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Conserved domains on  [gi|1943700588|ref|NP_990767|]
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intestinal zipper protein precursor [Gallus gallus]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
37-148 2.36e-36

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05713:

Pssm-ID: 472250  Cd Length: 114  Bit Score: 129.23  E-value: 2.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  37 TVVAPSLRVTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSGFVHHYRNGEDL--EQMTEYKGRTELLRKGLSDGNLDL 114
Cdd:cd05713     2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQeeEQMPEYRGRTELLKDAIAEGSVAL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1943700588 115 RITAVSSSDSGLYSCAVQDGDDgYAEALVELEVS 148
Cdd:cd05713    82 RIHNVRPSDEGQYTCFFRSGSF-YEEATLELKVA 114
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
179-380 1.31e-10

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 63.55  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  179 LYRKKVTQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKL-DIRNSL-------MKKQYKMTEKQA 250
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALnDLEARLshsripeIQAELSKLEEEV 807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  251 AELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNL 330
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1943700588  331 KKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLE 380
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
 
Name Accession Description Interval E-value
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
37-148 2.36e-36

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 129.23  E-value: 2.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  37 TVVAPSLRVTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSGFVHHYRNGEDL--EQMTEYKGRTELLRKGLSDGNLDL 114
Cdd:cd05713     2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQeeEQMPEYRGRTELLKDAIAEGSVAL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1943700588 115 RITAVSSSDSGLYSCAVQDGDDgYAEALVELEVS 148
Cdd:cd05713    82 RIHNVRPSDEGQYTCFFRSGSF-YEEATLELKVA 114
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
45-147 1.03e-10

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 58.62  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSG----FVHHYRNGEdleQMTEYKGRTELlRKGLSDGNLDLRITAVS 120
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKgptfLIAYYSNGS---EEGVKKGRFSG-RGDPSNGDGSLTIQNLT 81
                          90       100
                  ....*....|....*....|....*..
gi 1943700588 121 SSDSGLYSCAVQDGDDGYAEALVELEV 147
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRLTV 108
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
179-380 1.31e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.55  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  179 LYRKKVTQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKL-DIRNSL-------MKKQYKMTEKQA 250
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALnDLEARLshsripeIQAELSKLEEEV 807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  251 AELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNL 330
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1943700588  331 KKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLE 380
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
45-147 8.73e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588   45 VTANVGQDVVLRCHLcpcKNAWSSDIRWiqlrssgfvhhYRNGEdleQMTEYKGRTELLRkglSDGNLDLRITAVSSSDS 124
Cdd:smart00410   4 VTVKEGESVTLSCEA---SGSPPPEVTW-----------YKQGG---KLLAESGRFSVSR---SGSTSTLTISNVTPEDS 63
                           90       100
                   ....*....|....*....|...
gi 1943700588  125 GLYSCAVQDgDDGYAEALVELEV 147
Cdd:smart00410  64 GTYTCAATN-SSGSASSGTTLTV 85
PTZ00121 PTZ00121
MAEBL; Provisional
181-422 5.68e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 5.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  181 RKKVTQSRELKRKDAMLGRKdavleelpaildssAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQA---AELEKHL 257
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRK--------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKA 1628
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  258 INTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEvENHYEEMGLRAPNLKKNIVEL 337
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEEL 1707
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  338 EKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEiqnsllkirnKHRERKNEMLEKQTVEQEQTEEWAESK 417
Cdd:PTZ00121  1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK----------KDEEEKKKIAHLKKEEEKKAEEIRKEK 1777

                   ....*
gi 1943700588  418 KSVVE 422
Cdd:PTZ00121  1778 EAVIE 1782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-433 1.15e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 187 SRELKRKDAML-GRKDAVLEELPAILDSSAANLKILASKLVKQTEKLD-----IRNSLMKKQYKMTEKQAAELEkhlINT 260
Cdd:COG1196   219 KEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEaeleeLRLELEELELELEEAQAEEYE---LLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 261 DLSAAELKIAAAKLDKQTEELDKwkSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQ 340
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERL--EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 341 TKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQL--EIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKK 418
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                         250
                  ....*....|....*
gi 1943700588 419 SVVETKELEQPSKEQ 433
Cdd:COG1196   454 LEEEEEALLELLAEL 468
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
189-433 7.86e-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: 45.10  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 189 ELKRKDAMLGRKDAVL------EELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDL 262
Cdd:pfam05483 406 ELEELKKILAEDEKLLdekkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 263 SAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENhyEEMGLR---------------- 326
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE--KEMNLRdelesvreefiqkgde 563
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 327 -----------APNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRER 395
Cdd:pfam05483 564 vkckldkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1943700588 396 KNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQ 433
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
238-409 6.44e-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: 38.46  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  238 LMKKQYKMTeKQAAELE----------KHLIN----TDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLK 303
Cdd:smart00787 114 LMDKQFQLV-KTFARLEakkmwyewrmKLLEGlkegLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  304 KQVTELAKQTkevenhyeemglraPNLKKNIVE-LEKQTKHVENRKSVLKKQYENLASHASEL-KKQAEVLEEQAEQLEI 381
Cdd:smart00787 193 QLEDELEDCD--------------PTELDRAKEkLKKLLQEIMIKVKKLEELEEELQELESKIeDLTNKKSELNTEIAEA 258
                          170       180
                   ....*....|....*....|....*...
gi 1943700588  382 QNSLLKirNKHRERKNEMLEKQTVEQEQ 409
Cdd:smart00787 259 EKKLEQ--CRGFTFKEIEKLKEQLKLLQ 284
 
Name Accession Description Interval E-value
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
37-148 2.36e-36

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 129.23  E-value: 2.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  37 TVVAPSLRVTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSGFVHHYRNGEDL--EQMTEYKGRTELLRKGLSDGNLDL 114
Cdd:cd05713     2 SVIGPTEPILALVGEDAELPCHLSPKMSAEHMEVRWFRSQFSPVVHLYRDGQDQeeEQMPEYRGRTELLKDAIAEGSVAL 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1943700588 115 RITAVSSSDSGLYSCAVQDGDDgYAEALVELEVS 148
Cdd:cd05713    82 RIHNVRPSDEGQYTCFFRSGSF-YEEATLELKVA 114
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
37-131 3.73e-14

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 68.39  E-value: 3.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  37 TVVAPSLrvTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSGFVHHYRNGED--LEQMTEYKGRTELLRKGLSDGNLDL 114
Cdd:cd20984     1 TVTAKHL--AGNIGEDGILSCTFTPDIKLSDIVIQWLKEGDSGLVHEFKEGKDelSRQSPMFRGRTSLFADQVHVGNASL 78
                          90
                  ....*....|....*..
gi 1943700588 115 RITAVSSSDSGLYSCAV 131
Cdd:cd20984    79 RLKNVQLTDAGTYLCII 95
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
41-151 1.11e-11

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 61.46  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  41 PSLRVTANVGQDVVLRCHLCPCKNAWSSDIR--WIQLRSSGFVHHYRNGEDL--EQMTEYKGRTELLRKGLSDGNLDLRI 116
Cdd:cd20934     3 PEDPVVALVGTDATLRCSFSPEPGFSLAQLSvfWQLTDTKQLVHSFTESQDQgrDQGSAYANRTALFPDLLAQGNASLRL 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1943700588 117 TAVSSSDSGLYSCAVQDGDdgYAEALVELEVSDPF 151
Cdd:cd20934    83 QRVRVADEGSYTCFVSVQD--FGSAAVSLQVAAPF 115
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
45-131 3.90e-11

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 59.71  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLCPcknawSSD--IRWIQLRSSGFVHHYRNGED-LEQMTE-YKGRTELLRKGLSDGNLDLRITAVS 120
Cdd:cd16091     7 VVCLLSEDCILPCSFTP-----GSEvvIHWYKQDSDIKVHSYYYGKDqLESQDQrYRNRTSLFKDQISNGNASLLLRRVQ 81
                          90
                  ....*....|.
gi 1943700588 121 SSDSGLYSCAV 131
Cdd:cd16091    82 LQDEGRYKCYT 92
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
45-147 1.03e-10

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 58.62  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSG----FVHHYRNGEdleQMTEYKGRTELlRKGLSDGNLDLRITAVS 120
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKgptfLIAYYSNGS---EEGVKKGRFSG-RGDPSNGDGSLTIQNLT 81
                          90       100
                  ....*....|....*....|....*..
gi 1943700588 121 SSDSGLYSCAVQDGDDGYAEALVELEV 147
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRLTV 108
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
179-380 1.31e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.55  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  179 LYRKKVTQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKL-DIRNSL-------MKKQYKMTEKQA 250
Cdd:TIGR02169  728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALnDLEARLshsripeIQAELSKLEEEV 807
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  251 AELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNL 330
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1943700588  331 KKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLE 380
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
45-147 8.73e-09

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 52.12  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588   45 VTANVGQDVVLRCHLcpcKNAWSSDIRWiqlrssgfvhhYRNGEdleQMTEYKGRTELLRkglSDGNLDLRITAVSSSDS 124
Cdd:smart00410   4 VTVKEGESVTLSCEA---SGSPPPEVTW-----------YKQGG---KLLAESGRFSVSR---SGSTSTLTISNVTPEDS 63
                           90       100
                   ....*....|....*....|...
gi 1943700588  125 GLYSCAVQDgDDGYAEALVELEV 147
Cdd:smart00410  64 GTYTCAATN-SSGSASSGTTLTV 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
180-434 9.06e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 9.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  180 YRKKVTQSRELKrKDAMLGRKDAVLEELPAILDSSAAN---LKILASKLVKQTEKLDIrnsLMKKQYKMtEKQAAELEKH 256
Cdd:TIGR02168  215 YKELKAELRELE-LALLVLRLEELREELEELQEELKEAeeeLEELTAELQELEEKLEE---LRLEVSEL-EEEIEELQKE 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  257 L--INTDLSAAELKIAAAK-----LDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPN 329
Cdd:TIGR02168  290 LyaLANEISRLEQQKQILRerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  330 LKKNIVELEKQ-------TKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHR--ERKNEML 400
Cdd:TIGR02168  370 LESRLEELEEQletlrskVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEEL 449
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1943700588  401 EKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:TIGR02168  450 EELQEELERLEEALEELREELEEAEQALDAAERE 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
241-434 1.01e-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: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  241 KQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQY-------EKLALRAANLKKQVTELAKQT 313
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  314 KEVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRN--- 390
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLedl 843
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1943700588  391 -KHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:TIGR02168  844 eEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
180-428 4.33e-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: 55.45  E-value: 4.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  180 YRKKVTQSReLKRKDAMLGRKDAVLEELPAILDSsaanLKILASK------LVKQTEKLDIRNSLM------------KK 241
Cdd:TIGR02168  172 ERRKETERK-LERTRENLDRLEDILNELERQLKS----LERQAEKaerykeLKAELRELELALLVLrleelreeleelQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  242 QYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDK-------WKSALKIQYEKLALRAANLKKQVTELAKQTK 314
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyalanEISRLEQQKQILRERLANLERQLEELEAQLE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  315 EVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEvlEEQAEQLEIQNSLLKIRNKHR- 393
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE--TLRSKVAQLELQIASLNNEIEr 404
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1943700588  394 -ERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQ 428
Cdd:TIGR02168  405 lEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
PTZ00121 PTZ00121
MAEBL; Provisional
181-422 5.68e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 5.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  181 RKKVTQSRELKRKDAMLGRKdavleelpaildssAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQA---AELEKHL 257
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRK--------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKA 1628
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  258 INTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEvENHYEEMGLRAPNLKKNIVEL 337
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEEL 1707
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  338 EKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEiqnsllkirnKHRERKNEMLEKQTVEQEQTEEWAESK 417
Cdd:PTZ00121  1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK----------KDEEEKKKIAHLKKEEEKKAEEIRKEK 1777

                   ....*
gi 1943700588  418 KSVVE 422
Cdd:PTZ00121  1778 EAVIE 1782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-433 1.15e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 187 SRELKRKDAML-GRKDAVLEELPAILDSSAANLKILASKLVKQTEKLD-----IRNSLMKKQYKMTEKQAAELEkhlINT 260
Cdd:COG1196   219 KEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEaeleeLRLELEELELELEEAQAEEYE---LLA 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 261 DLSAAELKIAAAKLDKQTEELDKwkSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQ 340
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERL--EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 341 TKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQL--EIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKK 418
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                         250
                  ....*....|....*
gi 1943700588 419 SVVETKELEQPSKEQ 433
Cdd:COG1196   454 LEEEEEALLELLAEL 468
PTZ00121 PTZ00121
MAEBL; Provisional
224-434 3.71e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  224 KLVKQTEKLDIRNSLMKKqyKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLalRAANLK 303
Cdd:PTZ00121  1564 KKAEEAKKAEEDKNMALR--KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLK 1639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  304 KQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQN 383
Cdd:PTZ00121  1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1943700588  384 SLlkiRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:PTZ00121  1720 EL---KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
PTZ00121 PTZ00121
MAEBL; Provisional
217-433 3.74e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  217 NLKILASKLVKQTEKLDIRnSLMKKQYKMTEKQAAELEKhlintdlsAAELKIAAAKLDKQtEELDKWKSALKIQYEKLA 296
Cdd:PTZ00121  1577 NMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKK--------AEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEK 1646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  297 LRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNiVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQA 376
Cdd:PTZ00121  1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1943700588  377 EQLEIQNSLLKIRNKHRERKNEMLEKQTVEQE--QTEEWAESKKSVVETKELEQPSKEQ 433
Cdd:PTZ00121  1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEEKKAEEIRKEKEAVIEEE 1784
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-434 6.88e-07

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: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 188 RELKRKDAMLGRKDAVLEELpailDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDLSAAEL 267
Cdd:COG1196   253 AELEELEAELAELEAELEEL----RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 268 KIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHVENR 347
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 348 KSVLKKQYENLASHASELKKQ-----AEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVE 422
Cdd:COG1196   409 EEALLERLERLEEELEELEEAlaeleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                         250
                  ....*....|..
gi 1943700588 423 TKELEQPSKEQD 434
Cdd:COG1196   489 AAARLLLLLEAE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
188-428 9.32e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 188 RELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEK---LDIRNSLMKKQYKMTEKQAAELEKHLINTDLSA 264
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleeLELELEEAQAEEYELLAELARLEQDIARLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 265 AELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHV 344
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 345 ENRKSVLKKQYENLASHA-------SELKKQAEVLEEQAEQLEIQnsLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESK 417
Cdd:COG1196   392 LRAAAELAAQLEELEEAEeallerlERLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                         250
                  ....*....|.
gi 1943700588 418 KSVVETKELEQ 428
Cdd:COG1196   470 EEAALLEAALA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
188-425 9.47e-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: 51.21  E-value: 9.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  188 RELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDLSAAEL 267
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  268 KIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNL--------------KKN 333
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLrerleslerriaatERR 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  334 IVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRERK-NEMLEKQTVEQEQTEE 412
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEE 919
                          250
                   ....*....|...
gi 1943700588  413 WAESKKSVVETKE 425
Cdd:TIGR02168  920 LREKLAQLELRLE 932
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
218-424 1.12e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.79  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 218 LKILASKLVKQTEKL-DIRNSLMKKQYKMTE--KQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEK 294
Cdd:TIGR04523 309 NKELKSELKNQEKKLeEIQNQISQNNKIISQlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 295 LALRAANL-------KKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKK 367
Cdd:TIGR04523 389 LESQINDLeskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943700588 368 QAEV-----------LEEQAEQLEIQNS---LLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETK 424
Cdd:TIGR04523 469 QLKVlsrsinkikqnLEQKQKELKSKEKelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
PTZ00121 PTZ00121
MAEBL; Provisional
244-434 2.20e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  244 KMTEKQAAElEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEM 323
Cdd:PTZ00121  1291 KADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  324 GLRAPNLKKNIVELEKQTKHVEnRKSVLKKQYENLASHASELKK------QAEVLEEQAEQLEIQNSLLKirNKHRERKN 397
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKaaaakkKADEAKKKAEEKKKADEAKK--KAEEAKKA 1446
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1943700588  398 EMLEKQTVEQEQTEEW---AESKKSVVETKELEQPSKEQD 434
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAkkkAEEAKKADEAKKKAEEAKKAD 1486
PTZ00121 PTZ00121
MAEBL; Provisional
211-434 2.37e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  211 LDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKwKSALKI 290
Cdd:PTZ00121  1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAKK 1398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  291 QYEKLALRAANLKKQVTElAKQTKEVENHYEEMGlRAPNLKKNIVELEK----QTKHVENRKSVLKKQYENLASHASELK 366
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAA-KKKADEAKKKAEEKK-KADEAKKKAEEAKKadeaKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943700588  367 KQAEV------LEEQAEqlEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEW--AESKKSVVETKELEQPSKEQD 434
Cdd:PTZ00121  1477 KKAEEakkadeAKKKAE--EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEKKKADE 1550
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
45-129 2.71e-06

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 45.90  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLCPCKNAWSSDIRWIQLRSSG----FVHHYRNGEDLEQmtEYKGRTELLRKGLSDGNLDLRITAVS 120
Cdd:cd05718     9 VTGFLGGSVTLPCSLTSPGTTKITQVTWMKIGAGSsqnvAVFHPQYGPSVPN--PYAERVEFLAARLGLRNATLRIRNLR 86

                  ....*....
gi 1943700588 121 SSDSGLYSC 129
Cdd:cd05718    87 VEDEGNYIC 95
PTZ00121 PTZ00121
MAEBL; Provisional
211-434 3.59e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  211 LDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLdKQTEELDKWKSALKI 290
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL-KKAEELKKAEEKKKA 1566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  291 QYEKLALRAANLKKQVTELAKQTKE------VENHYEEMGLRAPNLKKnivELEKQTKHVENRKSV-LKKQYENLASHAS 363
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEarieevMKLYEEEKKMKAEEAKK---AEEAKIKAEELKKAEeEKKKVEQLKKKEA 1643
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943700588  364 ELKKQAEVLEEQAEQLeiqnsllKIRNKHRERKNEMlEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:PTZ00121  1644 EEKKKAEELKKAEEEN-------KIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
181-401 4.77e-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: 48.91  E-value: 4.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  181 RKKVTQSRELKRK-DAMLGRKDAVLEELPAILDSSAANLKILASK---LVKQTEKLDIRNSLMKKQYKMTEKQAAELEKH 256
Cdd:TIGR02169  790 HSRIPEIQAELSKlEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  257 LINTDLSAAELKIAAAKLDKQTEELDKWKSA-------LKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEM------ 323
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRElerkieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipee 949
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943700588  324 GLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLeiqnsLLKIRNKHRERKNEMLE 401
Cdd:TIGR02169  950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI-----LERIEEYEKKKREVFME 1022
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
37-129 1.33e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.94  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  37 TVVAPSLRVTANVGQDVVLRCHlcpCKNAWSSDIRWiqlrssgfvhhYRNGEDLEQmteykgrTELLRKGLSDGNLDLRI 116
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCE---ATGSPPPTITW-----------YKNGEPISS-------GSTRSRSLSGSNSTLTI 61
                          90
                  ....*....|...
gi 1943700588 117 TAVSSSDSGLYSC 129
Cdd:pfam13927  62 SNVTRSDAGTYTC 74
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
39-147 1.46e-05

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 44.12  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  39 VAPSLRVTANVGQDVVLRCHLCPCKNAWSSD-----IRWIQLRSSG--------FVhhyRNGEDLEQMTEYKGRTELLRK 105
Cdd:cd05714     1 EAESAKVFSHLGGNVTLPCKFYRDPTAFGSGihkirIKWTKLTSDSgylkevdvLV---AMGNVVYHKKTYGGRVSVPLK 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1943700588 106 GLSDGNLDLRITAVSSSDSGLYSCAVQDG--DDgyaEALVELEV 147
Cdd:cd05714    78 PGSDSDASLVITDLTASDYGLYRCEVIEGieDD---QDVVALDV 118
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
240-434 2.27e-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: 46.30  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 240 KKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENH 319
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 320 YEEMgLRAPNLKKNIVELE-----KQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRE 394
Cdd:COG4942   106 LAEL-LRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1943700588 395 RKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:COG4942   185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
224-427 2.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 224 KLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINT--DLSAA--------ELKIAAAKLDKQTEELDKWKSALKIQYE 293
Cdd:PRK03918  183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELreELEKLekevkeleELKEEIEELEKELESLEGSKRKLEEKIR 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 294 KLALRAANLKKQVTELAKQTKEVEN------HYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKK 367
Cdd:PRK03918  263 ELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 368 QAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELE 427
Cdd:PRK03918  343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
164-380 2.75e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 164 VIVTILVGSFVIIAFLYRKKVTQsRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRN---SLMK 240
Cdd:COG4942     4 LLLLALLLALAAAAQADAAAEAE-AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEqelAALE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 241 KQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQT-----------EELDKWKSALKIQYEKLALRAANLKKQVTEL 309
Cdd:COG4942    83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943700588 310 AKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLE 380
Cdd:COG4942   163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
38-138 3.68e-05

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 42.71  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  38 VVAPSLRVTANVGQDVVLRCHLcpcKNAWSSD-IRWI-QLRSSGFVH-HYRNGEDLEQMTEYKGRTELLRKGLSDGNLdl 114
Cdd:cd00099     1 VTQSPRSLSVQEGESVTLSCEV---SSSFSSTyIYWYrQKPGQGPEFlIYLSSSKGKTKGGVPGRFSGSRDGTSSFSL-- 75
                          90       100
                  ....*....|....*....|....
gi 1943700588 115 RITAVSSSDSGLYSCAVQDGDDGY 138
Cdd:cd00099    76 TISNLQPEDSGTYYCAVSESGGTD 99
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
52-147 6.64e-05

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 42.13  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  52 DVVLRCHLCPCKNAWSSDIRWIQLRSSGFVHHY-RNGE-DLEQMTEYKGRTELLRKglSDGNLDLRITAVSSSDSGLYSC 129
Cdd:cd16089    16 SVNLPCTYVPEEGYTQVLVKWLVQRDSDPVTIFlRDSSgDHIQQAKYRGRLEVSKD--TPGDVSLQLDTLEMDDRGHYTC 93
                          90       100
                  ....*....|....*....|..
gi 1943700588 130 AV----QDGDDGYAEALVELEV 147
Cdd:cd16089    94 QVtwqtPDGNLIVREKTTELRV 115
PTZ00121 PTZ00121
MAEBL; Provisional
241-434 7.30e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 7.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  241 KQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQT----EELDKWKSALKIQYEKLA--LRAANLKKQVTELAKQTK 314
Cdd:PTZ00121  1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAE 1312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  315 EVENHyEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHA--------------SELKKQAEVLEEQAEQLE 380
Cdd:PTZ00121  1313 EAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaekkkEEAKKKADAAKKKAEEKK 1391
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1943700588  381 IQNSLLKiRNKHRERKNEMLEKQTVEQEQTEEW---AESKKSVVETKELEQPSKEQD 434
Cdd:PTZ00121  1392 KADEAKK-KAEEDKKKADELKKAAAAKKKADEAkkkAEEKKKADEAKKKAEEAKKAD 1447
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
189-433 7.86e-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: 45.10  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 189 ELKRKDAMLGRKDAVL------EELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDL 262
Cdd:pfam05483 406 ELEELKKILAEDEKLLdekkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 263 SAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENhyEEMGLR---------------- 326
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE--KEMNLRdelesvreefiqkgde 563
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 327 -----------APNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRER 395
Cdd:pfam05483 564 vkckldkseenARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLEL 643
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1943700588 396 KNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKEQ 433
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
227-434 8.00e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 227 KQTEKLDIRNSLMKKQYKMT--EKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKK 304
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEklKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 305 QVTELAKQTKEVENH-------YEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAE 377
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1943700588 378 QLEIQNSLLKirNKHRERKNEMLEKQTvEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:TIGR04523 514 DLTKKISSLK--EKIEKLESEKKEKES-KISDLEDELNKDDFELKKENLEKEIDEKN 567
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
80-138 1.12e-04

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 41.46  E-value: 1.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  80 FVHhyrNGEDLE-QMTEYKGRTELLRKGLSDGNLDLRITAVSSSDSGLYSCAVQDGDDGY 138
Cdd:cd20947    47 FVH---GEEDLKvQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADY 103
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
199-428 1.42e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  199 RKDAVLEELPAILDSSAANLKILASKLvKQTEKLDI-RNSLMKKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQ 277
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKR-QQLERLRReREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  278 TEELDKwksaLKIQYEKLALRAANLKKQVTELAKQTK--------EVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKS 349
Cdd:TIGR02169  250 EEELEK----LTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943700588  350 VLKKQYENLASHASELKKQaevLEEQAEQLEiqnsllKIRNKHRERKNEMLEKQtveQEQTEEWAESKKSVVETKELEQ 428
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELERE---IEEERKRRD------KLTEEYAELKEELEDLR---AELEEVDKEFAETRDELKDYRE 392
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
218-389 1.76e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 218 LKILASKLVKQTEKLDIRNSLMKKQYKMTEKQA-AELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLA 296
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEeLEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 297 LRAANLKKQVTELAKQTKEVENH----YEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVL 372
Cdd:COG4717   153 ERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
                         170
                  ....*....|....*..
gi 1943700588 373 EEQAEQLEIQNSLLKIR 389
Cdd:COG4717   233 ENELEAAALEERLKEAR 249
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
44-147 2.21e-04

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 40.77  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  44 RVTANVGQDVVLRCHLcPCKNAWSSD----IRWIQLRSSGFV---------HHYRngedleQMTEYKGRTELLRKGlsDG 110
Cdd:cd05877     6 KVFSHRGGNVTLPCRY-HYEPELSAPrkirVKWTKLEVDYAKeedvlvaigTRHK------SYGSYQGRVFLRRAD--DL 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1943700588 111 NLDLRITAVSSSDSGLYSCAVQDG--DDgyaEALVELEV 147
Cdd:cd05877    77 DASLVITDLRLEDYGRYRCEVIDGleDE---SVVVALRL 112
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
39-134 2.55e-04

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 40.71  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  39 VAPSLRVTANVGQDVVLRCH------LCPCKNAWSS--DIRWIQLRSSgfvhhyRNGEDLEQMT-------------EYK 97
Cdd:cd05901     1 VRKSSRVHGSLSGSVVLPCRfstlptLPPSYNITSEflRIKWTKIQVD------KNGKDHKETTvlvaqngiikigqEYM 74
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1943700588  98 GRTELLRKGLSDGNLDLRITAVSSSDSGLYSCAVQDG 134
Cdd:cd05901    75 GRVSVPSHPEDQGDASLTIVKLRASDAGVYRCEVMHG 111
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
53-143 2.64e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 39.23  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  53 VVLRCHLcpcKNAWSSDIRWiqlrssgfvhhYRNGEDLEQMTEYKGRTEllrkglsDGNLDLRITAVSSSDSGLYSCAVQ 132
Cdd:cd00096     1 VTLTCSA---SGNPPPTITW-----------YKNGKPLPPSSRDSRRSE-------LGNGTLTISNVTLEDSGTYTCVAS 59
                          90
                  ....*....|.
gi 1943700588 133 DGDDGYAEALV 143
Cdd:cd00096    60 NSAGGSASASV 70
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
244-412 2.64e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.07  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 244 KMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEM 323
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPA 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 324 GLRAPNLKKNIV-----ELEKQTKHVENRKSVLKKQYEnlaSHASELKKQAEVLEEQAEQ--LEIQNSLLKIRNKHRERK 396
Cdd:pfam05262 265 DTSSPKEDKQVAenqkrEIEKAQIEIKKNDEEALKAKD---HKAFDLKQESKASEKEAEDkeLEAQKKREPVAEDLQKTK 341
                         170
                  ....*....|....*.
gi 1943700588 397 NEMLEKQTVEQEQTEE 412
Cdd:pfam05262 342 PQVEAQPTSLNEDAID 357
IGv smart00406
Immunoglobulin V-Type;
61-131 3.03e-04

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 39.29  E-value: 3.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1943700588   61 PCKnAWSSD-----IRWIQ--LRSSGFVHHYRNGEDLEQ-MTEYKGRTELLRKgLSDGNLDLRITAVSSSDSGLYSCAV 131
Cdd:smart00406   5 SCK-FSGSTfssyyVSWVRqpPGKGLEWLGYIGSNGSSYyQESYKGRFTISKD-TSKNDVSLTISNLRVEDTGTYYCAV 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
209-415 6.04e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 209 AILDSSAANLKILASKLVKQTEKLDIRNS----LMKKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKW 284
Cdd:COG4717    42 FIRAMLLERLEKEADELFKPQGRKPELNLkelkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 285 KSAlkIQYEKLALRAANLKKQVTELAKQTKEVENH---YEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQyenlasH 361
Cdd:COG4717   122 EKL--LQLLPLYQELEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEE------E 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1943700588 362 ASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAE 415
Cdd:COG4717   194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
189-427 6.89e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.34  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  189 ELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKhlINTDLSAAELK 268
Cdd:TIGR00606  710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT--IMPEEESAKVC 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  269 IA----AAKLDKQTEELDKwksalKIQYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRAPNLKKNIVELEKQTKHV 344
Cdd:TIGR00606  788 LTdvtiMERFQMELKDVER-----KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  345 ENRKSVLKKQYENLASHAselkKQAEVLEEQAEQL--EIQNSLLKIRNKhreRKNEMLEKQTVEQEQTEEWAESKKSVVE 422
Cdd:TIGR00606  863 KSKTNELKSEKLQIGTNL----QRRQQFEEQLVELstEVQSLIREIKDA---KEQDSPLETFLEKDQQEKEELISSKETS 935

                   ....*
gi 1943700588  423 TKELE 427
Cdd:TIGR00606  936 NKKAQ 940
46 PHA02562
endonuclease subunit; Provisional
229-432 7.85e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 229 TEKLDIRNSLMKKQYKMTEKQAAELEKhlINTDLSAAELKIAAAKLDKQTE------ELDKWKSALKiqyeKLALRAANL 302
Cdd:PHA02562  194 QQQIKTYNKNIEEQRKKNGENIARKQN--KYDELVEEAKTIKAEIEELTDEllnlvmDIEDPSAALN----KLNTAAAKI 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 303 KKQVTELAKqtkeVENHYEEMGLrAPNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQA-EVLEEQAEQLEI 381
Cdd:PHA02562  268 KSKIEQFQK----VIKMYEKGGV-CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdEFNEQSKKLLEL 342
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1943700588 382 QNsllKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPSKE 432
Cdd:PHA02562  343 KN---KISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
187-433 1.23e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 187 SRELKRKDAMLGRKDAVLEELPAILDSSAANLKiLASKLVKQTEKLD----IRNSLMKKQYKMTEKQAAELEKHLINTDL 262
Cdd:PRK03918  458 TAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEqlkeLEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 263 SAAELKIAAAKLdKQTEELDKWKSALKIQYEKLALRAANLKKQ--------VTELAKQTKEVENHYEEMgLRAPNLKKni 334
Cdd:PRK03918  537 LKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNEY-LELKDAEK-- 612
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 335 vELEKQTKHVENRKSVLKKQYENLAshasELKKQAEVLEEQAEQLEIQNSllkiRNKHRERKNEMLEKQTVEQEQTEEWA 414
Cdd:PRK03918  613 -ELEREEKELKKLEEELDKAFEELA----ETEKRLEELRKELEELEKKYS----EEEYEELREEYLELSRELAGLRAELE 683
                         250
                  ....*....|....*....
gi 1943700588 415 ESKKSVVETKELEQPSKEQ 433
Cdd:PRK03918  684 ELEKRREEIKKTLEKLKEE 702
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
176-376 1.26e-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: 40.90  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 176 IAFLYRKKVTQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQ----YKMTE---- 247
Cdd:COG4942    43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralYRLGRqppl 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 248 ------KQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVEnhye 321
Cdd:COG4942   123 alllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ---- 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1943700588 322 emglrapnlkKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQA 376
Cdd:COG4942   199 ----------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
181-402 1.28e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 181 RKKVTQSRELKRK-DAMLGRKDAVLE---ELPAILDSSAANLKILASKLVKQTEKLDIRNsLMKKQYKMTEKQAAELEKH 256
Cdd:COG1340    46 DELNAQVKELREEaQELREKRDELNEkvkELKEERDELNEKLNELREELDELRKELAELN-KAGGSIDKLRKEIERLEWR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 257 LINTDLSAAELKIAAAKLDKQTEELDKWKSALKI---------QYEKLALRAANLKKQVTELAKQTKEVENHYEEMGLRA 327
Cdd:COG1340   125 QQTEVLSPEEEKELVEKIKELEKELEKAKKALEKneklkelraELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943700588 328 PNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQnsllKIRNKHRERKNEMLEK 402
Cdd:COG1340   205 DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE----KEKEELEEKAEEIFEK 275
I-set pfam07679
Immunoglobulin I-set domain;
44-147 1.29e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 37.62  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  44 RVTANVGQDVVLRCHL--CPcknawSSDIRWiqlrssgfvhhYRNGEDLEQMTEYKGRTEllrkglsDGNLDLRITAVSS 121
Cdd:pfam07679   9 DVEVQEGESARFTCTVtgTP-----DPEVSW-----------FKDGQPLRSSDRFKVTYE-------GGTYTLTISNVQP 65
                          90       100
                  ....*....|....*....|....*.
gi 1943700588 122 SDSGLYSCAVQDGdDGYAEALVELEV 147
Cdd:pfam07679  66 DDSGKYTCVATNS-AGEAEASAELTV 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
255-433 1.43e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 255 KHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKEVENhyeemglrapnLKKNI 334
Cdd:COG4372    21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-----------LNEQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 335 VELEKQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWA 414
Cdd:COG4372    90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
                         170
                  ....*....|....*....
gi 1943700588 415 ESKKSVVETKELEQPSKEQ 433
Cdd:COG4372   170 EQELQALSEAEAEQALDEL 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
186-380 1.49e-03

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: 41.20  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  186 QSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDirnslmkKQYKMTEKQAAELEKHLINTDLSAA 265
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL-------NERASLEEALALLRSELEELSEELR 904
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  266 ELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTKE-VENHYEEMGLRAPNLKKNIVELEKQTKHV 344
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKEL 984
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1943700588  345 ENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLE 380
Cdd:TIGR02168  985 GPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
PRK12704 PRK12704
phosphodiesterase; Provisional
288-433 1.53e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 288 LKIQYEKLALRAANLKKQVTELAKqtKEVENHYEEMGLRApnlKKNIVELEKQT-KHVENRKSVLKKQYENLASHASELK 366
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAK--KEAEAIKKEALLEA---KEEIHKLRNEFeKELRERRNELQKLEKRLLQKEENLD 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943700588 367 KQAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQ--------TEEwaESKKSVVEtkELEQPSKEQ 433
Cdd:PRK12704  100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelerisglTAE--EAKEILLE--KVEEEARHE 170
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
38-138 1.75e-03

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 38.02  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  38 VVAPSLRVTANVGQDVVLRCHLcpcKNAWSSDIRWI-QLRSSGFVHHYRNGedLEQMTEYKGRTEL-LRKglSDGNLDLR 115
Cdd:cd04983     1 VTQSPQSLSVQEGENVTLNCNY---STSTFYYLFWYrQYPGQGPQFLIYIS--SDSGNKKKGRFSAtLDK--SRKSSSLH 73
                          90       100
                  ....*....|....*....|...
gi 1943700588 116 ITAVSSSDSGLYSCAVQDGDDGY 138
Cdd:cd04983    74 ISAAQLSDSAVYFCALSESGGTG 96
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
251-430 1.96e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 251 AELEKHLINTDLSAAELKIAA--AKLDKQTEELDkwksALKIQYEKLALRAANLKKQV----TELAKQTKEVENHYEEMG 324
Cdd:COG3883    14 ADPQIQAKQKELSELQAELEAaqAELDALQAELE----ELNEEYNELQAELEALQAEIdklqAEIAEAEAEIEERREELG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 325 LRAPNLKKN------------------------------------IVELEKQTKHVENRKSVLKKQYENLASHASELK-K 367
Cdd:COG3883    90 ERARALYRSggsvsyldvllgsesfsdfldrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEaA 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943700588 368 QAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEKQTVEQEQTEEWAESKKSVVETKELEQPS 430
Cdd:COG3883   170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
PRK12704 PRK12704
phosphodiesterase; Provisional
234-398 2.10e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 234 IRNSLMKKQYKMTEKQAAELekhlintdLSAAELKIAAAKLDKQTEELDKWKSaLKIQYEK-LALRAANLKKQVTELAKQ 312
Cdd:PRK12704   24 VRKKIAEAKIKEAEEEAKRI--------LEEAKKEAEAIKKEALLEAKEEIHK-LRNEFEKeLRERRNELQKLEKRLLQK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 313 TKEVENHYEEMGLRAPNLKKNIVELEKQTKHVENRKSVLKKQY-------ENLASHASELKKQaEVLEEQAEQLEIQNSL 385
Cdd:PRK12704   95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKE-ILLEKVEEEARHEAAV 173
                         170
                  ....*....|...
gi 1943700588 386 LkIRNKHRERKNE 398
Cdd:PRK12704  174 L-IKEIEEEAKEE 185
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
265-415 2.62e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 39.71  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 265 AELKIAAAKLDKQTEEL-DKWKSALK-----IQYEKLALrAANLKKQVTELAKqtKEVENHYEEMGLRAPNLKKNIVELE 338
Cdd:COG4026    58 ADLVLIATDADRVGRELaEKFFEELKgmvghVERMKLPL-GHDVEYVDVELVR--KEIKNAIIRAGLKSLQNIPEYNELR 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 339 KQTKHVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLK-----IRNKH---RERKNEMLEKQTVEQEQT 410
Cdd:COG4026   135 EELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEeefdnIKSEYsdlKSRFEELLKKRLLEVFSL 214

                  ....*.
gi 1943700588 411 EE-WAE 415
Cdd:COG4026   215 EElWKE 220
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
247-402 2.70e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 247 EKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTElAKQTKEVENHYEEMGlr 326
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEYEALQKEIE-- 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943700588 327 apNLKKNIVELEKQTKHVENRKSVLKKQYENLASHASELKKQAEvlEEQAEQLEIQNSLLKIRNKHRERKNEMLEK 402
Cdd:COG1579   100 --SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE--EKKAELDEELAELEAELEELEAEREELAAK 171
IgV_TCR_delta cd07706
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here ...
45-136 2.74e-03

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409503  Cd Length: 112  Bit Score: 37.50  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLrchLCPCKNAWSS-DIRWIQLRSSGFVHHYRNGEDLEQmTEYKGRTELLRKgLSDGNLDLRITAVSSSD 123
Cdd:cd07706     9 VSVQVGEEVTL---NCRYETSWTNyYLFWYKQLPSGEMTFLIRQDSSEQ-NAKSGRYSVNFQ-KAQKSISLTISALQLED 83
                          90
                  ....*....|...
gi 1943700588 124 SGLYSCAVQDGDD 136
Cdd:cd07706    84 SAKYFCALSLPYD 96
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
223-396 2.75e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.99  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 223 SKLVKQTEKLDIRNSLMKKQYKMTEKQAAELEKHLINTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANL 302
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 303 KKQVTElaKQTKEVENHYEEMglrapnlKKNIVELEKQTKHVENRksvLKKQyenlaSHASELKKQAEVLEEQAEQLEIQ 382
Cdd:pfam05262 272 DKQVAE--NQKREIEKAQIEI-------KKNDEEALKAKDHKAFD---LKQE-----SKASEKEAEDKELEAQKKREPVA 334
                         170
                  ....*....|....
gi 1943700588 383 NSLLKIRNKHRERK 396
Cdd:pfam05262 335 EDLQKTKPQVEAQP 348
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
45-146 3.91e-03

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 36.61  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLcPCKNAWSSdIRWIQLRSsgfvhhyrNGEDLEQMTEYKGRTE--LLRKGLSDGNLDLRITAVSSS 122
Cdd:cd05716     7 VTGVEGGSVTIQCPY-PPKYASSR-KYWCKWGS--------EGCQTLVSSEGVVPGGriSLTDDPDNGVFTVTLNQLRKE 76
                          90       100
                  ....*....|....*....|....
gi 1943700588 123 DSGLYSCAVQDGDDGYAEALVELE 146
Cdd:cd05716    77 DAGWYWCGVGDDGDRGLTVQVKLV 100
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
188-402 5.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 188 RELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMKKQYKmtekqaaeleKHLintdlsaaEL 267
Cdd:PRK03918  546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN----------EYL--------EL 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 268 KIAAAKLDKQTEELDKWKSALKIQYEKLALraanLKKQVTELAKQTKEVENHYEEMGLRapnlkknivELEKQTKHVENR 347
Cdd:PRK03918  608 KDAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYE---------ELREEYLELSRE 674
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1943700588 348 KSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRNKHRERKNEMLEK 402
Cdd:PRK03918  675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
245-420 5.68e-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: 38.37  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 245 MTEKQAAELEkhLINTDLSAAELKIAAAKLDKQTEELDKwksalkiQYEKLALRAANLKKQVTELAKQTKEVENHYEEmg 324
Cdd:COG1579     2 MPEDLRALLD--LQELDSELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEE-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 325 lrapnLKKNIVELEKQTKHVENRKSV---------LKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLK--IRNKHR 393
Cdd:COG1579    71 -----VEARIKKYEEQLGNVRNNKEYealqkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEaeLEEKKA 145
                         170       180
                  ....*....|....*....|....*..
gi 1943700588 394 ERKNEMLEKQTVEQEQTEEWAESKKSV 420
Cdd:COG1579   146 ELDEELAELEAELEELEAEREELAAKI 172
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
238-409 6.44e-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: 38.46  E-value: 6.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  238 LMKKQYKMTeKQAAELE----------KHLIN----TDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLK 303
Cdd:smart00787 114 LMDKQFQLV-KTFARLEakkmwyewrmKLLEGlkegLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  304 KQVTELAKQTkevenhyeemglraPNLKKNIVE-LEKQTKHVENRKSVLKKQYENLASHASEL-KKQAEVLEEQAEQLEI 381
Cdd:smart00787 193 QLEDELEDCD--------------PTELDRAKEkLKKLLQEIMIKVKKLEELEEELQELESKIeDLTNKKSELNTEIAEA 258
                          170       180
                   ....*....|....*....|....*...
gi 1943700588  382 QNSLLKirNKHRERKNEMLEKQTVEQEQ 409
Cdd:smart00787 259 EKKLEQ--CRGFTFKEIEKLKEQLKLLQ 284
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
45-147 6.76e-03

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 35.98  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  45 VTANVGQDVVLRCHLCpcKNAWSSDIRWIQL-RSSGFVHHYRNgedlEQMTEYKGRTELLRKGLsdgnldlRITAVSSSD 123
Cdd:cd20946     9 VTVVENQEVILSCKTP--KKTSSPRVEWKKLqRDVTFVVFQNN----KIQGDYKGRAEILGTNI-------TIKNVTRSD 75
                          90       100
                  ....*....|....*....|....*.
gi 1943700588 124 SGLYSCAVQDGDDG--YAEALVELEV 147
Cdd:cd20946    76 SGKYRCEVSARSDGqnLGEVTVTLEV 101
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
188-382 7.00e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 188 RELKRKDAMlgrKDAVLEELPAILDSSAANLKILASKLVKQTEKLDIRNSLMK---KQYKMTEKQAAELEKHLINTDLSA 264
Cdd:TIGR04523 443 KDLTNQDSV---KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKskeKELKKLNEEKKELEEKVKDLTKKI 519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 265 AELKIAAAKLDKQTEELDKWKSALKIQYEKL--ALRAANLKKQVTELAKQTKEVENHYEemglrapNLKKNIVELEKQTK 342
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKQTQK-------SLKKKQEEKQELID 592
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1943700588 343 HVENRKSVLKKQYENLASHASELKKQAEVLEEQAEQLEIQ 382
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
247-433 7.51e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 247 EKQAAELEK-HLINTDLSAAELKIAAAKLDKQTEELDKW------KSALKIQYEKLALRAANLKKQVTELAKQtKEVENH 319
Cdd:COG4717    52 EKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYaelqeeLEELEEELEELEAELEELREELEKLEKL-LQLLPL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588 320 YEEMGlrapNLKKNIVELEKQTKHVENRksvlKKQYENLASHASELKKQAEVLEEQAEQLEIQNSLLKIRN-KHRERKNE 398
Cdd:COG4717   131 YQELE----ALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELE 202
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1943700588 399 MLEKQTVEQEQTEEWAESKKSVVEtKELEQPSKEQ 433
Cdd:COG4717   203 ELQQRLAELEEELEEAQEELEELE-EELEQLENEL 236
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
185-434 9.13e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 9.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  185 TQSRELKRKDAMLGRKDAVLEELPAILDSSAANLKILASKL-----VKQTEKLDIRNSLM-KKQYKMTEKQAAELEKHLI 258
Cdd:pfam12128  615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdEKQSEKDKKNKALAeRKDSANERLNSLEAQLKQL 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  259 NTDLSAAELKIAAAKLDKQTEELDKWKSALKIQYEKLALRAANLKKQVTELAKQTK--EVENHYEEMGL-----RAPNLK 331
Cdd:pfam12128  695 DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKalETWYKRDLASLgvdpdVIAKLK 774
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943700588  332 KNIVELEKQTKHVENRKSVLKK----QYENLASHASELKKQAEVLEEQAEQLEIQ----NSLLKIRNKHRERKNEMLEKQ 403
Cdd:pfam12128  775 REIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQlarlIADTKLRRAKLEMERKASEKQ 854
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1943700588  404 TVEQEQTEEWAESKKSVVETKELEQPSKEQD 434
Cdd:pfam12128  855 QVRLSENLRGLRCEMSKLATLKEDANSEQAQ 885
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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