS-NERL-RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvksl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADndftNERLTALQGIQVDD-----------FLPKINgSTEKEK 397
Cdd:PRK05771 85 EELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE----IERLEPWGNFDLDLslllgfkyvsvFVGTVP-EDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 398 LMVQGHLTKVVEESKLSKEN-----QAKAKESDLSDTLSpskekssddttDAQMDEQDLNEPLAKVSLLKALLEE--ERK 470
Cdd:PRK05771 160 LKLESDVENVEYISTDKGYVyvvvvVLKELSDEVEEELK-----------KLGFERLELEEEGTPSELIREIKEEleEIE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 471 AYRNQVEESAKqiqvlqvqlqklhmdmenlqeekdtEISSTRDKLLSAQDEILLLRQAAAEAVSE-RDTD-FVSLQ---- 544
Cdd:PRK05771 229 KERESLLEELK-------------------------ELAKKYLEELLALYEYLEIELERAEALSKfLKTDkTFAIEgwvp 283
|
330
....*....|..
gi 1907106177 545 -EELKKVRAELE 555
Cdd:PRK05771 284 eDRVKKLKELID 295
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
302-650 |
2.65e-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: 44.34 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 302 ELANKYNG-AVNEIKDLSDKLKVAEGKQ--EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNdftnERLTALq 378
Cdd:pfam17380 255 EYTVRYNGqTMTENEFLNQLLHIVQHQKavSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEK----ARQAEM- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 379 giqvdDFLPKINGSTEKEKLMVQGHLTKVVEESKlsKENQAKAKESDLSDTLSPSKEKSSddttdAQMDEQDLNEPLAK- 457
Cdd:pfam17380 330 -----DRQAAIYAEQERMAMERERELERIRQEER--KRELERIRQEEIAMEISRMRELER-----LQMERQQKNERVRQe 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 458 --VSLLKALLEEERKayRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAE---- 531
Cdd:pfam17380 398 leAARKVKILEEERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrk 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 532 -AVSERDTDFVSLQEELKK--VRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQR----EEATRLQGELEKLKK-- 602
Cdd:pfam17380 476 kLELEKEKRDRKRAEEQRRkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrreaEEERRKQQEMEERRRiq 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907106177 603 EWDVLETECHSlKKENVLLSSELQRQEKELHNSQKQsFELTSDLSILQ 650
Cdd:pfam17380 556 EQMRKATEERS-RLEAMEREREMMRQIVESEKARAE-YEATTPITTIK 601
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-609 |
2.68e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 182 LEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEvmgnqlqacSKNQTEDSLRKELIALQEDKHSYETTaKESLRRV 261
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHE---------ERREELETLEAEIEDLRETIAETERE-REELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 262 LQEKIEVVRKLSEVERSL-----------SNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEE 330
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 331 IQQKGQAEKKELQ---TKIDEMEEKEQELQAKIEALQADNDFTNERLTALQGIQvDDFLPKINGSTEKEKLMVqghlTKV 407
Cdd:PRK02224 361 LREEAAELESELEearEAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL-EELREERDELREREAELE----ATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 408 VEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEqdlneplakvsllKALLEEERKAYRNQVEESAKqiqvlq 487
Cdd:PRK02224 436 RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRER-------------VEELEAELEDLEEEVEEVEE------ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 488 vqlqklhmDMENLQEEKDTEisSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENE 567
Cdd:PRK02224 497 --------RLERAEDLVEAE--DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907106177 568 IrslqssfqlrcqqceDQQREEATRLQGELEKLKKEWDVLET 609
Cdd:PRK02224 567 A---------------EEAREEVAELNSKLAELKERIESLER 593
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-378 |
2.68e-04 |
|
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: 43.37 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 258 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQ----- 332
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907106177 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
510-701 |
2.80e-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: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 510 STRDKLLSAQDEILLLRQAAAEAVSERDTdfvsLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQcedQQREE 589
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE---AELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 590 ATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQsfeltsdlsiLQMTRKELEkQVGSLKEQHLR 669
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----------LDELQDRLE-AAEDLARLELR 748
|
170 180 190
....*....|....*....|....*....|..
gi 1907106177 670 DAADLKTLLSKAENQAKDVQKEYEKTQTVLSE 701
Cdd:COG4913 749 ALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
496-735 |
2.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 496 DMENLQEEKDTEISSTRDKLLSAQDEILLLRqAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSsf 575
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 576 QLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRK- 654
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKk 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 655 --ELEKQVGSLKEQHlRDAADLKTLLSKAENQAKdvqkeyEKTQTVLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 732
Cdd:PRK03918 347 lkELEKRLEELEERH-ELYEEAKAKKEELERLKK------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
...
gi 1907106177 733 KGN 735
Cdd:PRK03918 420 EIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
493-719 |
3.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 493 LHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAvSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIRSLQ 572
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 573 SSFQLRcqqcedQQREEATRLQGELEKLKKEWDVLETECHSLKkenvllssELQRQEKELHNSqkqsfeltsdlsiLQMT 652
Cdd:COG4717 123 KLLQLL------PLYQELEALEAELAELPERLEELEERLEELR--------ELEEELEELEAE-------------LAEL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 653 RKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQSITDE 719
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
234-715 |
3.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 234 DSLRKELIALQEDKHSYETtAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNER--TQEELRELANKYNGAV 311
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 312 NEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpking 391
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ------------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 392 sTEKEKLMVQghLTKVVEESKLSKENQAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERKa 471
Cdd:COG4717 220 -EELEELEEE--LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 472 yrnqveesAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLlrqaaaeavserdtDFVSLQEELKKVR 551
Cdd:COG4717 296 --------EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL--------------ELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 552 AELEGWRKAA--SEYENEIRSLQSSFQLrcqQCEDQQREEATRLQgELEKLKKEWDVLETECHSLKKENVLLSSELQRQ- 628
Cdd:COG4717 354 REAEELEEELqlEELEQEIAALLAEAGV---EDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDEEe 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 629 -EKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQHlrDAADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFE 707
Cdd:COG4717 430 lEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
....*...
gi 1907106177 708 MTEQEKQS 715
Cdd:COG4717 508 EYREERLP 515
|
|
| FHA_FHAD1 |
cd22700 |
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ... |
53-106 |
4.54e-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: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907106177 53 RNHALVWFDHKTSKFYLQDTKSSNGTFINSQRLSRGSEESPPceilsGDIIQFG 106
Cdd:cd22700 36 EQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQNAAVRLAP-----GDVLRFG 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
546-732 |
4.70e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 546 ELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCeDQQREEATRLQGELEKL---KKEWDVLETECHSLKKENVLLS 622
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-NEISSELPELREELEKLekeVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 623 SELQRQEKELHNSQKQSFELTSDLSILQMTRKELEK---------QVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYE 693
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907106177 694 KtqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLLRE 732
Cdd:PRK03918 332 E----LEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
|
| FHA_ZEP-like |
cd22702 |
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ... |
25-108 |
4.71e-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: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 25 DEPIKIGRsvarcRPAQNNAT----FDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSR-GSEESPPCEILS 99
Cdd:cd22702 31 KQPCIIGS-----DPHQAISGisvvIPSPQVSELHARITC--KNGAFFLTDLGSEHGTWINDNEGRRyRAPPNFPVRLHP 103
|
....*....
gi 1907106177 100 GDIIQFGVD 108
Cdd:cd22702 104 SDVIEFGSD 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-733 |
5.42e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 251 ETTAKESLRRVLQ-EKIEVVRKLSEVERSLSNTEDECTHLKEMNERTQEELR-ELANKYNGA--VNEIKDLSDKLKVAE- 325
Cdd:PTZ00121 1114 ARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaEEARKAEDAkkAEAARKAEEVRKAEEl 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 326 GKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKI------------EALQADNDFTNERLTALQGIQVDDFLPKINGST 393
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 394 EKEKLMV----------QGHLTKVVEESKLSKENQAKAKESDLSDTLSPSKE--KSSDDTTDAQMDEQDLNEPLAKVSLL 461
Cdd:PTZ00121 1274 AEEARKAdelkkaeekkKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEeaKKKADAAKKKAEEAKKAAEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 462 KALLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEE---KDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDT 538
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakkKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 539 DFVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKEN 618
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 619 VLLSSELQRQEKELHNSQKQSfeltsdlsilqmTRKELEKQVGSLKEQHLRDAADLKtllsKAENQAKDVQKEYEKTQTV 698
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAK------------KADEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAEEDKN 1577
|
490 500 510
....*....|....*....|....*....|....*
gi 1907106177 699 LSELKLKfEMTEQEKQSITDELKQCKDNLKLLREK 733
Cdd:PTZ00121 1578 MALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| FHA_FhaB-like |
cd22693 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
16-111 |
5.90e-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: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 16 PFQERHVYLD-EPIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFdhKTSKFYLQDTKSSNGTFINSQRLSRgseespP 94
Cdd:cd22693 7 TLQGQTFPIDkSGITIGRA------DDNDLVLSDDFVSSRHARIYL--QGSSWYLEDLGSTNGTFVNGNRVTQ------P 72
|
90
....*....|....*..
gi 1907106177 95 CEILSGDIIQFGVDVTE 111
Cdd:cd22693 73 VVVQPGDTIRIGATVFE 89
|
|
| FHA_DUN1-like |
cd22683 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ... |
52-106 |
7.06e-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: 7.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907106177 52 SRNHALVWFDHKTSKFYLQ-----------DTKSSNGTFINSQRLSRGSeesppCEILSGDIIQFG 106
Cdd:cd22683 28 SRSCDLVLSDPSISRFHAElrleqnginviDNNSANGTFINGKRIKGKT-----YILKNGDIIVFG 88
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
589-712 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 589 EATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNsQKQSFELTSDLSilqmtrkELEKQVGSLKeqhl 668
Cdd:pfam15294 134 EIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGA-KKDVKSNLKEIS-------DLEEKMAALK---- 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907106177 669 rdaADLKTLLSKAENQAKDVQKEYEKTQTVLSELKLKFEMTEQE 712
Cdd:pfam15294 202 ---SDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-574 |
1.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 329 EEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgiqvddflpkingsTEKEKLmvqghltkvv 408
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ--------------AEIDKL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 409 EESKLSKENQAKAKESDLSDTLSPSKEKSSD-DTTDAQMDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQiqvlq 487
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSvSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAEL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 488 vqlqklhmdmenlqEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENE 567
Cdd:COG3883 146 --------------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
....*..
gi 1907106177 568 IRSLQSS 574
Cdd:COG3883 212 AAAAAAA 218
|
|
| FHA_FhaA-like |
cd22668 |
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ... |
27-106 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 27 PIKIGRSvarcrpAQNNATFDCKVLSRNHALVWFDHKTSkfYLQDTKSSNGTFINSQRLsrgseeSPPCEILSGDIIQFG 106
Cdd:cd22668 19 SNIIGRG------SDADFRLPDTGVSRRHAEIRWDGQVA--HLTDLGSTNGTTVNNAPV------TPEWRLADGDVITLG 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
163-348 |
1.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWqALIDEDRLLSRLEVMGNQLQACSKNQTE-DSLRKELI 241
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDASSDDlAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 242 ALQEDkhsyettakesLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLK----EMNERTQEELRELANKYNGAVNEIKDL 317
Cdd:COG4913 696 ELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQdrleAAEDLARLELRALLEERFAAALGDAVE 764
|
170 180 190
....*....|....*....|....*....|.
gi 1907106177 318 SDKLKVAEGKQEEIQQKGQAEKKELQTKIDE 348
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| FHA_PML1-like |
cd22681 |
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ... |
49-112 |
1.77e-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: 38.96 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 49 KVLSRNHALVWFDHKTS--KFYLQDTKSSNGTFINsqrlsrgSEESPPC---EILSGDIIQFGVDVTEN 112
Cdd:cd22681 64 ETCSKQHCVIQFRNVKGilKPYIMDLDSSNGTCLN-------DNVIPSSryvELRSGDVITFSKSNDYE 125
|
|
| COG3456 |
COG3456 |
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ... |
1-106 |
1.81e-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: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 1 MPSALAIFTCRPNSHPFQERHVYLDEPIKIGRSvARC-----RPAQnnatfdckVLSRNHALVWFDHktSKFYLQDTkSS 75
Cdd:COG3456 1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRS-ADCdwvlpDPDR--------SVSRRHAEIRFRD--GAFCLTDL-ST 68
|
90 100 110
....*....|....*....|....*....|...
gi 1907106177 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, ... |
465-691 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 465 LEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLqeekDTEISSTRDKLLSAQDEILLLRQAAAEavserdtdfvsLQ 544
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAE-----------LE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 545 EELKKVRAELEGWRKaasEYENEIRSLQSS-------FQLRCQQCEDQQREeATRLQGELEKLKKEWDVLETECHSLKKE 617
Cdd:COG4942 90 KEIAELRAELEAQKE---ELAELLRALYRLgrqpplaLLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907106177 618 NVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKEQ---HLRDAADLKTLLSKAENQAKDVQKE 691
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
514-691 |
1.88e-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: 40.68 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 514 KLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELEGWRKAASEYENEIrslqssfqlrcqqceDQQREEATRL 593
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 594 QGELEKLK--KEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQmtrKELEKQVGSLKEQHLRDA 671
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|
gi 1907106177 672 ADLKTLLSKAENQAKDVQKE 691
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
172-361 |
2.04e-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: 39.89 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 172 LQEALHREQMLEQKLATLQRLLaitqeasdtswQALIDEDRLLSRLEVmgNQLQACSKNQTEDSLRKELIAlqedKHSYE 251
Cdd:pfam15619 6 LSARLHKIKELQNELAELQSKL-----------EELRKENRLLKRLQK--RQEKALGKYEGTESELPQLIA----RHNEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 252 T-TAKESLRRvLQEKIEVV-RKLSEVERSLSNTEDECTHL------KEMNERT--QEELRELANKYNGAVNEIKDLSDKL 321
Cdd:pfam15619 69 VrVLRERLRR-LQEKERDLeRKLKEKEAELLRLRDQLKRLeklsedKNLAEREelQKKLEQLEAKLEDKDEKIQDLERKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907106177 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIE 361
Cdd:pfam15619 148 ELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-561 |
2.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 266 IEVVRKLSEVERSLSNTEDECTHLkemnertqEELRELANKYNGAVNEIKDLSDKLKVAEgkqeeiQQKGQAEKKELQTK 345
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELL--------EPIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 346 IDEMEEKEQELQAKIEALQADNDFTNERLTALQGiQVDDflpkiNGSTEKEKL--MVQGHLTKVVEESKLSKENQAKAKE 423
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEA-QIRG-----NGGDRLEQLerEIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 424 SDLSDTLspskekssddttdaqmDEQDLNEPLAKVSLLKALLEEERKAYRNQVEESAKQIQvlqvqlqklhmDMENLQEE 503
Cdd:COG4913 371 LGLPLPA----------------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-----------DLRRELRE 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907106177 504 KDTEISS--TRDKLLSAqdEILLLRQAAAEA--VSERDTDFVSlqeELKKVRAELEGWRKAA 561
Cdd:COG4913 424 LEAEIASleRRKSNIPA--RLLALRDALAEAlgLDEAELPFVG---ELIEVRPEEERWRGAI 480
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-366 |
2.46e-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: 40.29 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 173 QEALHREQMLEQKLATLQRLLAitqeasdtswqalidedRLLSRLEVMGNQLQACSKNQTEDSLRKELIALQEDKHSYET 252
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLK-----------------ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 253 TAKESLRRVLQEKIEVVRKlsevERSLSNTEDECTHLKEMNERTQEELRELankyngaVNEIKDLSDKLKVAEGKQEEIQ 332
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRN----NKEYEALQKEIESLKRRISDLEDEILEL-------MERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....
gi 1907106177 333 QKGQAEKKELQTKIDEMEEKEQELQAKIEALQAD 366
Cdd:COG1579 138 AELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-378 |
2.69e-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: 40.99 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 274 EVERSLSNTEDECTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEK----------K 340
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeelE 367
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907106177 341 ELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQ 378
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFK 405
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-366 |
3.21e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 208 IDEDRLLSRLEVMGNQLQACSKNQTE---DSLRKELIALQED-KHSYETTAKEslrrvLQEKIEVVRKLSEVERSLsnte 283
Cdd:PRK04778 249 LDHLDIEKEIQDLKEQIDENLALLEEldlDEAEEKNEEIQERiDQLYDILERE-----VKARKYVEKNSDTLPDFL---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 284 decTHLKEMNERTQEELRELANKY---NGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKK---ELQTKIDEMEEKEQELQ 357
Cdd:PRK04778 320 ---EHAKEQNKELKEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIaysELQEELEEILKQLEEIE 396
|
....*....
gi 1907106177 358 AKIEALQAD 366
Cdd:PRK04778 397 KEQEKLSEM 405
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-730 |
3.34e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 150 VDKVAANTPSMYSQELFqLSQYLQEALHREQMLEQKLATLQRLLAITQEASDTSWQALIDEDRLLSRLEVMGNQLQACsK 229
Cdd:pfam15921 460 LEKVSSLTAQLESTKEM-LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL-K 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 230 NQtEDSLRKelIALQEDKHSYETTAKESLRRVLQEKIEVVRKL---------------SEVERSLSNTEDECTHLKEMNE 294
Cdd:pfam15921 538 NE-GDHLRN--VQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtagamqvekAQLEKEINDRRLELQEFKILKD 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 295 RTQEELRELANKYNG-----------------AVNEIKDLSDKL----KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKE 353
Cdd:pfam15921 615 KKDAKIRELEARVSDlelekvklvnagserlrAVKDIKQERDQLlnevKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 354 QELQAKIEALQADNDFTNERLTALQGiqVDDFLPKINGSTEKEKLMVQGHLTKVVEESKLSKE------------NQAKA 421
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEG--SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtnankekhflKEEKN 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 422 KESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLA--KVSLLKALLE--EERKAYRNQVEESAKQIQVLQvqlqklhMDM 497
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmEVALDKASLQfaECQDIIQRQEQESVRLKLQHT-------LDV 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 498 ENLQEEKDTEISSTRDKLL-------------SAQDEILLLRQAA--AEAVSERDT-DFVSLQEELKKV----------R 551
Cdd:pfam15921 846 KELQGPGYTSNSSMKPRLLqpasftrthsnvpSSQSTASFLSHHSrkTNALKEDPTrDLKQLLQELRSVineeptvqlsK 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 552 AELEGWRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKLKKE-----WDVLETECHSLKKENVLLSSELQ 626
Cdd:pfam15921 926 AEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREpvllhAGELEDPSSCFTFPSTASPSVKN 1005
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 627 RQEKELHNSQKQSfELTSDLSILQMTRKELEKQVGSLKEQHLRDAA-DLKTL-LSKAENQAKDVQKEYEKTQTVLSELKL 704
Cdd:pfam15921 1006 SASRSFHSSPKKS-PVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVkDSQSLpIETTGKTCRKLQNRLESLQTLVEDLQL 1084
|
650 660
....*....|....*....|....*.
gi 1907106177 705 KFEMTEQEKQSITDELKQCKDNLKLL 730
Cdd:pfam15921 1085 KNQAMSSMIRNQEKRIQKVKDQEKML 1110
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
563-721 |
3.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 563 EYENEIRSLQssfQLRCQQceDQQREEATRLQGELEKLKKEWdvletechSLKKEnvllssELQRQEKELHNSQKQSFEl 642
Cdd:PRK00409 517 KLNELIASLE---ELEREL--EQKAEEAEALLKEAEKLKEEL--------EEKKE------KLQEEEDKLLEEAEKEAQ- 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907106177 643 tsdlSILQMTRKELEKQVGSLKEQHLRDAADLKtllskaENQAKDVQKEYEKTQTVLSELKLKfEMTEQEKQSITDELK 721
Cdd:PRK00409 577 ----QAIKEAKKEADEIIKELRQLQKGGYASVK------AHELIEARKRLNKANEKKEKKKKK-QKEKQEELKVGDEVK 644
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
256-359 |
3.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 256 ESLRRVLQEKI-EVVRKLSEVERSLSNTEDEcthLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQK 334
Cdd:PRK00409 526 EELERELEQKAeEAEALLKEAEKLKEELEEK---KEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100
....*....|....*....|....*
gi 1907106177 335 GQAEkKELQTKIDEMEEKEQELQAK 359
Cdd:PRK00409 603 SVKA-HELIEARKRLNKANEKKEKK 626
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-733 |
3.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 586 QREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGSLKE 665
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 666 QHLRDAADLKTLLSKAE-------------------------------NQAKDVQKEYEKTQTVLSELKLKFEMTEQEKQ 714
Cdd:COG4942 98 ELEAQKEELAELLRALYrlgrqpplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*....
gi 1907106177 715 SITDELKQCKDNLKLLREK 733
Cdd:COG4942 178 ALLAELEEERAALEALKAE 196
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
289-568 |
3.84e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 289 LKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALqadnd 368
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 369 ftNERLTALQgIQVDDFlpkingstekeklmvqghltkvveESKLSKENQAKAKESDLSDTLSpSKEKSSDDTTDAQMDE 448
Cdd:PHA02562 240 --TDELLNLV-MDIEDP------------------------SAALNKLNTAAAKIKSKIEQFQ-KVIKMYEKGGVCPTCT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 449 QDLNEPLAKVSLLKALLEEERKAYR---NQVEESAKQIQVLQVQLQKLHmDMENLQEEKDTEISSTRDKLLSAQDEIlll 525
Cdd:PHA02562 292 QQISEGPDRITKIKDKLKELQHSLEkldTAIDELEEIMDEFNEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAAI--- 367
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907106177 526 RQAAAEavserdtdFVSLQEELKKVRAELEGWRKAASEYENEI 568
Cdd:PHA02562 368 EELQAE--------FVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
493-632 |
3.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 493 LHMDMENLQEEK---DTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDfvsLQEELKKVRAELEGWRKAASEYENEIR 569
Cdd:COG4913 293 LEAELEELRAELarlEAELERLEARLDALREELDELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 570 SLQSS-----------------FQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVLLSSELQRQEKEL 632
Cdd:COG4913 370 ALGLPlpasaeefaalraeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
313-730 |
4.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 313 EIKDLSDKLKVAEGKQEEIQQKGQAEKKELQTK---IDEMEEKEQELQAKIEALQADndftNERLTALQGiqvddflpKI 389
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVlreINEISSELPELREELEKLEKE----VKELEELKE--------EI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 390 NGStEKEKLMVQGHLTKVVEESKLSKE--NQAKAKESDLSDTLSPSKEKSSDDTTDAQMDE--QDLNEPLAKVSLLKALL 465
Cdd:PRK03918 241 EEL-EKELESLEGSKRKLEEKIRELEEriEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 466 EEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQA------AAEAVSERDTD 539
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpekLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 540 FVSLQEELKKVRAELEGWRKAASEYENEIRSLQSSfQLRCQQC-----EDQQREEATRLQGELEKLKKEWDVLETECHSL 614
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCPVCgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 615 KKENVLLSSELQRQEKELhnSQKQSFELtsdlsiLQMTRKELEKQVGSLKEQHLRDAADLKTLLSKAENQAKDVQKEYEK 694
Cdd:PRK03918 479 RKELRELEKVLKKESELI--KLKELAEQ------LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907106177 695 tqtvLSELKLKFEMTEQEKQSITDELKQCKDNLKLL 730
Cdd:PRK03918 551 ----LEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
587-713 |
5.16e-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: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 587 REEATRLQGELEKLKKEWDVLETECHSLKK----ENVLLSSELQRQEKELHNSQKQSFELTSDLSILQMTRKELEKQVGS 662
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEELRQLKQledeLEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907106177 663 LKEQHLrdaaDLKTLLSKAENQAKDVQKeyeKTQTVLSELKLKFEMTEQEK 713
Cdd:smart00787 244 LTNKKS----ELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSLT 287
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-600 |
5.41e-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: 40.34 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 251 ETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE----DECTHLKEMNERTQEELRELANKYNGAVNEIKDLSDKLKVAEG 326
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKeqakKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 327 KQEEIQQKGQ---AEKKELQTKIDEMEEKEQELQ--------AKIEALQADNDFTNERLTALQGIQVDDFLPKINGSTEK 395
Cdd:pfam02463 251 EEIESSKQEIekeEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 396 EKLMVQGHLTKVVEESKLSKENQAKAKESDLSDTLspskekssddttdaQMDEQDLNEPLAKVSLLKALLEEERKAyRNQ 475
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ--------------EKLEQLEEELLAKKKLESERLSSAAKL-KEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 476 VEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISSTRDKLLSAQDEILLLRQAAAEAVSERDTDFVSLQEELKKVRAELE 555
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907106177 556 GWRKAAS-EYENEIRSLQSSFQLRCQQCEDQQREEATRLQGELEKL 600
Cdd:pfam02463 476 ETQLVKLqEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
256-698 |
6.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 256 ESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNEI--------------KDLSDKL 321
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLKSIeslkkkieeyskniERMSAFI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 322 KVAEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQAKIEALQADNDftnerltalqgiqvddflpkingSTEKEKLMVQ 401
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD-----------------------ELSRNMEMLN 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 402 GHLTKVVEESKLSKEnqakaKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLE----EERKAYRNQVE 477
Cdd:PRK01156 451 GQSVCPVCGTTLGEE-----KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 478 ESAKQIQVLQVQLQKLHmDMENLQEEKDTEISSTRDKLLSAQDEILLlrqaaaEAVSERDT-DFVSLQEELKKVRAELEG 556
Cdd:PRK01156 526 SARADLEDIKIKINELK-DKHDKYEEIKNRYKSLKLEDLDSKRTSWL------NALAVISLiDIETNRSRSNEIKKQLND 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 557 WRKAASEYENEIRSLQSSFQLRCQQCEDQQREEATRLQgELEKLKKEWDVLETECHSLKKEnvllSSELQRQEKELHnsq 636
Cdd:PRK01156 599 LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLK--- 670
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907106177 637 kqsfELTSDLSILQMTRKELEKQVGSLKEQHLRDAADLKTLLS---KAENQAKDVQKEYEKTQTV 698
Cdd:PRK01156 671 ----EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTrinELSDRINDINETLESMKKI 731
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
530-692 |
8.22e-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: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 530 AEAVSERDTDfvSLQEELKKVRAELEGWRKAASEYENEIRSLQSSFQlrcqqcedQQREEATRLQGELEKLKKEWDVLET 609
Cdd:COG2433 379 EEALEELIEK--ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE--------RLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 610 ECHSLKKE---NVLLSSELQRQEKELHNsqkqsfeLTSDLSILQMTRKELEKQVGSLKE----QHLRDAADLKTLLSKAE 682
Cdd:COG2433 449 ELSEARSEerrEIRKDREISRLDREIER-------LERELEEERERIEELKRKLERLKElwklEHSGELVPVKVVEKFTK 521
|
170
....*....|
gi 1907106177 683 NQAKDVQKEY 692
Cdd:COG2433 522 EAIRRLEEEY 531
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
163-365 |
8.29e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.67 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 163 QELFQLSQYLQEALHREQMLEQKLATLQRLLAITQEasdtsWQALIDEDRLLSR----LEVMGNQLQACSKNQT--EDSL 236
Cdd:COG0497 172 KELEELRADEAERARELDLLRFQLEELEAAALQPGE-----EEELEEERRRLSNaeklREALQEALEALSGGEGgaLDLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 237 ---RKELIALQEDKHSYETTAkESLRRVLQEKIEVVRklsEVERSLSNTEDECTHLKEMNERtQEELRELANKYNGAVNE 313
Cdd:COG0497 247 gqaLRALERLAEYDPSLAELA-ERLESALIELEEAAS---ELRRYLDSLEFDPERLEEVEER-LALLRRLARKYGVTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907106177 314 IKDLSDKLkvaegkqeeiqqkgQAEKKELQTKIDEMEEKEQELQAKIEALQA 365
Cdd:COG0497 322 LLAYAEEL--------------RAELAELENSDERLEELEAELAEAEAELLE 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
545-736 |
9.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 545 EELKKVRAELEGWRKAASEYENEIRSLQssfQLRcQQCE--DQQREEATRLQGELEKLKKEWDVLETEchslkkenvLLS 622
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE---PIR-ELAEryAAARERLAELEYLRAALRLWFAQRRLE---------LLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 623 SELQRQEKELHnsqkqsfELTSDLSILQMTRKELEKQVGSLKEQHL----RDAADLKTLLSKAENQAKDVQKEYEKTQTV 698
Cdd:COG4913 295 AELEELRAELA-------RLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907106177 699 LSELKLKFEMTEQEKQSITDELKQCKDNLKLLREKGNN 736
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
213-549 |
9.52e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 213 LLSRLEVMGNQLQACSKNQteDSLRKELIALQE--DKHSYETTAKESLRRVLQEKIE---------VVRKLSEVERSLSN 281
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQL--ASLEEELEKLTEeiSELEKRLEEIEQLLEELNKKIKdlgeeeqlrVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 282 TEDECTHLKEMNERTQEELRELANKYNGAVNEIKDLsdklkvaEGKQEEIQQKGQAEKKELQTKIDEMEEKEQELQakie 361
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELE---- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 362 ALQADNDFTNERLTALQgiqvddflpkingsTEKEKLMvqghltkvveesklSKENQAKAKESDLSDTLSPSKEKSSDDT 441
Cdd:TIGR02169 375 EVDKEFAETRDELKDYR--------------EKLEKLK--------------REINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 442 TDAQMDEQDLNEplakvsllkalLEEERKAYRNQVEESAKQIQVLQVQLQKLHMDMENLQEekdtEISSTRDKLLSAQDE 521
Cdd:TIGR02169 427 AAIAGIEAKINE-----------LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE----EYDRVEKELSKLQRE 491
|
330 340
....*....|....*....|....*...
gi 1907106177 522 ILLLrQAAAEAVSERDTDFVSLQEELKK 549
Cdd:TIGR02169 492 LAEA-EAQARASEERVRGGRAVEEVLKA 518
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
339-715 |
9.60e-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: 39.34 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 339 KKELQTKIDEMEEKEQELQAKIEALQADNDFTNERLTALQgIQVDDFLPKINGSTEKEKLMVQGH-LTKVVEESKLSKEN 417
Cdd:pfam05557 15 QNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQ-KRIRLLEKREAEAEEALREQAELNrLKKKYLEALNKKLN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 418 QAKAKESDLSDTLSPSKEKSSDDTTDAQMDEQDLNEPLAKVSLLKALLEEERK--------------------------- 470
Cdd:pfam05557 94 EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAkaseaeqlrqnlekqqsslaeaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 471 --AYRNQVEESAKQIQVLQVQLQKLHMDMENLQEEKDTEISstrdKLLSAQDEILLLR------QAAAEAVSERDTDFVS 542
Cdd:pfam05557 174 elEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK----HLNENIENKLLLKeevedlKRKLEREEKYREEAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 543 LQEELKKVRAELEGWRKAASEYENEIRS--LQSSFQLRCQQCEDQQREEATRLQGELEKLKKEWDVLETECHSLKKENVL 620
Cdd:pfam05557 250 LELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907106177 621 LSSELQRQEKELHNSQKQSFELTSDL----SILQMTRKEL-EKQVGSLKEQHLRDAADlktLLSKAENQAKDVQKEYEKT 695
Cdd:pfam05557 330 LNKKLKRHKALVRRLQRRVLLLTKERdgyrAILESYDKELtMSNYSPQLLERIEEAED---MTQKMQAHNEEMEAQLSVA 406
|
410 420
....*....|....*....|
gi 1907106177 696 QTVLSELKLKFEMTEQEKQS 715
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQA 426
|
|
| |
